ID MPRI_HUMAN Reviewed; 2491 AA. AC P11717; Q7Z7G9; Q96PT5; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 02-SEP-2026, entry version 252. DE RecName: Full=Cation-independent mannose-6-phosphate receptor; DE Short=CI Man-6-P receptor; DE Short=CI-MPR; DE Short=M6PR; DE AltName: Full=300 kDa mannose 6-phosphate receptor; DE Short=MPR 300; DE AltName: Full=Insulin-like growth factor 2 receptor; DE AltName: Full=Insulin-like growth factor II receptor; DE Short=IGF-II receptor; DE AltName: Full=M6P/IGF2 receptor; DE Short=M6P/IGF2R; DE AltName: CD_antigen=CD222; DE Flags: Precursor; GN Name=IGF2R; Synonyms=MPRI; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT GLY-1619, RP CLEAVAGE OF SIGNAL PEPTIDE AFTER CYS-23, AND TOPOLOGY. RX PubMed=2957598; DOI=10.1038/329301a0; RA Morgan D.O., Edman J.C., Standring D.N., Fried V.A., Smith M.C., Roth R.A., RA Rutter W.J.; RT "Insulin-like growth factor II receptor as a multifunctional binding RT protein."; RL Nature 329:301-307(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-1619, AND FUNCTION. RX PubMed=2963003; DOI=10.1016/s0021-9258(18)69243-9; RA Oshima A., Nolan C.M., Kyle J.W., Grubb J.H., Sly W.S.; RT "The human cation-independent mannose 6-phosphate receptor. Cloning and RT sequence of the full-length cDNA and expression of functional receptor in RT COS cells."; RL J. Biol. Chem. 263:2553-2562(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-1619. RA Gemma A., Seike Y., Uematsu K., Seike M., Bennett W.P., Harris C.C., RA Kudoh S.; RT "The genomic structure of the gene encoding the human mannose 6 RT phosphate/insulin-like growth factor 2 receptor (M6P/IGF2R)."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9892739; DOI=10.1007/s003359900947; RA Killian J.K., Jirtle R.L.; RT "Genomic structure of the human M6P/IGF2 receptor."; RL Mamm. Genome 10:74-77(1999). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-91; LEU-203; ASP-231; RP VAL-252; GLY-273; GLN-512; SER-604; THR-724; VAL-817; SER-856; MET-1107; RP ILE-1124; SER-1184; GLU-1315; HIS-1335; GLY-1619; HIS-1832; ASP-1860; RP MET-1908; SER-2020 AND VAL-2459. RG NIEHS SNPs program; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [7] RP FUNCTION, INTERACTION WITH DPP4, AND SUBCELLULAR LOCATION. RX PubMed=10900005; DOI=10.1073/pnas.97.15.8439; RA Ikushima H., Munakata Y., Ishii T., Iwata S., Terashima M., Tanaka H., RA Schlossman S.F., Morimoto C.; RT "Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor RT II receptor contributes to T cell activation."; RL Proc. Natl. Acad. Sci. U.S.A. 97:8439-8444(2000). RN [8] RP INTERACTION WITH GGA1; GGA2 AND GGA3. RX PubMed=11387475; DOI=10.1126/science.1060750; RA Puertollano R., Aguilar R.C., Gorshkova I., Crouch R.J., Bonifacino J.S.; RT "Sorting of mannose 6-phosphate receptors mediated by the GGAs."; RL Science 292:1712-1716(2001). RN [9] RP GLYCOSYLATION AT ASN-112; ASN-581; ASN-747 AND ASN-1246. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Prostate cancer; RX PubMed=17487921; DOI=10.1002/elps.200600782; RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; RT "Toward a global characterization of the phosphoproteome in prostate cancer RT cells: identification of phosphoproteins in the LNCaP cell line."; RL Electrophoresis 28:2027-2034(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [17] RP FUNCTION, INTERACTION WITH THE RETROMER COMPLEX, SUBCELLULAR LOCATION, AND RP PALMITOYLATION. RX PubMed=18817523; DOI=10.1111/j.1600-0854.2008.00814.x; RA McCormick P.J., Dumaresq-Doiron K., Pluviose A.S., Pichette V., Tosato G., RA Lefrancois S.; RT "Palmitoylation controls recycling in lysosomal sorting and trafficking."; RL Traffic 9:1984-1997(2008). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [19] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-626 AND ASN-747. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2352, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409 AND SER-2484, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [29] RP INTERACTION WITH SNX32. RX PubMed=37158588; DOI=10.7554/elife.84396; RA Sugatha J., Priya A., Raj P., Jaimon E., Swaminathan U., Jose A., RA Pucadyil T.J., Datta S.; RT "Insights into cargo sorting by SNX32 and its role in neurite outgrowth."; RL Elife 12:0-0(2023). RN [30] RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 1508-2128 ALONE AND IN COMPLEX RP WITH IGF2, DISULFIDE BONDS, AND FUNCTION. RX PubMed=18046459; DOI=10.1038/sj.emboj.7601938; RA Brown J., Delaine C., Zaccheo O.J., Siebold C., Gilbert R.J., van Boxel G., RA Denley A., Wallace J.C., Hassan A.B., Forbes B.E., Jones E.Y.; RT "Structure and functional analysis of the IGF-II/IGF2R interaction."; RL EMBO J. 27:265-276(2008). CC -!- FUNCTION: Mediates the transport of phosphorylated lysosomal enzymes CC from the Golgi complex and the cell surface to lysosomes CC (PubMed:18817523, PubMed:2963003). Lysosomal enzymes bearing CC phosphomannosyl residues bind specifically to mannose-6-phosphate CC receptors in the Golgi apparatus and the resulting receptor-ligand CC complex is transported to an acidic prelysosomal compartment where the CC low pH mediates the dissociation of the complex (PubMed:18817523, CC PubMed:2963003). The receptor is then recycled back to the Golgi for CC another round of trafficking through its binding to the retromer CC (PubMed:18817523). This receptor also binds IGF2 (PubMed:18046459). CC Acts as a positive regulator of T-cell coactivation by binding DPP4 CC (PubMed:10900005). {ECO:0000269|PubMed:10900005, CC ECO:0000269|PubMed:18046459, ECO:0000269|PubMed:18817523, CC ECO:0000269|PubMed:2963003}. CC -!