ID MACF1_HUMAN Reviewed; 7388 AA. AC Q9UPN3; B1ALC5; E9PJT0; O75053; Q5VW20; Q8WXY1; Q8WXY2; Q96PK2; Q9H540; AC Q9UKP0; Q9ULG9; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 4. DT 03-MAY-2023, entry version 211. DE RecName: Full=Microtubule-actin cross-linking factor 1, isoforms 1/2/3/4/5 {ECO:0000305}; DE AltName: Full=620 kDa actin-binding protein; DE Short=ABP620; DE AltName: Full=Actin cross-linking family protein 7 {ECO:0000303|PubMed:20937854}; DE AltName: Full=Macrophin-1 {ECO:0000303|PubMed:10529403}; DE AltName: Full=Trabeculin-alpha; GN Name=MACF1 {ECO:0000312|HGNC:HGNC:13664}; GN Synonyms=ABP620, ACF7 {ECO:0000303|PubMed:20937854}, KIAA0465, KIAA0754, GN KIAA1251; 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] (ISOFORM 2). RX PubMed=10529403; DOI=10.1006/bbrc.1999.1538; RA Okuda T., Matsuda S., Nakatsugawa S., Ichigotani Y., Iwahashi N., RA Takahashi M., Ishigaki T., Hamaguchi M.; RT "Molecular cloning of macrophin, a human homologue of Drosophila kakapo RT with a close structural similarity to plectin and dystrophin."; RL Biochem. Biophys. Res. Commun. 264:568-574(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANTS VAL-4357 AND THR-6628. RX PubMed=10559237; DOI=10.1074/jbc.274.47.33522; RA Sun Y., Zhang J., Kraeft S.-K., Auclair D., Chang M.-S., Liu Y., RA Sutherland R., Salgia R., Griffin J.D., Ferland L.H., Chen L.B.; RT "Molecular cloning and characterization of human trabeculin-alpha, a giant RT protein defining a new family of actin-binding proteins."; RL J. Biol. Chem. 274:33522-33530(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE RP [GENOMIC DNA] OF 182-6770 (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE RP SPECIFICITY, AND VARIANT THR-6628. RX PubMed=11845288; DOI=10.1007/s00335-001-3037-3; RA Gong T.-W.L., Besirli C.G., Lomax M.I.; RT "MACF1 gene structure: a hybrid of plectin and dystrophin."; RL Mamm. Genome 12:852-861(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 868-4417 (ISOFORM 2). RC TISSUE=Brain; RX PubMed=10574462; DOI=10.1093/dnares/6.5.337; RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:337-345(1999). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 868-7388 (ISOFORM 5). RC TISSUE=Brain; RX PubMed=9455484; DOI=10.1093/dnares/4.5.345; RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., RA Nomura N., Ohara O.; RT "Characterization of cDNA clones in size-fractionated cDNA libraries from RT human brain."; RL DNA Res. 4:345-349(1997). RN [7] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [8] RP SEQUENCE REVISION. RA Ohara O.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GOLGA4. RX PubMed=15265687; DOI=10.1016/j.yexcr.2004.04.047; RA Kakinuma T., Ichikawa H., Tsukada Y., Nakamura T., Toh B.H.; RT "Interaction between p230 and MACF1 is associated with transport of a RT glycosyl phosphatidyl inositol-anchored protein from the Golgi to the cell RT periphery."; RL Exp. Cell Res. 298:388-398(2004). RN [10] RP IDENTIFICATION OF ISOFORM 1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=16076900; DOI=10.1242/jcs.02510; RA Lin C.-M., Chen H.-J., Leung C.L., Parry D.A.D., Liem R.K.H.; RT "Microtubule actin crosslinking factor 1b: a novel plakin that localizes to RT the Golgi complex."; RL J. Cell Sci. 118:3727-3738(2005). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4521, AND IDENTIFICATION BY RP 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1376; SER-3927; SER-4495; RP SER-4496; SER-6967; THR-7254; SER-7292 AND SER-7330, 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 [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1376; SER-4521 AND SER-7330, 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6210, 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 [16] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=20937854; DOI=10.1073/pnas.1000975107; RA Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.; RT "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the RT plasma membrane of migrating cells."; RL Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-1376; SER-3927 AND RP SER-4521, 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 [18] 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-1376; SER-4496; RP SER-4521 AND SER-4962, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1122; SER-1367; SER-1376; RP SER-2006; SER-2051; SER-3331; SER-3927; SER-4496; SER-4521; SER-4836; RP SER-5808; SER-6967; SER-7279 AND SER-7330, AND