ID TSP2_HUMAN Reviewed; 1172 AA. AC P35442; A6H8N1; A7E232; Q5RI52; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 27-MAR-2024, entry version 218. DE RecName: Full=Thrombospondin-2; DE Flags: Precursor; GN Name=THBS2; Synonyms=TSP2; 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]. RX PubMed=8406456; DOI=10.1006/geno.1993.1308; RA Labell T.L., Byers P.H.; RT "Sequence and characterization of the complete human thrombospondin 2 cDNA: RT potential regulatory role for the 3' untranslated region."; RL Genomics 17:225-229(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 560-1172. RC TISSUE=Fibroblast; RX PubMed=1559694; DOI=10.1016/0888-7543(92)90430-z; RA Labell T.L., McGookey Milewicz D.J., Disteche C.M., Byers P.H.; RT "Thrombospondin II: partial cDNA sequence, chromosome location, and RT expression of a second member of the thrombospondin gene family in RT humans."; RL Genomics 12:421-429(1992). RN [7] RP INTERACTION WITH THBS1 AND THBS2. RX PubMed=1371676; DOI=10.1016/0006-291x(92)91860-s; RA Asch A.S., Silbiger S., Heimer E., Nachman R.L.; RT "Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding."; RL Biochem. Biophys. Res. Commun. 182:1208-1217(1992). RN [8] RP DISULFIDE BONDS IN THROMBOSPONDIN DOMAIN. RX PubMed=11590138; DOI=10.1074/jbc.m104218200; RA Misenheimer T.M., Hahr A.J., Harms A.C., Annis D.S., Mosher D.F.; RT "Disulfide connectivity of recombinant C-terminal region of human RT thrombospondin 2."; RL J. Biol. Chem. 276:45882-45887(2001). RN [9] RP INVOLVEMENT IN SUSCEPTIBILITY TO IDD, AND TISSUE SPECIFICITY. RX PubMed=18455130; DOI=10.1016/j.ajhg.2008.03.013; RA Hirose Y., Chiba K., Karasugi T., Nakajima M., Kawaguchi Y., Mikami Y., RA Furuichi T., Mio F., Miyake A., Miyamoto T., Ozaki K., Takahashi A., RA Mizuta H., Kubo T., Kimura T., Tanaka T., Toyama Y., Ikegawa S.; RT "A functional polymorphism in THBS2 that affects alternative splicing and RT MMP binding is associated with lumbar-disc herniation."; RL Am. J. Hum. Genet. 82:1122-1129(2008). RN [10] RP FUNCTION. RX PubMed=20714802; DOI=10.1007/s10549-010-1085-7; RA Koch M., Hussein F., Woeste A., Grundker C., Frontzek K., Emons G., RA Hawighorst T.; RT "CD36-mediated activation of endothelial cell apoptosis by an N-terminal RT recombinant fragment of thrombospondin-2 inhibits breast cancer growth and RT metastasis in vivo."; RL Breast Cancer Res. Treat. 128:337-346(2011). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 551-1172 IN COMPLEX WITH CALCIUM RP IONS, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-584; ASN-710 AND ASN-1069. RX PubMed=16186819; DOI=10.1038/nsmb997; RA Carlson C.B., Bernstein D.A., Annis D.S., Misenheimer T.M., Hannah B.L., RA Mosher D.F., Keck J.L.; RT "Structure of the calcium-rich signature domain of human RT thrombospondin-2."; RL Nat. Struct. Mol. Biol. 12:910-914(2005). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 551-1172, AND MUTAGENESIS OF RP ASN-702. RX PubMed=18499674; DOI=10.1074/jbc.m800223200; RA Carlson C.B., Liu Y., Keck J.L., Mosher D.F.; RT "Influences of the N700S thrombospondin-1 polymorphism on protein structure RT and stability."; RL J. Biol. Chem. 283:20069-20076(2008). CC -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to- CC matrix interactions. Ligand for CD36 mediating antiangiogenic CC properties. {ECO:0000269|PubMed:20714802}. CC -!- SUBUNIT: Homotrimer; disulfide-linked. Interacts (via the TSP type I CC repeats) with CD36; the interaction conveys an antiangiogenic effect. CC Interacts (via the TSP type I repeats) with HRG; the interaction blocks CC the antiangiogenic effect of THBS2 with CD36 (By similarity). Can bind CC to fibrinogen, fibronectin, laminin and type V collagen. {ECO:0000250, CC ECO:0000269|PubMed:11590138, ECO:0000269|PubMed:1371676, CC ECO:0000269|PubMed:16186819}. CC -!