- SUBUNIT: Binds HA-I and HA-II plasma membrane adapters (By similarity). CC Interacts with DPP4; the interaction is direct. Binds GGA1, GGA2 and CC GGA3. Interacts with the heterotrimeric retromer cargo-selective CC complex (CSC), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35; CC which is involved in retrograde trafficking of the receptor from CC endosomes to the Golgi apparatus (Probable). Interacts with SNX32; the CC interaction is involved in intracellular trafficking of the receptor CC (PubMed:37158588). {ECO:0000250, ECO:0000269|PubMed:10900005, CC ECO:0000269|PubMed:11387475, ECO:0000269|PubMed:18046459, CC ECO:0000269|PubMed:37158588, ECO:0000305|PubMed:18817523}. CC -!- INTERACTION: CC P11717; Q9UJY5: GGA1; NbExp=9; IntAct=EBI-1048580, EBI-447141; CC P11717; Q9NZ52: GGA3; NbExp=8; IntAct=EBI-1048580, EBI-447404; CC P11717; P01344: IGF2; NbExp=17; IntAct=EBI-1048580, EBI-7178764; CC P11717; P01344-1: IGF2; NbExp=2; IntAct=EBI-1048580, EBI-15658078; CC P11717; P11717: IGF2R; NbExp=4; IntAct=EBI-1048580, EBI-1048580; CC P11717; Q6VY07: PACS1; NbExp=2; IntAct=EBI-1048580, EBI-2555014; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:18817523}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:2957598}. Endosome membrane CC {ECO:0000269|PubMed:18817523}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:2957598}. Note=Mainly localized in the Golgi at CC steady state and not detectable in lysosome (PubMed:18817523). CC Colocalized with DPP4 in internalized cytoplasmic vesicles adjacent to CC the cell surface (PubMed:10900005). {ECO:0000269|PubMed:10900005, CC ECO:0000269|PubMed:18817523}. CC -!- DOMAIN: Contains 15 repeating units of approximately 147 AA harboring CC four disulfide bonds each. The most highly conserved region within the CC repeat consists of a stretch of 13 AA that contains cysteines at both CC ends. CC -!- PTM: Palmitoylated (PubMed:18817523). Undergoes cysteine S- CC palmitoylation which promotes interaction with the retromer cargo- CC selective complex which mediates its retrograde trafficking to the CC Golgi apparatus (PubMed:18817523). {ECO:0000269|PubMed:18817523}. CC -!- SIMILARITY: Belongs to the MRL1/IGF2R family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/380/IGF2R"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y00285; CAA68395.1; -; mRNA. DR EMBL; J03528; AAA59866.1; -; mRNA. DR EMBL; AF109291; AAF16870.1; -; Genomic_DNA. DR EMBL; AF109244; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109245; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109246; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109247; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109248; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109249; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109250; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109251; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109252; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109253; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109254; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109255; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109256; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109257; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109258; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109259; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109260; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109261; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109262; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109263; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109264; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109265; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109266; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109267; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109268; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109269; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109270; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109271; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109272; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109273; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109274; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109275; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109276; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109277; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109278; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109279; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109280; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109281; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109282; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109283; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109284; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109285; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109286; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109287; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109288; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109289; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF109290; AAF16870.1; JOINED; Genomic_DNA. DR EMBL; AF069333; AAL04402.1; -; Genomic_DNA. DR EMBL; AY293855; AAP37954.1; -; Genomic_DNA. DR EMBL; AL353625; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL035691; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS5273.1; -. DR PIR; A28372; A28372. DR RefSeq; NP_000867.3; NM_000876.4. DR PDB; 1E6F; X-ray; 1.75 A; A/B=1508-1650. DR PDB; 1GP0; X-ray; 1.40 A; A=1508-1650. DR PDB; 1GP3; X-ray; 1.95 A; A=1508-1650. DR PDB; 1GQB; X-ray; 1.80 A; A/B=1508-1650. DR PDB; 1JPL; X-ray; 2.40 A; E/F/G/H=2480-2491. DR PDB; 1JWG; X-ray; 2.00 A; C/D=2479-2491. DR PDB; 1LF8; X-ray; 2.30 A; E/F/G/H=2480-2491. DR PDB; 2CNJ; NMR; -; D=1508-1651. DR PDB; 2L29; NMR; -; A=1508-1647. DR PDB; 2L2A; NMR; -; A=1508-1647. DR PDB; 2M68; NMR; -; A=1508-1649. DR PDB; 2M6T; NMR; -; A=1508-1649. DR PDB; 2V5N; X-ray; 3.20 A; A=1508-1800. DR PDB; 2V5O; X-ray; 2.91 A; A=1508-2128. DR PDB; 2V5P; X-ray; 