IDENTIFICATION BY MASS RP 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-814; SER-1376; RP SER-3927; SER-5808; SER-6032 AND SER-7330, AND IDENTIFICATION BY MASS RP 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 [22] 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 [23] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAMSAP3. RX PubMed=27693509; DOI=10.1016/j.devcel.2016.09.003; RA Ning W., Yu Y., Xu H., Liu X., Wang D., Wang J., Wang Y., Meng W.; RT "The CAMSAP3-ACF7 complex couples noncentrosomal microtubules with actin RT filaments to coordinate their dynamics."; RL Dev. Cell 39:61-74(2016). RN [24] RP INTERACTION WITH CAMSAP3. RX PubMed=27802168; DOI=10.1242/jcs.194878; RA Noordstra I., Liu Q., Nijenhuis W., Hua S., Jiang K., Baars M., RA Remmelzwaal S., Martin M., Kapitein L.C., Akhmanova A.; RT "Control of apico-basal epithelial polarity by the microtubule minus-end- RT binding protein CAMSAP3 and spectraplakin ACF7."; RL J. Cell Sci. 129:4278-4288(2016). RN [25] RP INVOLVEMENT IN LIS9, AND VARIANTS LIS9 ARG-6664; PHE-7135; TYR-7186; RP GLY-7188 AND PHE-7188. RX PubMed=30471716; DOI=10.1016/j.ajhg.2018.10.019; RG University of Washington Center for Mendelian Genomics; RG Center for Mendelian Genomics at the Broad Institute of MIT and Harvard; RA Dobyns W.B., Aldinger K.A., Ishak G.E., Mirzaa G.M., Timms A.E., RA Grout M.E., Dremmen M.H.G., Schot R., Vandervore L., van Slegtenhorst M.A., RA Wilke M., Kasteleijn E., Lee A.S., Barry B.J., Chao K.R., Szczaluba K., RA Kobori J., Hanson-Kahn A., Bernstein J.A., Carr L., D'Arco F., Miyana K., RA Okazaki T., Saito Y., Sasaki M., Das S., Wheeler M.M., Bamshad M.J., RA Nickerson D.A., Engle E.C., Verheijen F.W., Doherty D., Mancini G.M.S.; RT "MACF1 mutations encoding highly conserved zinc-binding residues of the GAR RT domain cause defects in neuronal migration and axon guidance."; RL Am. J. Hum. Genet. 103:1009-1021(2018). RN [26] RP VARIANTS [LARGE SCALE ANALYSIS] VAL-302; GLN-6462 AND GLU-7093. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: [Isoform 2]: F-actin-binding protein which plays a role in CC cross-linking actin to other cytoskeletal proteins and also binds to CC microtubules (PubMed:15265687, PubMed:20937854). Plays an important CC role in ERBB2-dependent stabilization of microtubules at the cell CC cortex (PubMed:20937854). Acts as a positive regulator of Wnt receptor CC signaling pathway and is involved in the translocation of AXIN1 and its CC associated complex (composed of APC, CTNNB1 and GSK3B) from the CC cytoplasm to the cell membrane (By similarity). Has actin-regulated CC ATPase activity and is essential for controlling focal adhesions (FAs) CC assembly and dynamics (By similarity). Interaction with CAMSAP3 at the CC minus ends of non-centrosomal microtubules tethers microtubules minus- CC ends to actin filaments, regulating focal adhesion size and cell CC migration (PubMed:27693509). May play role in delivery of transport CC vesicles containing GPI-linked proteins from the trans-Golgi network CC through its interaction with GOLGA4 (PubMed:15265687). Plays a key role CC in wound healing and epidermal cell migration (By similarity). Required CC for efficient upward migration of bulge cells in response to wounding CC and this function is primarily rooted in its ability to coordinate CC microtubule dynamics and polarize hair follicle stem cells (By CC similarity). As a regulator of actin and microtubule arrangement and CC stabilization, it plays an essential role in neurite outgrowth, CC branching and spine formation during brain development (By similarity). CC {ECO:0000250|UniProtKB:Q9QXZ0, ECO:0000269|PubMed:15265687, CC ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:27693509}. CC -!- SUBUNIT: Isoform 2: Interacts with MAPRE1, CLASP1, CLASP2, AXIN1 and CC LRP6 (By similarity). Isoform 2: Found in a complex composed of MACF1, CC APC, AXIN1, CTNNB1 and GSK3B (By similarity). Isoform 2: Interacts with CC GOLGA4 (PubMed:15265687). Isoform 2: Interacts with CAMSAP3 CC (PubMed:27693509, PubMed:27802168). {ECO:0000250|UniProtKB:Q9QXZ0, CC ECO:0000269|PubMed:15265687, ECO:0000269|PubMed:27693509, CC ECO:0000269|PubMed:27802168}. CC -!