- INTERACTION: CC P35442; P54290: Cacna2d1; Xeno; NbExp=2; IntAct=EBI-2466249, EBI-2466294; CC -!- TISSUE SPECIFICITY: High expression in invertebral disk tissue. CC {ECO:0000269|PubMed:18455130}. CC -!- DISEASE: Intervertebral disc disease (IDD) [MIM:603932]: A common CC musculo-skeletal disorder caused by degeneration of intervertebral CC disks of the lumbar spine. It results in low-back pain and unilateral CC leg pain. {ECO:0000269|PubMed:18455130}. Note=Disease susceptibility is CC associated with variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42549/THBS2"; 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; L12350; AAA03703.1; -; mRNA. DR EMBL; M81339; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK292429; BAF85118.1; -; mRNA. DR EMBL; BX322234; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW47455.1; -; Genomic_DNA. DR EMBL; BC146676; AAI46677.1; -; mRNA. DR EMBL; BC150175; AAI50176.1; -; mRNA. DR CCDS; CCDS34574.1; -. DR PIR; A47379; TSHUP2. DR RefSeq; NP_003238.2; NM_003247.3. DR PDB; 1YO8; X-ray; 2.60 A; A=551-1172. DR PDB; 2RHP; X-ray; 2.90 A; A=551-1172. DR PDBsum; 1YO8; -. DR PDBsum; 2RHP; -. DR AlphaFoldDB; P35442; -. DR SMR; P35442; -. DR BioGRID; 112916; 22. DR ComplexPortal; CPX-1788; Thrombospondin 2 complex. DR CORUM; P35442; -. DR IntAct; P35442; 13. DR STRING; 9606.ENSP00000355751; -. DR GlyConnect; 1805; 24 N-Linked glycans (4 sites). DR GlyCosmos; P35442; 7 sites, 23 glycans. DR GlyGen; P35442; 11 sites, 23 N-linked glycans (4 sites), 1 O-linked glycan (4 sites). DR iPTMnet; P35442; -. DR PhosphoSitePlus; P35442; -. DR BioMuta; THBS2; -. DR DMDM; 215273908; -. DR CPTAC; CPTAC-1186; -. DR EPD; P35442; -. DR jPOST; P35442; -. DR MassIVE; P35442; -. DR MaxQB; P35442; -. DR PaxDb; 9606-ENSP00000355751; -. DR PeptideAtlas; P35442; -. DR ProteomicsDB; 55062; -. DR Antibodypedia; 33564; 286 antibodies from 26 providers. DR DNASU; 7058; -. DR Ensembl; ENST00000366787.7; ENSP00000355751.3; ENSG00000186340.17. DR Ensembl; ENST00000617924.6; ENSP00000482784.1; ENSG00000186340.17. DR Ensembl; ENST00000676498.1; ENSP00000504820.1; ENSG00000186340.17. DR Ensembl; ENST00000676760.1; ENSP00000503020.1; ENSG00000186340.17. DR GeneID; 7058; -. DR KEGG; hsa:7058; -. DR MANE-Select; ENST00000617924.6; ENSP00000482784.1; NM_003247.5; NP_003238.2. DR UCSC; uc003qwt.5; human. DR AGR; HGNC:11786; -. DR CTD; 7058; -. DR DisGeNET; 7058; -. DR GeneCards; THBS2; -. DR HGNC; HGNC:11786; THBS2. DR HPA; ENSG00000186340; Low tissue specificity. DR MalaCards; THBS2; -. DR MIM; 188061; gene. DR MIM; 603932; phenotype. DR neXtProt; NX_P35442; -. DR OpenTargets; ENSG00000186340; -. DR PharmGKB; PA36498; -. DR VEuPathDB; HostDB:ENSG00000186340; -. DR eggNOG; ENOG502QRK8; Eukaryota. DR GeneTree; ENSGT00940000157846; -. DR HOGENOM; CLU_009257_0_0_1; -. DR InParanoid; P35442; -. DR OMA; MPGVMLQ; -. DR OrthoDB; 5345349at2759; -. DR PhylomeDB; P35442; -. DR TreeFam; TF324917; -. DR PathwayCommons; P35442; -. DR Reactome; R-HSA-186797; Signaling by PDGF. DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS. DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins. DR SignaLink; P35442; -. DR SIGNOR; P35442; -. DR BioGRID-ORCS; 7058; 10 hits in 1154 CRISPR screens. DR ChiTaRS; THBS2; human. DR EvolutionaryTrace; P35442; -. DR GeneWiki; THBS2; -. DR GenomeRNAi; 7058; -. DR Pharos; P35442; Tbio. DR PRO; PR:P35442; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P35442; Protein. DR Bgee; ENSG00000186340; Expressed in pericardium and 190 other cell types or tissues. DR ExpressionAtlas; P35442; baseline and differential. DR GO; GO:0005604; C:basement membrane; IEA:Ensembl. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0008201; F:heparin binding; TAS:ProtInc. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB. DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl. DR Gene3D; 2.60.120.200; -; 2. DR Gene3D; 6.20.200.20; -; 1. DR Gene3D; 2.10.25.10; Laminin; 3. DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3. DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 2. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR024731; EGF_dom. DR InterPro; IPR003367; Thrombospondin_3-like_rpt. DR InterPro; IPR017897; Thrombospondin_3_rpt. DR InterPro; IPR008859; Thrombospondin_C. DR InterPro; IPR000884; TSP1_rpt. DR InterPro; IPR036383; TSP1_rpt_sf. DR InterPro; IPR028974; TSP_type-3_rpt. DR InterPro; IPR048287; TSPN-like_N. DR InterPro; IPR001007; VWF_dom. DR PANTHER; PTHR10199; THROMBOSPONDIN; 1. DR PANTHER; PTHR10199:SF10; THROMBOSPONDIN-2; 1. DR Pfam; PF12947; EGF_3; 1. DR Pfam; PF00090; TSP_1; 3. DR Pfam; PF02412; TSP_3; 6. DR Pfam; PF05735; TSP_C; 1. DR Pfam; PF00093; VWC; 1. DR PRINTS; PR01705; TSP1REPEAT. DR SMART; SM00181; EGF; 3. DR SMART; SM00179; EGF_CA; 2. DR SMART; SM00209; TSP1; 3. DR SMART; SM00210; TSPN; 1. DR SMART; SM00214; VWC; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF57603; FnI-like domain; 1. DR SUPFAM; SSF103647; TSP type-3 repeat; 3. DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 2. DR PROSITE; PS50092; TSP1; 3. DR PROSITE; PS51234; TSP3; 8. DR PROSITE; PS51236; TSP_CTER; 1. DR PROSITE; PS01208; VWFC_1; 1. DR PROSITE; PS50184; VWFC_2; 1. DR Genevisible; P35442; HS. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cell adhesion; Disulfide bond; EGF-like domain; KW Glycoprotein; Heparin-binding; Reference proteome; Repeat; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..1172 FT /note="Thrombospondin-2" FT /id="PRO_0000035846" FT DOMAIN 19..215 FT /note="Laminin G-like" FT DOMAIN 318..375 FT /note="VWFC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220" FT DOMAIN 381..431 FT /note="TSP type-1 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210" FT DOMAIN 437..492 FT /note="TSP type-1 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210" FT DOMAIN 494..549 FT /note="TSP type-1 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210" FT DOMAIN 549..589 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 648..692 FT /note="EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REPEAT 693..728 FT /note="TSP type-3 1" FT REPEAT 729..764 FT /note="TSP type-3 2" FT REPEAT 765..787 FT /note="TSP type-3 3" FT REPEAT 788..823 FT /note="TSP type-3 4" FT REPEAT 824..846 FT /note="TSP type-3 5" FT REPEAT 847..884 FT /note="TSP type-3 6" FT REPEAT 885..920 FT /note="TSP type-3 7" FT REPEAT 921..956 FT /note="TSP type-3 8" FT DOMAIN 960..1172 FT /note="TSP C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635" FT REGION 19..232 FT /note="Heparin-binding" FT /evidence="ECO:0000255" FT REGION 843..931 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 928..930 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT COMPBIAS 871..886 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 906..931 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 151 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 316 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 330 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 457 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 584 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16186819" FT CARBOHYD 710 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16186819" FT CARBOHYD 1069 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16186819" FT DISULFID 266 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 270 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 393..425 FT /evidence="ECO:0000250" FT DISULFID 397..430 FT /evidence="ECO:0000250" FT DISULFID 408..415 FT /evidence="ECO:0000250" FT DISULFID 449..486 FT /evidence="ECO:0000250" FT DISULFID 453..491 FT /evidence="ECO:0000250" FT DISULFID 464..476 FT /evidence="ECO:0000250" FT DISULFID 506..543 FT /evidence="ECO:0000250" FT DISULFID 510..548 FT /evidence="ECO:0000250" FT DISULFID 521..533 FT /evidence="ECO:0000250" FT DISULFID 553..564 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 558..574 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 577..588 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 594..610 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 601..619 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 622..646 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 652..665 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 659..678 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 680..691 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 707..715 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 720..740 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 756..776 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 779..799 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 815..835 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 838..858 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 876..896 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 912..932 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT DISULFID 948..1169 FT /evidence="ECO:0000269|PubMed:16186819, FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8, FT ECO:0007744|PDB:2RHP" FT VARIANT 133 FT /note="T -> S (in dbSNP:rs36088849)" FT /id="VAR_045842" FT VARIANT 375 FT /note="L -> F (in dbSNP:rs35404985)" FT /id="VAR_045843" FT MUTAGEN 702 FT /note="N->S: Alters protein stability." FT /evidence="ECO:0000269|PubMed:18499674" FT CONFLICT 2 FT /note="V -> A (in Ref. 5; AAI50176)" FT /evidence="ECO:0000305" FT CONFLICT 171..173 FT /note="DSF -> GPV (in Ref. 1; AAA03703)" FT /evidence="ECO:0000305" FT CONFLICT 576 FT /note="S -> F (in Ref. 1; AAA03703)" FT /evidence="ECO:0000305" FT CONFLICT 1111 FT /note="R -> G (in Ref. 5; AAI46677)" FT /evidence="ECO:0000305" FT HELIX 552..555 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 564..566 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 572..574 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 585..587 FT /evidence="ECO:0007829|PDB:1YO8" FT TURN 593..596 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 605..607 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 610..612 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 614..619 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 626..628 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 632..636 FT /evidence="ECO:0007829|PDB:1YO8" FT HELIX 637..640 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 646..648 FT /evidence="ECO:0007829|PDB:1YO8" FT TURN 651..655 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 663..667 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 673..680 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 684..693 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 697..700 FT /evidence="ECO:0007829|PDB:1YO8" FT TURN 706..710 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 712..714 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 734..736 FT /evidence="ECO:0007829|PDB:1YO8" FT TURN 738..740 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 746..749 FT /evidence="ECO:0007829|PDB:1YO8" FT TURN 751..753 FT /evidence="ECO:0007829|PDB:1YO8" FT TURN 755..758 FT /evidence="ECO:0007829|PDB:2RHP" FT STRAND 767..772 FT /evidence="ECO:0007829|PDB:1YO8" FT HELIX 774..776 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 