4.10 A; A/B=1508-1993. DR PDB; 5IEI; X-ray; 2.80 A; A=1508-1649. DR PDB; 6N5X; X-ray; 2.05 A; A=2347-2377. DR PDB; 6N5Y; X-ray; 2.26 A; A=2347-2377. DR PDB; 6P8I; X-ray; 2.54 A; A=36-763. DR PDB; 6V02; X-ray; 2.46 A; A=43-763. DR PDB; 6Z30; X-ray; 1.50 A; A=1222-1510. DR PDB; 6Z31; X-ray; 2.56 A; A/B=1082-1220. DR PDB; 6Z32; X-ray; 3.47 A; A/B=927-1649. DR PDB; 8AFZ; EM; 10.00 A; C=2347-2377. DR AlphaFoldDB; P11717; -. DR EMDB; EMD-15413; -. DR MDRepo; P11717; -. DR SASBDB; P11717; -. DR SMR; P11717; -. DR BioGRID; 109703; 441. DR CORUM; P11717; -. DR DIP; DIP-6027N; -. DR ELM; P11717; -. DR FunCoup; P11717; 1582. DR IntAct; P11717; 179. DR MINT; P11717; -. DR NDEx; IQUERY-CP-IGF2R; 6 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000349437; -. DR BindingDB; P11717; -. DR ChEMBL; CHEMBL3240; -. DR DrugBank; DB01272; Alglucosidase alfa. DR DrugBank; DB02900; alpha-D-mannose 6-phosphate. DR DrugBank; DB16099; Avalglucosidase alfa. DR DrugBank; DB13173; Cerliponase alfa. DR DrugBank; DB16708; Cipaglucosidase alfa. DR DrugBank; DB11848; Mannose 6-phosphate. DR DrugBank; DB01277; Mecasermin. DR DrugBank; DB14751; Mecasermin rinfabate. DR DrugCentral; P11717; -. DR TCDB; 9.B.247.1.2; the mannose 6-phosphate receptor (m6pr) family. DR UniLectin; P11717; -. DR GlyConnect; P11717; 38 N-Linked glycans (16 sites). DR GlyCosmos; P11717; 23 sites, 41 glycans. DR GlyGen; P11717; 35 sites, 110 N-linked glycans (21 sites), 2 O-linked glycans (10 sites). DR iPTMnet; P11717; -. DR PhosphoSitePlus; P11717; -. DR SwissPalm; P11717; -. DR BioMuta; IGF2R; -. DR DMDM; 317373416; -. DR CPTAC; CPTAC-2601; -. DR CPTAC; non-CPTAC-2642; -. DR jPOST; P11717; -. DR MassIVE; P11717; -. DR PaxDb; 9606-ENSP00000349437; -. DR PeptideAtlas; P11717; -. DR ProteomicsDB; 52802; -. DR Pumba; P11717; -. DR Antibodypedia; 1396; 756 antibodies from 44 providers. DR DNASU; 3482; -. DR Ensembl; ENST00000356956.6; ENSP00000349437.1; ENSG00000197081.16. DR GeneID; 3482; -. DR KEGG; hsa:3482; -. DR MANE-Select; ENST00000356956.6; ENSP00000349437.1; NM_000876.4; NP_000867.3. DR UCSC; uc003qta.4; human. DR AGR; HGNC:5467; -. DR ClinPGx; PA29701; -. DR CTD; 3482; -. DR DisGeNET; 3482; -. DR GeneCards; IGF2R; -. DR HGNC; HGNC:5467; IGF2R. DR HPA; ENSG00000197081; Low tissue specificity. DR MalaCards; IGF2R; -. DR MIM; 147280; gene. DR OpenTargets; ENSG00000197081; -. DR VEuPathDB; HostDB:ENSG00000197081; -. DR eggNOG; KOG4504; Eukaryota. DR GeneTree; ENSGT00390000013943; -. DR HOGENOM; CLU_001182_0_0_1; -. DR InParanoid; P11717; -. DR OMA; FITYQSS; -. DR OrthoDB; 4504960at2759; -. DR PAN-GO; P11717; 5 GO annotations based on evolutionary models. DR PhylomeDB; P11717; -. DR PathwayCommons; P11717; -. DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network. DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR SignaLink; P11717; -. DR SIGNOR; P11717; -. DR Agora; ENSG00000197081; -. DR BioGRID-ORCS; 3482; 22 hits in 1171 CRISPR screens. DR ChiTaRS; IGF2R; human. DR EvolutionaryTrace; P11717; -. DR GeneWiki; Insulin-like_growth_factor_2_receptor; -. DR GenomeRNAi; 3482; -. DR Pharos; P11717; Tclin. DR PRO; PR:P11717; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P11717; protein. DR Bgee; ENSG00000197081; Expressed in stromal cell of endometrium and 195 other cell types or tissues. DR ExpressionAtlas; P11717; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0030118; C:clathrin coat; IEA:Ensembl. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; IEA:GOC. DR GO; GO:0005769; C:early endosome; IMP:UniProtKB. DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB. DR GO; GO:0005768; C:endosome; IDA:MGI. DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; EXP:UniProtKB. DR GO; GO:0005770; C:late endosome; IDA:MGI. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0005802; C:trans-Golgi network; IMP:UniProtKB. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:MGI. DR GO; GO:0030133; C:transport vesicle; TAS:Reactome. DR GO; GO:0038024; F:cargo receptor activity; IDA:UniProtKB. DR GO; GO:0005537; F:D-mannose binding; IEA:Ensembl. DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl. DR GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005520; F:insulin-like growth factor binding; IBA:GO_Central. DR GO; GO:0031995; F:insulin-like growth factor II binding; IEA:Ensembl. DR GO; GO:0051219; F:phosphoprotein binding; IDA:UniProtKB. DR GO; GO:0001972; F:retinoic acid binding; IEA:Ensembl. DR GO; GO:1905394; F:retromer complex binding; IDA:UniProtKB. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:0090160; P:Golgi to lysosome transport; IDA:UniProtKB. DR GO; GO:0044794; P:host-mediated activation of viral process; IMP:ARUK-UCL. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl. DR GO; GO:0006622; P:protein targeting to lysosome; IBA:GO_Central. DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl. DR GO; GO:1904772; P:response to tetrachloromethane; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR CDD; cd00062; FN2; 1. DR FunFam; 2.10.10.10:FF:000006; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000004; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000005; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000006; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000007; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000009; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000010; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000011; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000012; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000013; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000015; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000016; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000017; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000019; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000020; Insulin-like growth factor 2 receptor; 1. DR FunFam; 2.70.130.10:FF:000022; Insulin-like growth factor 2 receptor; 1. DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1. DR Gene3D; 2.70.130.10; Mannose-6-phosphate receptor binding domain; 15. DR InterPro; IPR000479; CIMR_rpt. DR InterPro; IPR000562; FN_type2_dom. DR InterPro; IPR036943; FN_type2_sf. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf. DR InterPro; IPR044865; MRH_dom. DR PANTHER; PTHR15071:SF17; CATION-INDEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR; 1. DR PANTHER; PTHR15071; MANNOSE-6-PHOSPHATE RECEPTOR FAMILY MEMBER; 1. DR Pfam; PF00878; CIMR; 15. DR Pfam; PF00040; fn2; 1. DR PRINTS; PR00013; FNTYPEII. DR SMART; SM01404; CIMR; 14. DR SMART; SM00059; FN2; 1. DR SUPFAM; SSF57440; Kringle-like; 1. DR SUPFAM; SSF50911; Mannose 6-phosphate receptor domain; 15. DR PROSITE; PS00023; FN2_1; 1. DR PROSITE; PS51092; FN2_2; 1. DR PROSITE; PS51914; MRH; 15. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Disulfide bond; KW Endosome; Glycoprotein; Golgi apparatus; Lipoprotein; Membrane; KW Methylation; Palmitate; Phosphoprotein; Proteomics identification; KW Receptor; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix; Transport. FT SIGNAL 1..40 FT /evidence="ECO:0000269|PubMed:2957598" FT CHAIN 41..2491 FT /note="Cation-independent mannose-6-phosphate receptor" FT /id="PRO_0000019229" FT TOPO_DOM 41..2304 FT /note="Lumenal" FT /evidence="ECO:0000269|PubMed:2957598" FT TRANSMEM 2305..2327 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2328..2491 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:2957598" FT DOMAIN 47..163 FT /note="MRH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 172..320 FT /note="MRH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 326..468 FT /note="MRH 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 473..619 FT /note="MRH 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 625..762 FT /note="MRH 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 765..924 FT /note="MRH 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 932..1079 FT /note="MRH 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 1082..1219 FT /note="MRH 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 1225..1363 FT /note="MRH 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 1367..1508 FT /note="MRH 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 1514..1648 FT /note="MRH 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 1650..1797 FT /note="MRH 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 1802..1989 FT /note="Fibronectin type-II" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DOMAIN 1992..2127 FT /note="MRH 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DOMAIN 2135..2280 FT /note="MRH 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT REGION 2424..2491 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2444..2459 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2464..2477 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2479..2491 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2352 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 2409 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 2425 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q07113" FT MOD_RES 2479 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 2484 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT CARBOHYD 112 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519" FT CARBOHYD 400 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 435 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 543 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 581 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519" FT CARBOHYD 626 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 747 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 871 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 951 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 957 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1164 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1246 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519" FT CARBOHYD 1312 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1656 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1757 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1816 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2085 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2136 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 49..69 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 77..84 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 117..149 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 134..161 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 174..212 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 228..235 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 275..306 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 288..318 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 328..366 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 374..382 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 420..454 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 434..466 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 475..519 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 531..538 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 572..605 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 586..617 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 627..664 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 672..679 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 731..760 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 767..814 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 823..830 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 875..910 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 