- INTERACTION: CC Q9UPN3; Q9NRI5: DISC1; NbExp=4; IntAct=EBI-522925, EBI-529989; CC Q9UPN3; Q9NRI5-1: DISC1; NbExp=3; IntAct=EBI-522925, EBI-15881455; CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:15265687, ECO:0000269|PubMed:27693509}. Cytoplasm CC {ECO:0000269|PubMed:15265687}. Golgi apparatus CC {ECO:0000269|PubMed:15265687}. Cell membrane CC {ECO:0000269|PubMed:20937854}. Cell projection, ruffle membrane CC {ECO:0000269|PubMed:20937854}. Note=The phosphorylated form is found in CC the cytoplasm while the non-phosphorylated form associates with the CC microtubules (By similarity). Localizes to the tips of microtubules CC (PubMed:27693509). Associated with the minus-end of microtubules via CC interaction with CAMSAP3 (PubMed:27693509). APC controls its CC localization to the cell membrane which is critical for its function in CC microtubule stabilization (PubMed:20937854). CC {ECO:0000250|UniProtKB:Q9QXZ0, ECO:0000269|PubMed:20937854, CC ECO:0000269|PubMed:27693509}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm CC {ECO:0000269|PubMed:16076900}. Golgi apparatus CC {ECO:0000269|PubMed:16076900}. Note=Localizes to the tips of CC microtubules. {ECO:0000269|PubMed:16076900}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=Macf1b; CC IsoId=Q9UPN3-1; Sequence=Displayed; CC Name=2; Synonyms=Macf1a; CC IsoId=Q9UPN3-2; Sequence=VSP_041391, VSP_041393; CC Name=3; CC IsoId=Q9UPN3-3; Sequence=VSP_041390, VSP_041391, VSP_041392, CC VSP_041393; CC Name=5; CC IsoId=Q9UPN3-4; Sequence=VSP_041391, VSP_041392; CC Name=4; CC IsoId=Q9UPN3-5; Sequence=VSP_043626, VSP_041393, VSP_043627; CC Name=6; CC IsoId=O94854-3; Sequence=External; CC Name=7; CC IsoId=O94854-4; Sequence=External; CC -!- TISSUE SPECIFICITY: Isoform 2: Ubiquitously expressed. Isoform 1: CC Expressed in cell lines NCI-H460, A-549 and HaCaT. Isoform 4: Expressed CC in heart, lung, pituitary and placenta, not found in brain, kidney, CC liver, pancreas or skeletal muscle. {ECO:0000269|PubMed:11845288, CC ECO:0000269|PubMed:16076900}. CC -!- DOMAIN: The C-terminal tail is required for phosphorylation by GSK3B CC and for microtubule-binding. {ECO:0000250|UniProtKB:Q9QXZ0}. CC -!- PTM: Phosphorylated on serine residues in the C-terminal tail by GSK3B. CC Phosphorylation inhibits microtubule-binding and this plays a critical CC role in bulge stem cell migration and skin wound repair. Wnt-signaling CC can repress phosphorylation (By similarity). CC {ECO:0000250|UniProtKB:Q9QXZ0}. CC -!- DISEASE: Lissencephaly 9 with complex brainstem malformation (LIS9) CC [MIM:618325]: A form of lissencephaly, a disorder of cortical CC development characterized by agyria or pachygyria and disorganization CC of the clear neuronal lamination of normal six-layered cortex. LIS9 is CC an autosomal dominant form clinically characterized by global CC developmental delay apparent since infancy, impaired intellectual CC development with poor or absent speech, and sometimes abnormal or CC involuntary movements. Brain imaging shows malformation of the CC brainstem, in addition to pachygyria and lissencephaly. CC {ECO:0000269|PubMed:30471716}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA83821.1; Type=Frameshift; Evidence={ECO:0000305}; 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; AB029290; BAA83821.1; ALT_FRAME; mRNA. DR EMBL; AF141968; AAF06360.1; -; mRNA. DR EMBL; AF317696; AAL09459.1; -; mRNA. DR EMBL; AF325341; AAL38997.1; -; Genomic_DNA. DR EMBL; AF325333; AAL38997.1; JOINED; Genomic_DNA. DR EMBL; AF325334; AAL38997.1; JOINED; Genomic_DNA. DR EMBL; AF325335; AAL38997.1; JOINED; Genomic_DNA. DR EMBL; AF325336; AAL38997.1; JOINED; Genomic_DNA. DR EMBL; AF325339; AAL38997.1; JOINED; Genomic_DNA. DR EMBL; AF325340; AAL38997.1; JOINED; Genomic_DNA. DR EMBL; AF325341; AAL39000.1; -; Genomic_DNA. DR EMBL; AF325330; AAL39000.1; JOINED; Genomic_DNA. DR EMBL; AF325331; AAL39000.1; JOINED; Genomic_DNA. DR EMBL; AF325332; AAL39000.1; JOINED; Genomic_DNA. DR EMBL; AF325333; AAL39000.1; JOINED; Genomic_DNA. DR EMBL; AF325334; AAL39000.1; JOINED; Genomic_DNA. DR EMBL; AF325335; AAL39000.1; JOINED; Genomic_DNA. DR EMBL; AF325336; AAL39000.1; JOINED; Genomic_DNA. DR EMBL; AF325339; AAL39000.1; JOINED; Genomic_DNA. DR EMBL; AF325340; AAL39000.1; JOINED; Genomic_DNA. DR EMBL; AL137853; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL355477; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL365277; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL442071; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL356055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB033077; BAA86565.1; -; mRNA. DR EMBL; AB007934; BAA32310.3; -; mRNA. DR