793..795 FT /evidence="ECO:0007829|PDB:1YO8" FT HELIX 797..799 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 805..808 FT /evidence="ECO:0007829|PDB:1YO8" FT TURN 810..812 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 829..831 FT /evidence="ECO:0007829|PDB:1YO8" FT HELIX 833..835 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 851..854 FT /evidence="ECO:0007829|PDB:1YO8" FT TURN 856..858 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 866..869 FT /evidence="ECO:0007829|PDB:1YO8" FT HELIX 871..873 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 890..892 FT /evidence="ECO:0007829|PDB:1YO8" FT TURN 894..896 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 903..905 FT /evidence="ECO:0007829|PDB:1YO8" FT HELIX 907..909 FT /evidence="ECO:0007829|PDB:1YO8" FT TURN 911..914 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 926..928 FT /evidence="ECO:0007829|PDB:1YO8" FT HELIX 930..932 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 939..941 FT /evidence="ECO:0007829|PDB:1YO8" FT HELIX 943..945 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 960..968 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 971..973 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 979..982 FT /evidence="ECO:0007829|PDB:1YO8" FT HELIX 983..985 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 987..990 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 995..1016 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 1024..1033 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 1036..1045 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 1053..1055 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 1061..1069 FT /evidence="ECO:0007829|PDB:1YO8" FT HELIX 1076..1083 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 1084..1086 FT /evidence="ECO:0007829|PDB:1YO8" FT TURN 1089..1091 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 1092..1097 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 1110..1116 FT /evidence="ECO:0007829|PDB:1YO8" FT TURN 1118..1120 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 1122..1129 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 1132..1136 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 1139..1141 FT /evidence="ECO:0007829|PDB:2RHP" FT STRAND 1148..1156 FT /evidence="ECO:0007829|PDB:1YO8" FT STRAND 1159..1169 FT /evidence="ECO:0007829|PDB:1YO8" SQ SEQUENCE 1172 AA; 129991 MW; 415BF376F4669F6A CRC64; MVWRLVLLAL WVWPSTQAGH QDKDTTFDLF SISNINRKTI GAKQFRGPDP GVPAYRFVRF DYIPPVNADD LSKITKIMRQ KEGFFLTAQL KQDGKSRGTL LALEGPGLSQ RQFEIVSNGP ADTLDLTYWI DGTRHVVSLE DVGLADSQWK NVTVQVAGET YSLHVGCDLI DSFALDEPFY EHLQAEKSRM YVAKGSARES HFRGLLQNVH LVFENSVEDI LSKKGCQQGQ GAEINAISEN TETLRLGPHV TTEYVGPSSE RRPEVCERSC EELGNMVQEL SGLHVLVNQL SENLKRVSND NQFLWELIGG PPKTRNMSAC WQDGRFFAEN ETWVVDSCTT CTCKKFKTIC HQITCPPATC ASPSFVEGEC CPSCLHSVDG EEGWSPWAEW TQCSVTCGSG TQQRGRSCDV TSNTCLGPSI QTRACSLSKC DTRIRQDGGW SHWSPWSSCS VTCGVGNITR IRLCNSPVPQ MGGKNCKGSG RETKACQGAP CPIDGRWSPW SPWSACTVTC AGGIRERTRV CNSPEPQYGG KACVGDVQER QMCNKRSCPV DGCLSNPCFP GAQCSSFPDG SWSCGSCPVG FLGNGTHCED LDECALVPDI CFSTSKVPRC VNTQPGFHCL PCPPRYRGNQ PVGVGLEAAK TEKQVCEPEN PCKDKTHNCH KHAECIYLGH FSDPMYKCEC QTGYAGDGLI CGEDSDLDGW PNLNLVCATN ATYHCIKDNC PHLPNSGQED FDKDGIGDAC DDDDDNDGVT DEKDNCQLLF NPRQADYDKD EVGDRCDNCP YVHNPAQIDT DNNGEGDACS VDIDGDDVFN ERDNCPYVYN TDQRDTDGDG VGDHCDNCPL VHNPDQTDVD NDLVGDQCDN NEDIDDDGHQ NNQDNCPYIS NANQADHDRD GQGDACDPDD DNDGVPDDRD NCRLVFNPDQ EDLDGDGRGD ICKDDFDNDN IPDIDDVCPE NNAISETDFR NFQMVPLDPK GTTQIDPNWV IRHQGKELVQ TANSDPGIAV GFDEFGSVDF SGTFYVNTDR DDDYAGFVFG YQSSSRFYVV MWKQVTQTYW EDQPTRAYGY SGVSLKVVNS TTGTGEHLRN ALWHTGNTPG QVRTLWHDPR NIGWKDYTAY RWHLTHRPKT GYIRVLVHEG KQVMADSGPI YDQTYAGGRL GLFVFSQEMV YFSDLKYECR DI //