893..922 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 934..970 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 976..987 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1042..1077 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1084..1125 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1134..1142 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1177..1205 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1190..1217 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1227..1262 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1270..1282 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1319..1349 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1333..1361 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1369..1408 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1420..1427 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1461..1494 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1476..1506 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 1516..1553 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 1559..1566 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 1598..1634 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 1614..1646 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 1652..1695 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 1706..1713 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 1750..1783 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 1766..1795 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 1804..1839 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 1850..1856 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 1893..1975 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 1903..1927 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479, FT ECO:0000269|PubMed:18046459" FT DISULFID 1917..1942 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479, FT ECO:0000269|PubMed:18046459" FT DISULFID 1957..1987 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 1994..2029 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 2039..2046 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 2082..2113 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 2096..2125 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262, FT ECO:0000269|PubMed:18046459" FT DISULFID 2188..2194 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 2232..2266 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT DISULFID 2248..2278 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262" FT VARIANT 91 FT /note="R -> H (in dbSNP:rs8191704)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_021304" FT VARIANT 203 FT /note="P -> L (in dbSNP:rs8191746)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_020470" FT VARIANT 231 FT /note="G -> D (in dbSNP:rs8191753)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_021305" FT VARIANT 252 FT /note="L -> V (in dbSNP:rs8191754)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_020471" FT VARIANT 273 FT /note="D -> G (in dbSNP:rs8191758)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_021306" FT VARIANT 512 FT /note="K -> Q (in dbSNP:rs8191776)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_021307" FT VARIANT 529 FT /note="R -> Q (in dbSNP:rs6413489)" FT /id="VAR_020472" FT VARIANT 604 FT /note="G -> S (in dbSNP:rs8191797)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_020473" FT VARIANT 724 FT /note="A -> T (in dbSNP:rs6413491)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_020474" FT VARIANT 817 FT /note="L -> V (in dbSNP:rs8191808)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_021308" FT VARIANT 856 FT /note="G -> S (in dbSNP:rs8191819)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_020475" FT VARIANT 1107 FT /note="T -> M (in dbSNP:rs8191842)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_020476" FT VARIANT 1124 FT /note="V -> I (in dbSNP:rs8191843)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_021309" FT VARIANT 1184 FT /note="T -> S (in dbSNP:rs8191844)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_020477" FT VARIANT 1254 FT /note="E -> A (in dbSNP:rs2230043)" FT /id="VAR_050428" FT VARIANT 1315 FT /note="G -> E (in dbSNP:rs8191859)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_021310" FT VARIANT 1335 FT /note="R -> H (in dbSNP:rs8191860)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_021311" FT VARIANT 1395 FT /note="T -> S (in dbSNP:rs2230048)" FT /id="VAR_050429" FT VARIANT 1619 FT /note="R -> G (in dbSNP:rs629849)" FT /evidence="ECO:0000269|PubMed:2957598, FT ECO:0000269|PubMed:2963003, ECO:0000269|Ref.3, FT ECO:0000269|Ref.5" FT /id="VAR_021312" FT VARIANT 1696 FT /note="Q -> R (in dbSNP:rs11552587)" FT /id="VAR_050430" FT VARIANT 1832 FT /note="R -> H (in dbSNP:rs8191904)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_021313" FT VARIANT 1860 FT /note="G -> D (in dbSNP:rs8191905)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_021314" FT VARIANT 1908 FT /note="I -> M (in dbSNP:rs8191908)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_021315" FT VARIANT 2020 FT /note="N -> S (in dbSNP:rs1805075)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_014722" FT VARIANT 2459 FT /note="A -> V (in dbSNP:rs8191955)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_021316" FT CONFLICT 254 FT /note="L -> V (in Ref. 2; AAA59866)" FT /evidence="ECO:0000305" FT CONFLICT 510 FT /note="E -> K (in Ref. 2; AAA59866)" FT /evidence="ECO:0000305" FT CONFLICT 612 FT /note="H -> R (in Ref. 1; CAA68395 and 3; AAF16870)" FT /evidence="ECO:0000305" FT CONFLICT 845 FT /note="V -> A (in Ref. 2; AAA59866)" FT /evidence="ECO:0000305" FT CONFLICT 1489 FT /note="S -> N (in Ref. 2; AAA59866)" FT /evidence="ECO:0000305" FT CONFLICT 1703 FT /note="G -> A (in Ref. 1; CAA68395 and 3; AAF16870)" FT /evidence="ECO:0000305" FT CONFLICT 