CCDS; CCDS435.1; -. [Q9UPN3-2] DR PIR; T00079; T00079. DR RefSeq; NP_036222.3; NM_012090.5. [Q9UPN3-2] DR PDB; 4Z6G; X-ray; 2.65 A; A=74-421. DR PDB; 5VE9; X-ray; 2.79 A; A/B=7024-7108, C=7118-7191. DR PDB; 5X57; X-ray; 1.45 A; A=7113-7193. DR PDBsum; 4Z6G; -. DR PDBsum; 5VE9; -. DR PDBsum; 5X57; -. DR SMR; Q9UPN3; -. DR BioGRID; 117048; 166. DR DIP; DIP-50616N; -. DR IntAct; Q9UPN3; 61. DR MINT; Q9UPN3; -. DR STRING; 9606.ENSP00000354573; -. DR TCDB; 8.A.66.1.8; the dystrophin (dystrophin) family. DR GlyCosmos; Q9UPN3; 7 sites, 1 glycan. DR GlyGen; Q9UPN3; 12 sites, 1 O-linked glycan (12 sites). DR iPTMnet; Q9UPN3; -. DR PhosphoSitePlus; Q9UPN3; -. DR SwissPalm; Q9UPN3; -. DR BioMuta; MACF1; -. DR DMDM; 338817989; -. DR EPD; Q9UPN3; -. DR jPOST; Q9UPN3; -. DR MassIVE; Q9UPN3; -. DR MaxQB; Q9UPN3; -. DR PaxDb; Q9UPN3; -. DR PeptideAtlas; Q9UPN3; -. DR ProteomicsDB; 85382; -. [Q9UPN3-1] DR ProteomicsDB; 85383; -. [Q9UPN3-2] DR ProteomicsDB; 85384; -. [Q9UPN3-3] DR ProteomicsDB; 85385; -. [Q9UPN3-4] DR ProteomicsDB; 85386; -. [Q9UPN3-5] DR Antibodypedia; 31853; 71 antibodies from 18 providers. DR DNASU; 23499; -. DR Ensembl; ENST00000361689.7; ENSP00000354573.2; ENSG00000127603.32. [Q9UPN3-2] DR GeneID; 23499; -. DR KEGG; hsa:23499; -. DR UCSC; uc031pmd.2; human. [Q9UPN3-1] DR AGR; HGNC:13664; -. DR CTD; 23499; -. DR DisGeNET; 23499; -. DR GeneCards; MACF1; -. DR HGNC; HGNC:13664; MACF1. DR HPA; ENSG00000127603; Low tissue specificity. DR MalaCards; MACF1; -. DR MIM; 608271; gene. DR MIM; 618325; phenotype. DR neXtProt; NX_Q9UPN3; -. DR OpenTargets; ENSG00000127603; -. DR Orphanet; 572013; Posterior-predominant lissencephaly-broad flat pons and medulla-midline crossing defects syndrome. DR PharmGKB; PA30518; -. DR VEuPathDB; HostDB:ENSG00000127603; -. DR eggNOG; KOG0516; Eukaryota. DR GeneTree; ENSGT00940000155824; -. DR HOGENOM; CLU_000015_1_0_1; -. DR InParanoid; Q9UPN3; -. DR OrthoDB; 5489926at2759; -. DR PhylomeDB; Q9UPN3; -. DR TreeFam; TF335163; -. DR PathwayCommons; Q9UPN3; -. DR SignaLink; Q9UPN3; -. DR SIGNOR; Q9UPN3; -. DR BioGRID-ORCS; 23499; 14 hits in 1153 CRISPR screens. DR ChiTaRS; MACF1; human. DR GeneWiki; MACF1; -. DR GenomeRNAi; 23499; -. DR Pharos; Q9UPN3; Tbio. DR PRO; PR:Q9UPN3; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9UPN3; protein. DR Bgee; ENSG00000127603; Expressed in inferior olivary complex and 210 other tissues. DR ExpressionAtlas; Q9UPN3; baseline and differential. DR Genevisible; Q9UPN3; HS. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; NAS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB. DR GO; GO:0003779; F:actin binding; IDA:UniProtKB. DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0051011; F:microtubule minus-end binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB. DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IBA:GO_Central. DR GO; GO:0045773; P:positive regulation of axon extension; IDA:UniProtKB. DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB. DR GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB. DR GO; GO:0010632; P:regulation of epithelial cell migration; ISS:UniProtKB. DR GO; GO:0051893; P:regulation of focal adhesion assembly; IDA:UniProtKB. DR GO; GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB. DR GO; GO:0150011; P:regulation of neuron projection arborization; ISS:UniProtKB. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0042060; P:wound healing; ISS:UniProtKB. DR CDD; cd21240; CH_MACF1_rpt2; 1. DR CDD; cd21188; CH_PLEC-like_rpt1; 1. DR CDD; cd00051; EFh; 1. DR CDD; cd00176; SPEC; 16. DR Gene3D; 1.20.58.1060; -; 1. DR Gene3D; 1.20.58.60; -; 31. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 3.30.920.20; Gas2-like domain; 1. DR Gene3D; 3.90.1290.10; Plakin repeat; 5. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR041615; Desmoplakin_SH3. DR InterPro; IPR041573; Desmoplakin_Spectrin-like. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR003108; GAR_dom. DR InterPro; IPR036534; GAR_dom_sf. DR InterPro; IPR043197; Plakin. DR InterPro; IPR035915; Plakin_repeat_sf. DR InterPro; IPR001101; Plectin_repeat. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR002017; Spectrin_repeat. DR PANTHER; PTHR23169; ENVOPLAKIN; 1. DR PANTHER; PTHR23169:SF21; EPIPLAKIN; 1. DR Pfam; PF00307; CH; 2. DR Pfam; PF13499; EF-hand_7; 1. DR Pfam; PF02187; GAS2; 1. DR Pfam; PF00681; Plectin; 8. DR Pfam; PF17902; SH3_10; 1. DR Pfam; PF00435; Spectrin; 17. DR Pfam; PF18373; Spectrin_like; 1. DR SMART; SM00033; CH; 2. DR SMART; SM01129; DELLA; 1. DR SMART; SM00054; EFh; 2. DR SMART; SM00243; GAS2; 1. DR SMART; SM00250; PLEC; 20. DR SMART; SM00150; SPEC; 33. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF143575; GAS2 domain-like; 1. DR SUPFAM; SSF75399; Plakin repeat; 6. DR SUPFAM; SSF46966; Spectrin repeat; 31. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS50021; CH; 2. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS50222; EF_HAND_2; 2. DR PROSITE; PS51460; GAR; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; Calcium; KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Disease variant; KW Golgi apparatus; Leucine-rich repeat; Lissencephaly; Membrane; KW Metal-binding; Microtubule; Phosphoprotein; Reference proteome; Repeat; KW SH3 domain; Wnt signaling pathway. FT CHAIN 1..7388 FT /note="Microtubule-actin cross-linking factor 1, isoforms FT 1/2/3/4/5" FT /id="PRO_0000073449" FT DOMAIN 78..181 FT /note="Calponin-homology (CH) 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT REPEAT 148..171 FT /note="LRR 1" FT DOMAIN 194..298 FT /note="Calponin-homology (CH) 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT REPEAT 240..264 FT /note="LRR 2" FT REPEAT 377..399 FT /note="LRR 3" FT REPEAT 441..464 FT /note="LRR 4" FT DOMAIN 868..925 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REPEAT 1050..1073 FT /note="LRR 5" FT REPEAT 1128..1154 FT /note="LRR 6" FT REPEAT 1187..1210 FT /note="LRR 7" FT REPEAT 1257..1282 FT /note="LRR 8" FT REPEAT 1577..1621 FT /note="Plectin 1" FT REPEAT 1654..1696 FT /note="Plectin 2" FT REPEAT 1769..1809 FT /note="Plectin 3" FT REPEAT 1811..1848 FT /note="Plectin 4" FT REPEAT 1855..1886 FT /note="Plectin 5" FT REPEAT 2290..2332 FT /note="Plectin 6" FT REPEAT 2367..2410 FT /note="Plectin 7" FT REPEAT 2411..2437 FT /note="Plectin 8" FT REPEAT 2501..2543 FT /note="Plectin 9" FT REPEAT 2581..2612 FT /note="Plectin 10" FT REPEAT 2686..2730 FT /note="Plectin 11" FT REPEAT 3239..3262 FT /note="LRR 9" FT REPEAT 3264..3283 FT /note="LRR 10" FT REPEAT 3646..3669 FT /note="LRR 11" FT REPEAT 3696..3720 FT /note="LRR 12" FT REPEAT 3883..3957 FT /note="Spectrin 1" FT REPEAT 3936..3958 FT /note="LRR 13" FT REPEAT 4000..4108 FT /note="Spectrin 2" FT REPEAT 4125..4150 FT /note="LRR 14" FT REPEAT 4261..4287 FT /note="LRR 15" FT REPEAT 4466..4574 FT /note="Spectrin 3" FT REPEAT 4511..4534 FT /note="LRR 16" FT REPEAT 4601..4624 FT /note="LRR 17" FT REPEAT 4769..4792 FT /note="LRR 18" FT REPEAT 4800..4904 FT /note="Spectrin 4" FT REPEAT 4909..5012 FT /note="Spectrin 5" FT REPEAT 5051..5076 FT /note="LRR 19" FT REPEAT 5172..5194 FT /note="LRR 20" FT REPEAT 5236..5341 FT /note="Spectrin 6" FT REPEAT 5281..5304 FT /note="LRR 21" FT REPEAT 5348..5450 FT /note="Spectrin 7" FT REPEAT 5455..5557 FT /note="Spectrin 8" FT REPEAT 5695..5719 FT /note="LRR 22" FT REPEAT 5783..5885 FT /note="Spectrin 9" FT REPEAT 5804..5828 FT /note="LRR 23" FT REPEAT 6005..6110 FT /note="Spectrin 10" FT REPEAT 6115..6219 FT /note="Spectrin 11" FT REPEAT 6225..6328 FT /note="Spectrin 12" FT REPEAT 6333..6439 FT /note="Spectrin 13" FT REPEAT 6443..6547 FT /note="Spectrin 14" FT REPEAT 6496..6519 FT /note="LRR 24" FT REPEAT 6552..6658 FT /note="Spectrin 15" FT REPEAT 6665..6766 FT /note="Spectrin 16" FT REPEAT 6771..6874 FT /note="Spectrin 17" FT DOMAIN 7041..7076 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 7077..7112 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 7117..7189 FT /note="GAR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792" FT REGION 1..295 FT /note="Actin-binding" FT REGION 1..47 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2051..2085 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3013..3034 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3104..3174 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3321..3350 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 5583..5603 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 6951..6981 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 7117..7388 FT /note="C-terminal tail" FT /evidence="ECO:0000250" FT REGION 7205..7388 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 7313..7328 FT /note="4 X 4 AA tandem repeats of [GS]-S-R-[AR]" FT COMPBIAS 8..28 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2053..2076 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3125..3164 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 5587..5602 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7224..7303 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7335..7388 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 7054 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7056 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7058 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7060 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7065 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7090 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7092 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7094 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7096 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7101 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:D3ZHV2" FT MOD_RES 35 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0" FT MOD_RES 57 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0" FT MOD_RES 280 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 814 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1122 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1367 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1376 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 2006 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2051 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2077 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0" FT MOD_RES 3122 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0" FT MOD_RES 3331 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 3927 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 4495 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 4496 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 4521 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 4836 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 4962 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 5435 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0" FT MOD_RES 5808 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 6032 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 6210 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 6967 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 7254 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 7279 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 7292 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 7330 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 7333 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0" FT VAR_SEQ 1..1565 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11845288" FT /id="VSP_043626" FT VAR_SEQ 1..72 FT /note="MSSSDEETLSERSCRSERSCRSERSYRSERSGSLSPCPPGDTLPWNLPLHEQ FT KKRKSQDSVLDPAERAVVRV -> MFPVLWAGIPGRDVGSLQPLPPGFKQFCTSASRVA FT VI (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10559237" FT /id="VSP_041390" FT VAR_SEQ 1543..3609 FT /note="Missing (in isoform 2, isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:10529403, FT ECO:0000303|PubMed:10559237, ECO:0000303|PubMed:10574462, FT ECO:0000303|PubMed:9455484" FT /id="VSP_041391" FT VAR_SEQ 4410..4430 FT /note="Missing (in isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:10559237, FT ECO:0000303|PubMed:9455484" FT /id="VSP_041392" FT VAR_SEQ 5497 FT /note="K -> KALEEDIENHATDVHQAVKIGQSLSSLTSPAEQGVLSEKIDSLQARY FT SEIQDRCCRKAALLDQALSNARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHRQH FT ADHL (in isoform 2, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:10529403, FT ECO:0000303|PubMed:10559237, ECO:0000303|PubMed:10574462, FT ECO:0000303|PubMed:11845288" FT /id="VSP_041393" FT VAR_SEQ 7150 FT /note="R -> RFFLGNQ (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11845288" FT /id="VSP_043627" FT VARIANT 302 FT /note="E -> V (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035451" FT VARIANT 4357 FT /note="M -> V (in dbSNP:rs2296172)" FT /evidence="ECO:0000269|PubMed:10559237" FT /id="VAR_048625" FT VARIANT 6201 FT /note="K -> R (in dbSNP:rs682351)" FT /id="VAR_048626" FT VARIANT 6308 FT /note="A -> T (in dbSNP:rs587404)" FT /id="VAR_048627" FT VARIANT 6462 FT /note="E -> Q (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035452" FT VARIANT 6628 FT /note="S -> T (in dbSNP:rs668556)" FT /evidence="ECO:0000269|PubMed:10559237, FT ECO:0000269|PubMed:11845288" FT /id="VAR_048628" FT VARIANT 6664 FT /note="G -> R (in LIS9; unknown pathological