2026 FT /note="I -> M (in Ref. 2; AAA59866)" FT /evidence="ECO:0000305" FT CONFLICT 2075 FT /note="T -> M (in Ref. 2; AAA59866)" FT /evidence="ECO:0000305" FT CONFLICT 2156 FT /note="K -> N (in Ref. 2; AAA59866)" FT /evidence="ECO:0000305" FT CONFLICT 2160 FT /note="A -> E (in Ref. 2; AAA59866)" FT /evidence="ECO:0000305" FT CONFLICT 2176 FT /note="Q -> L (in Ref. 2; AAA59866)" FT /evidence="ECO:0000305" FT CONFLICT 2330 FT /note="E -> K (in Ref. 2; AAA59866)" FT /evidence="ECO:0000305" FT CONFLICT 2335 FT /note="V -> M (in Ref. 2; AAA59866)" FT /evidence="ECO:0000305" FT CONFLICT 2341 FT /note="T -> S (in Ref. 2; AAA59866)" FT /evidence="ECO:0000305" FT CONFLICT 2410 FT /note="E -> T (in Ref. 2; AAA59866)" FT /evidence="ECO:0000305" FT HELIX 46..48 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:6V02" FT TURN 58..61 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 62..66 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:6V02" FT TURN 75..77 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 81..85 FT /evidence="ECO:0007829|PDB:6V02" FT TURN 88..91 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 94..105 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 108..112 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 127..134 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 148..157 FT /evidence="ECO:0007829|PDB:6V02" FT HELIX 158..160 FT /evidence="ECO:0007829|PDB:6V02" FT HELIX 164..166 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:6V02" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 196..199 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 206..209 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:6V02" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 218..220 FT /evidence="ECO:0007829|PDB:6V02" FT HELIX 224..227 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 233..240 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 242..247 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:6V02" FT TURN 256..258 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 259..265 FT /evidence="ECO:0007829|PDB:6V02" FT TURN 273..277 FT /evidence="ECO:0007829|PDB:6V02" FT HELIX 278..280 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 281..287 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 291..293 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 299..302 FT /evidence="ECO:0007829|PDB:6V02" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 307..313 FT /evidence="ECO:0007829|PDB:6V02" FT HELIX 315..317 FT /evidence="ECO:0007829|PDB:6V02" FT HELIX 319..321 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 322..329 FT /evidence="ECO:0007829|PDB:6V02" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 352..355 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 357..363 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 380..385 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 392..394 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 398..406 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 409..414 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 421..423 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 427..434 FT /evidence="ECO:0007829|PDB:6V02" FT TURN 440..443 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 444..452 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 455..462 FT /evidence="ECO:0007829|PDB:6V02" FT HELIX 463..465 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 475..479 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 482..485 FT /evidence="ECO:0007829|PDB:6P8I" FT TURN 487..489 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 518..520 FT /evidence="ECO:0007829|PDB:6P8I" FT HELIX 521..523 FT /evidence="ECO:0007829|PDB:6P8I" FT TURN 524..526 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 559..566 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 580..586 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 596..599 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 607..613 FT /evidence="ECO:0007829|PDB:6P8I" FT HELIX 614..616 FT /evidence="ECO:0007829|PDB:6P8I" FT STRAND 626..630 FT /evidence="ECO:0007829|PDB:6V02" FT TURN 632..634 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 637..639 FT /evidence="ECO:0007829|PDB:6V02" FT HELIX 641..643 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 650..653 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 655..661 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 663..665 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 670..672 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 676..682 FT /evidence="ECO:0007829|PDB:6V02" FT TURN 683..685 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 688..693 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 699..701 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 704..709 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 725..731 FT /evidence="ECO:0007829|PDB:6V02" FT TURN 733..737 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 740..743 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 751..756 FT /evidence="ECO:0007829|PDB:6V02" FT HELIX 757..759 FT /evidence="ECO:0007829|PDB:6V02" FT STRAND 935..937 FT /evidence="ECO:0007829|PDB:6Z32" FT TURN 939..941 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 944..946 FT /evidence="ECO:0007829|PDB:6Z32" FT HELIX 948..950 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 956..959 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 961..967 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 969..971 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 979..982 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 985..989 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 1002..1005 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 1007..1013 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 1019..1029 