significance; FT dbSNP:rs1488808726)" FT /evidence="ECO:0000269|PubMed:30471716" FT /id="VAR_081966" FT VARIANT 6752 FT /note="T -> I (in dbSNP:rs2296174)" FT /id="VAR_048629" FT VARIANT 6855 FT /note="I -> V (in dbSNP:rs12068423)" FT /id="VAR_048630" FT VARIANT 7093 FT /note="G -> E (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_065256" FT VARIANT 7135 FT /note="C -> F (in LIS9; dbSNP:rs1557668270)" FT /evidence="ECO:0000269|PubMed:30471716" FT /id="VAR_081967" FT VARIANT 7186 FT /note="D -> Y (in LIS9; dbSNP:rs1557670503)" FT /evidence="ECO:0000269|PubMed:30471716" FT /id="VAR_081968" FT VARIANT 7188 FT /note="C -> F (in LIS9; dbSNP:rs1557670520)" FT /evidence="ECO:0000269|PubMed:30471716" FT /id="VAR_081969" FT VARIANT 7188 FT /note="C -> G (in LIS9; dbSNP:rs1557670515)" FT /evidence="ECO:0000269|PubMed:30471716" FT /id="VAR_081970" FT CONFLICT 1295..1296 FT /note="TA -> LP (in Ref. 4; AAL39000)" FT /evidence="ECO:0000305" FT CONFLICT 1487 FT /note="T -> A (in Ref. 1; BAA83821 and 4; AAL39000)" FT /evidence="ECO:0000305" FT CONFLICT 3277 FT /note="P -> S (in Ref. 3; AAL38997)" FT /evidence="ECO:0000305" FT CONFLICT 4030 FT /note="V -> A (in Ref. 1; BAA83821)" FT /evidence="ECO:0000305" FT CONFLICT 4119 FT /note="E -> D (in Ref. 1; BAA83821)" FT /evidence="ECO:0000305" FT CONFLICT 4150 FT /note="E -> K (in Ref. 2; AAF06360)" FT /evidence="ECO:0000305" FT CONFLICT 4388 FT /note="C -> Y (in Ref. 1; BAA83821)" FT /evidence="ECO:0000305" FT CONFLICT 4411..4417 FT /note="SILPSVG -> EYRLFKI (in Ref. 5; BAA86565)" FT /evidence="ECO:0000305" FT CONFLICT 4590 FT /note="R -> Q (in Ref. 1; BAA83821)" FT /evidence="ECO:0000305" FT CONFLICT 6791 FT /note="Missing (in Ref. 2; AAF06360)" FT /evidence="ECO:0000305" FT HELIX 75..93 FT /evidence="ECO:0007829|PDB:4Z6G" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:4Z6G" FT TURN 102..108 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 110..120 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 132..148 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 158..162 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 166..180 FT /evidence="ECO:0007829|PDB:4Z6G" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 196..208 FT /evidence="ECO:0007829|PDB:4Z6G" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 221..223 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 227..236 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 243..246 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 251..264 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 273..276 FT /evidence="ECO:0007829|PDB:4Z6G" FT STRAND 277..280 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 283..296 FT /evidence="ECO:0007829|PDB:4Z6G" FT STRAND 302..305 FT /evidence="ECO:0007829|PDB:4Z6G" FT TURN 309..311 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 312..332 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 358..361 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 363..386 FT /evidence="ECO:0007829|PDB:4Z6G" FT HELIX 398..418 FT /evidence="ECO:0007829|PDB:4Z6G" FT STRAND 7024..7026 FT /evidence="ECO:0007829|PDB:5VE9" FT HELIX 7028..7041 FT /evidence="ECO:0007829|PDB:5VE9" FT HELIX 7046..7053 FT /evidence="ECO:0007829|PDB:5VE9" FT STRAND 7058..7062 FT /evidence="ECO:0007829|PDB:5VE9" FT HELIX 7063..7072 FT /evidence="ECO:0007829|PDB:5VE9" FT HELIX 7079..7089 FT /evidence="ECO:0007829|PDB:5VE9" FT STRAND 7094..7098 FT /evidence="ECO:0007829|PDB:5VE9" FT HELIX 7099..7106 FT /evidence="ECO:0007829|PDB:5VE9" FT HELIX 7118..7130 FT /evidence="ECO:0007829|PDB:5X57" FT STRAND 7141..7143 FT /evidence="ECO:0007829|PDB:5X57" FT STRAND 7148..7151 FT /evidence="ECO:0007829|PDB:5X57" FT STRAND 7157..7163 FT /evidence="ECO:0007829|PDB:5X57" FT STRAND 7166..7171 FT /evidence="ECO:0007829|PDB:5X57" FT STRAND 7174..7177 FT /evidence="ECO:0007829|PDB:5X57" FT HELIX 7178..7185 FT /evidence="ECO:0007829|PDB:5X57" FT HELIX 7187..7192 FT /evidence="ECO:0007829|PDB:5X57" SQ SEQUENCE 7388 AA; 838308 MW; B044DC183C048416 CRC64; MSSSDEETLS ERSCRSERSC RSERSYRSER SGSLSPCPPG DTLPWNLPLH EQKKRKSQDS VLDPAERAVV RVADERDRVQ KKTFTKWVNK HLMKVRKHIN DLYEDLRDGH NLISLLEVLS GIKLPREKGR MRFHRLQNVQ IALDFLKQRQ VKLVNIRNDD ITDGNPKLTL GLIWTIILHF QISDIYISGE SGDMSAKEKL LLWTQKVTAG YTGIKCTNFS SCWSDGKMFN ALIHRYRPDL VDMERVQIQS NRENLEQAFE VAERLGVTRL LDAEDVDVPS PDEKSVITYV SSIYDAFPKV PEGGEGISAT EVDSRWQEYQ SRVDSLIPWI KQHTILMSDK TFPQNPVELK ALYNQYIHFK ETEILAKERE