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 1032..1042 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 1047..1059 FT /evidence="ECO:0007829|PDB:6Z32" FT HELIX 1060..1062 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 1064..1074 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 1085..1087 FT /evidence="ECO:0007829|PDB:6Z31" FT STRAND 1093..1095 FT /evidence="ECO:0007829|PDB:6Z31" FT HELIX 1097..1099 FT /evidence="ECO:0007829|PDB:6Z31" FT STRAND 1102..1104 FT /evidence="ECO:0007829|PDB:6Z31" FT STRAND 1106..1111 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 1113..1115 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 1116..1122 FT /evidence="ECO:0007829|PDB:6Z31" FT STRAND 1124..1126 FT /evidence="ECO:0007829|PDB:6Z31" FT HELIX 1127..1129 FT /evidence="ECO:0007829|PDB:6Z31" FT TURN 1136..1138 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 1139..1145 FT /evidence="ECO:0007829|PDB:6Z31" FT STRAND 1148..1151 FT /evidence="ECO:0007829|PDB:6Z31" FT STRAND 1168..1172 FT /evidence="ECO:0007829|PDB:6Z31" FT STRAND 1175..1177 FT /evidence="ECO:0007829|PDB:6Z31" FT STRAND 1183..1190 FT /evidence="ECO:0007829|PDB:6Z31" FT STRAND 1198..1203 FT /evidence="ECO:0007829|PDB:6Z31" FT STRAND 1206..1213 FT /evidence="ECO:0007829|PDB:6Z31" FT HELIX 1214..1216 FT /evidence="ECO:0007829|PDB:6Z31" FT STRAND 1221..1224 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 1228..1230 FT /evidence="ECO:0007829|PDB:6Z30" FT TURN 1232..1234 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1237..1239 FT /evidence="ECO:0007829|PDB:6Z30" FT HELIX 1241..1244 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1248..1252 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1255..1259 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1279..1285 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1287..1289 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1291..1297 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1303..1305 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1308..1313 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1317..1319 FT /evidence="ECO:0007829|PDB:6Z30" FT TURN 1320..1322 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1326..1332 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1335..1337 FT /evidence="ECO:0007829|PDB:6Z30" FT HELIX 1338..1340 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1341..1345 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1350..1357 FT /evidence="ECO:0007829|PDB:6Z30" FT HELIX 1358..1360 FT /evidence="ECO:0007829|PDB:6Z30" FT HELIX 1361..1363 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1370..1372 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1378..1380 FT /evidence="ECO:0007829|PDB:6Z30" FT HELIX 1382..1384 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1387..1389 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1402..1405 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1407..1409 FT /evidence="ECO:0007829|PDB:6Z30" FT HELIX 1410..1413 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1415..1418 FT /evidence="ECO:0007829|PDB:6Z30" FT HELIX 1419..1421 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1425..1433 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1445..1447 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1450..1456 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1464..1467 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1469..1476 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1486..1491 FT /evidence="ECO:0007829|PDB:6Z30" FT TURN 1492..1494 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1495..1502 FT /evidence="ECO:0007829|PDB:6Z30" FT HELIX 1503..1505 FT /evidence="ECO:0007829|PDB:6Z30" FT STRAND 1512..1514 FT /evidence="ECO:0007829|PDB:5IEI" FT STRAND 1517..1519 FT /evidence="ECO:0007829|PDB:1GP0" FT TURN 1521..1523 FT /evidence="ECO:0007829|PDB:1GP0" FT STRAND 1526..1528 FT /evidence="ECO:0007829|PDB:1GP0" FT HELIX 1530..1532 FT /evidence="ECO:0007829|PDB:1GP0" FT STRAND 1533..1536 FT /evidence="ECO:0007829|PDB:1GP0" FT STRAND 1538..1542 FT /evidence="ECO:0007829|PDB:1GP0" FT TURN 1543..1545 FT /evidence="ECO:0007829|PDB:1GP0" FT STRAND 1546..1550 FT /evidence="ECO:0007829|PDB:1GP0" FT STRAND 1552..1554 FT /evidence="ECO:0007829|PDB:1GP0" FT STRAND 1557..1560 FT /evidence="ECO:0007829|PDB:6Z32" FT STRAND 1563..1567 FT /evidence="ECO:0007829|PDB:1GP0" FT TURN 1568..1570 FT /evidence="ECO:0007829|PDB:1GP0" FT STRAND 1573..1576 FT /evidence="ECO:0007829|PDB:5IEI" FT STRAND 1582..1584 FT /evidence="ECO:0007829|PDB:1GP0" FT STRAND 1587..1592 FT /evidence="ECO:0007829|PDB:1GP0" FT STRAND 1596..1598 FT /evidence="ECO:0007829|PDB:2L2A" FT STRAND 1599..1601 FT /evidence="ECO:0007829|PDB:1GP0" FT STRAND 1607..1614 FT /evidence="ECO:0007829|PDB:1GP0" FT STRAND 1616..1618 FT /evidence="ECO:0007829|PDB:2L2A" FT STRAND 1625..1630 FT /evidence="ECO:0007829|PDB:1GP0" FT TURN 1631..1634 FT /evidence="ECO:0007829|PDB:1GP0" FT STRAND 1635..1642 FT /evidence="ECO:0007829|PDB:1GP0" FT HELIX 1643..1645 FT /evidence="ECO:0007829|PDB:1GP0" FT TURN 1649..1651 FT /evidence="ECO:0007829|PDB:2CNJ" FT STRAND 1653..1656 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1659..1662 FT /evidence="ECO:0007829|PDB:2V5O" FT HELIX 1664..1666 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1669..1671 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1673..1675 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1690..1692 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1694..1696 FT /evidence="ECO:0007829|PDB:2V5O" FT HELIX 1697..1700 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1711..1714 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1717..1719 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1722..1727 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1732..1734 FT /evidence="ECO:0007829|PDB:2V5N" FT STRAND 1735..1737 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1743..1745 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1759..1766 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1775..1777 FT /evidence="ECO:0007829|PDB:2V5O" FT TURN 1781..1783 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1784..1791 FT /evidence="ECO:0007829|PDB:2V5O" FT HELIX 1792..1794 FT /evidence="ECO:0007829|PDB:2V5O" FT TURN 1801..1804 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1805..1807 FT /evidence="ECO:0007829|PDB:2V5O" FT TURN 1809..1811 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1814..1816 FT /evidence="ECO:0007829|PDB:2V5O" FT HELIX 1818..1821 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1825..1829 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1832..1836 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1838..1840 FT /evidence="ECO:0007829|PDB:2V5O" FT TURN 1845..1847 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1850..1858 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1863..1877 FT /evidence="ECO:0007829|PDB:2V5O" FT TURN 1878..1881 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1882..1888 FT /evidence="ECO:0007829|PDB:2V5O" FT HELIX 1893..1895 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1905..1909 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1912..1916 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1920..1924 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1926..1932 FT /evidence="ECO:0007829|PDB:2V5O" FT HELIX 1933..1936 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1939..1943 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1950..1957 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1967..1972 FT /evidence="ECO:0007829|PDB:2V5O" FT TURN 1973..1975 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1976..1984 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 1995..2000 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 2002..2004 FT /evidence="ECO:0007829|PDB:2V5O" FT HELIX 2005..2007 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 2011..2013 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 2015..2019 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 2022..2026 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 2043..2048 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 2054..2059 FT /evidence="ECO:0007829|PDB:2V5O" FT HELIX 2060..2062 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 2064..2068 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 2071..2076 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 2089..2096 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 2098..2109 FT /evidence="ECO:0007829|PDB:2V5O" FT TURN 2110..2113 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 2114..2121 FT /evidence="ECO:0007829|PDB:2V5O" FT HELIX 2122..2124 FT /evidence="ECO:0007829|PDB:2V5O" FT STRAND 2350..2355 FT /evidence="ECO:0007829|PDB:6N5X" FT STRAND 2368..2373 FT /evidence="ECO:0007829|PDB:6N5X" FT HELIX 2486..2490 FT /evidence="ECO:0007829|PDB:1JWG" SQ SEQUENCE 2491 AA; 274375 MW; 3841ADE559B48057 CRC64; MGAAAGRSPH LGPAPARRPQ RSLLLLQLLL LVAAPGSTQA QAAPFPELCS YTWEAVDTKN NVLYKINICG SVDIVQCGPS SAVCMHDLKT RTYHSVGDSV LRSATRSLLE FNTTVSCDQQ GTNHRVQSSI AFLCGKTLGT PEFVTATECV HYFEWRTTAA CKKDIFKANK EVPCYVFDEE LRKHDLNPLI KLSGAYLVDD SDPDTSLFIN VCRDIDTLRD PGSQLRACPP GTAACLVRGH QAFDVGQPRD GLKLVRKDRL VLSYVREEAG KLDFCDGHSP AVTITFVCPS ERREGTIPKL TAKSNCRYEI EWITEYACHR DYLESKTCSL SGEQQDVSID LTPLAQSGGS SYISDGKEYL FYLNVCGETE IQFCNKKQAA VCQVKKSDTS QVKAAGRYHN QTLRYSDGDL TLIYFGGDEC SSGFQRMSVI NFECNKTAGN DGKGTPVFTG EVDCTYFFTW DTEYACVKEK EDLLCGATDG KKRYDLSALV RHAEPEQNWE AVDGSQTETE KKHFFINICH RVLQEGKARG CPEDAAVCAV DKNGSKNLGK FISSPMKEKG NIQLSYSDGD DCGHGKKIKT NITLVCKPGD LESAPVLRTS GEGGCFYEFE WHTAAACVLS KTEGENCTVF DSQAGFSFDL SPLTKKNGAY KVETKKYDFY INVCGPVSVS PCQPDSGACQ VAKSDEKTWN LGLSNAKLSY YDGMIQLNYR GGTPYNNERH TPRATLITFL CDRDAGVGFP EYQEEDNSTY NFRWYTSYAC PEEPLECVVT DPSTLEQYDL SSLAKSEGGL GGNWYAMDNS GEHVTWRKYY INVCRPLNPV PGCNRYASAC QMKYEKDQGS FTEVVSISNL GMAKTGPVVE DSGSLLLEYV NGSACTTSDG RQTTYTTRIH LVCSRGRLNS HPIFSLNWEC VVSFLWNTEA ACPIQTTTDT DQACSIRDPN SGFVFNLNPL NSSQGYNVSG IGKIFMFNVC GTMPVCGTIL GKPASGCEAE TQTEELKNWK PARPVGIEKS LQLSTEGFIT LTYKGPLSAK GTADAFIVRF VCNDDVYSGP LKFLHQDIDS GQGIRNTYFE FETALACVPS PVDCQVTDLA GNEYDLTGLS TVRKPWTAVD TSVDGRKRTF YLSVCNPLPY IPGCQGSAVG SCLVSEGNSW NLGVVQMSPQ AAANGSLSIM YVNGDKCGNQ RFSTRITFEC AQISGSPAFQ LQDGCEYVFI WRTVEACPVV RVEGDNCEVK DPRHGNLYDL KPLGLNDTIV SAGEYTYYFR VCGKLSSDVC PTSDKSKVVS SCQEKREPQG FHKVAGLLTQ KLTYENGLLK MNFTGGDTCH KVYQRSTAIF FYCDRGTQRP VFLKETSDCS YLFEWRTQYA CPPFDLTECS FKDGAGNSFD LSSLSRYSDN WEAITGTGDP EHYLINVCKS LAPQAGTEPC PPEAAACLLG GSKPVNLGRV RDGPQWRDGI IVLKYVDGDL CPDGIRKKST TIRFTCSESQ VNSRPMFISA VEDCEYTFAW PTATACPMKS NEHDDCQVTN PSTGHLFDLS SLSGRAGFTA AYSEKGLVYM SICGENENCP PGVGACFGQT RISVGKANKR LRYVDQVLQL VYKDGSPCPS KSGLSYKSVI SFVCRPEARP TNRPMLISLD KQTCTLFFSW HTPLACEQAT ECSVRNGSSI VDLSPLIHRT GGYEAYDESE DDASDTNPDF YINICQPLNP MHGVPCPAGA AVCKVPIDGP PIDIGRVAGP PILNPIANEI YLNFESSTPC LADKHFNYTS LIAFHCKRGV SMGTPKLLRT SECDFVFEWE TPVVCPDEVR MDGCTLTDEQ LLYSFNLSSL STSTFKVTRD SRTYSVGVCT FAVGPEQGGC KDGGVCLLSG TKGASFGRLQ SMKLDYRHQD EAVVLSYVNG DRCPPETDDG VPCVFPFIFN GKSYEECIIE SRAKLWCSTT ADYDRDHEWG FCRHSNSYRT SSIIFKCDED EDIGRPQVFS EVRGCDVTFE WKTKVVCPPK KLECKFVQKH KTYDLRLLSS LTGSWSLVHN GVSYYINLCQ KIYKGPLGCS ERASICRRTT TGDVQVLGLV HTQKLGVIGD KVVVTYSKGY PCGGNKTASS VIELTCTKTV GRPAFKRFDI DSCTYYFSWD SRAACAVKPQ EVQMVNGTIT NPINGKSFSL GDIYFKLFRA SGDMRTNGDN YLYEIQLSSI TSSRNPACSG ANICQVKPND QHFSRKVGTS DKTKYYLQDG DLDVVFASSS KCGKDKTKSV SSTIFFHCDP LVEDGIPEFS HETADCQYLF SWYTSAVCPL GVGFDSENPG DDGQMHKGLS ERSQAVGAVL SLLLVALTCC LLALLLYKKE RRETVISKLT TCCRRSSNVS YKYSKVNKEE ETDENETEWL MEEIQLPPPR QGKEGQENGH ITTKSVKALS SLHGDDQDSE DEVLTIPEVK VHSGRGAGAE SSHPVRNAQS NALQEREDDR VGLVRGEKAR KGKSSSAQQK TVSSTKLVSF HDDSDEDLLH I //