KGRIEELYKL LEVWIEFGRI KLPQGYHPND VEEEWGKLII EMLEREKSLR PAVERLELLL QIANKIQNGA LNCEEKLTLA KNTLQADAAH LESGQPVQCE SDVIMYIQEC EGLIRQLQVD LQILRDENYY QLEELAFRVM RLQDELVTLR LECTNLYRKG HFTSLELVPP STLTTTHLKA EPLTKATHSS STSWFRKPMT RAELVAISSS EDEGNLRFVY ELLSWVEEMQ MKLERAEWGN DLPSVELQLE TQQHIHTSVE ELGSSVKEAR LYEGKMSQNF HTSYAETLGK LETQYCKLKE TSSFRMRHLQ SLHKFVSRAT AELIWLNEKE EEELAYDWSD NNSNISAKRN YFSELTMELE EKQDVFRSLQ DTAELLSLEN HPAKQTVEAY SAAVQSQLQW MKQLCLCVEQ HVKENTAYFQ FFSDARELES FLRNLQDSIK RKYSCDHNTS LSRLEDLLQD SMDEKEQLIQ SKSSVASLVG RSKTIVQLKP RSPDHVLKNT ISVKAVCDYR QIEITICKND ECVLEDNSQR TKWKVISPTG NEAMVPSVCF LIPPPNKDAI EMASRVEQSY QKVMALWHQL HVNTKSLISW NYLRKDLDLV QTWNLEKLRS SAPGECHQIM KNLQAHYEDF LQDSRDSVLF SVADRLRLEE EVEACKARFQ HLMKSMENED KEETVAKMYI SELKNIRLRL EEYEQRVVKR IQSLASSRTD RDAWQDNALR IAEQEHTQED LQQLRSDLDA VSMKCDSFLH QSPSSSSVPT LRSELNLLVE KMDHVYGLST VYLNKLKTVD VIVRSIQDAE LLVKGYEIKL SQEEVVLADL SALEAHWSTL RHWLSDVKDK NSVFSVLDEE IAKAKVVAEQ MSRLTPERNL DLERYQEKGS QLQERWHRVI AQLEIRQSEL ESIQEVLGDY RACHGTLIKW IEETTAQQEM MKPGQAEDSR VLSEQLSQQT ALFAEIERNQ TKLDQCQKFS QQYSTIVKDY ELQLMTYKAF VESQQKSPGK RRRMLSSSDA ITQEFMDLRT RYTALVTLTT QHVKYISDAL RRLEEEEKVV EEEKQEHVEK VKELLGWVST LARNTQGKAT SSETKESTDI EKAILEQQVL SEELTTKKEQ VSEAIKTSQI FLAKHGHKLS EKEKKQISEQ LNALNKAYHD LCDGSANQLQ QLQSQLAHQT EQKECRAVAG VIDLGTVEIF PIFKAMQKGL LDQDTGLVLL ESQVIMSGLI APETGENLSL EEGIARNLIN PQMYQQLREL QDALALISRL TESRGPLSVV EAIEKRIISE TVGLKILEAH LATGGFSLSP SENCINLEEA FHQGLISAWL HSVLESYLRT SKNLIDPNTA EKIGLLDLMQ RCIVHQESGF KLLPVKQLAG GMVSLKSGRK VSIFRAVQEG LIDRQVTVRL LEAQLFAGGI VDPRTGHRLT VEEAVRHNLI DQDMACAILI RQLQTGGIID TVTGQRLTID EAVSNDLVAA KIALVILESL WSFMGLLWPE SGEILPITDA LEQGIVSTEL AHKILSNRQH IKALFLPATT EILSWKKAIE SGILDRDLAN NLKSICIPDV MPHMQLADSA EQNINPGAAV LPCSKSHPKA TASQSENLLF QLMTHSYINV QNGQRLLLLD KELMETLTSR DEYQTSPPKV VEIGHQRQKT PEGLQESANV KISGTFSSGW TVRLPEFQFS SQNKEYPDRE DCTTEKGKKT TVETEDSSVE NPEQDLFVEQ KERNPNIDAL KVINKVKLEV QRQLIGTQRE DQTAVSVREN ASRGHLLTIP PAEAEGVPLV VDKDVFSVET PKKEHQPLRN TSFTCQNEQA HTLETEYIHD ETGGSHIKPQ SKKLQVQVKK TLGIKLELKS ETDGNVHPLD KKEMLKKTFL AKDDHKESQE AQNIAGGSMM MSEKTDEEDS GREIFLSCSH PLELLEEATL NVLSAQLLDG GIFHEQTGQK LLLNEAISRG IVPSHTAVKL MEKLNMFQGF FDSQTCESLT TEEVINEGLM DEKLLHNVLM ADKAISGVLD PRTQTLCSVK DAVTVGLLDK ETATRILERQ VVTGGIIDLK RGKKVSVTLA STLGLVDVAD QPELINLEKA SKGRDAEKTV RERLISLQME TTGLIDPDSK APLTVVQSID RGLLEREEAV RLLTKQVVDG GIIHHISGMR LSVDNAFRHG LIGEDLAEKL KRVENLNIHQ IFNPETKENI SLPKAIKLDL ITSDLKREIQ EVQAFTGNFV DLISGQRLTL AEAKKEGLLT NEAVLSPGMM HGIVDPENCR IVPYSELVKK CKIDIESGQR YLEVIPFSDI KDGVSDKVLT LSQAIQLGKV DFASTLKVLE AQANTGGIID TATGKRLTLA SALEEKLVDE NMVRIIASHQ VLNGGIVDIF SDQRVTLVEA IEKRLISPEL ANMIQIDSSE FSDHRAQIEK QEGIEVCALQ NEFLGKDMLI ACNQTAEMSC NKVEESERLF QVENQSAQEK VKVRVSDGEQ AKKSREISLK EFGCKDQRKP RMSSDAKEFI SIINPHNLKG KSLGQVSLTH PYSECDFKLK EVARNNMGND TNEEQEKAVT KIEIISHMKQ STSCLDSEEI RENQGEVILE VQETYCETSG KLPSEQVLQQ PMNARVKSKR EKREVIVEES IRTCKPAFLS EEKLYQETAI RDEHDSHIKS QPREMTSSEK GKEADTEMGF SITFKIEESS SQVVPQGISV KHLDALTLFS SKQANEGKVN NLSLCLTLKP EENLSREIAC GAQSEPFPCM TPRPEGLHYQ ESDGKAQVTG PSQISKTDKS FQGTTRQETN YQDSWVTSKT KETKHQISSS NECKEKSYQE VSFDPARGLK LEEITVSRPD SKEVRYLEFS DRKDLHHQGS KSDDKLCGTL KSEIATQELT GEKFLEMANP NVAGLEAGSI EDIVTQRGSR VLGSFLPEKL FKGVSQKENT GQQNAIISPT VLETSEEKTV SLTVCSAVKT EKTPQEKLRE SPGSEQTPFM TAPEGKGNGG VNPEPFRATQ NVFTRQLCLE HDEKLVSYLS LLRNIEMRTK QIQPLELNLA ELQDLLCQAK VLERELKDLT TLVSQELECV NQIIISQPQE VPAQLLKALE KDAKNLQKSL SSVSDTWNSR LLHFQNAVEI EKTKVLNQHT QLEGRLQDLR AWVGNKNLIL NSKGSNSEID VDSLNLCLQQ YEDLKQPMAE RKAQLDALAF DIQFFISEHA QDLSPQQNRQ MLRLLNELQR SFQDILEQTA AQVDALQGHL QQMEQEALVK TLQKQQNTCH QQLEDLCSWV GQAERALAGH QGRTTQQDLS ALQKNQSDLK DLQDDIQNRA TSFATVVKDI EGFMEENQTK LSPRELTALR EKLHQAKEQY EALQEETRVA QKELEEAVTS ALQQETEKSK AAKELAENKK KIDALLDWVT SVGSSGGQLL TNLPGMEQLS GASLEKGALD TTDGYMGVNQ APEKLDKQCE MMKARHQELL SQQQNFILAT QSAQAFLDQH GHNLTPEEQQ MLQQKLGELK EQYSTSLAQS EAELKQVQTL QDELQKFLQD HKEFESWLER SEKELENMHK GGSSPETLPS LLKRQGSFSE DVISHKGDLR FVTISGQKVL DMENSFKEGK EPSEIGNLVK DKLKDATERY TALHSKCTRL GSHLNMLLGQ YHQFQNSADS LQAWMQACEA NVEKLLSDTV ASDPGVLQEQ LATTKQLQEE LAEHQVPVEK LQKVARDIME IEGEPAPDHR HVQETTDSIL SHFQSLSYSL AERSSLLQKA IAQSQSVQES LESLLQSIGE VEQNLEGKQV SSLSSGVIQE ALATNMKLKQ DIARQKSSLE ATREMVTRFM ETADSTTAAV LQGKLAEVSQ RFEQLCLQQQ EKESSLKKLL PQAEMFEHLS GKLQQFMENK SRMLASGNQP DQDITHFFQQ IQELNLEMED QQENLDTLEH LVTELSSCGF ALDLCQHQDR VQNLRKDFTE LQKTVKEREK DASSCQEQLD EFRKLVRTFQ KWLKETEGSI PPTETSMSAK ELEKQIEHLK SLLDDWASKG TLVEEINCKG TSLENLIMEI TAPDSQGKTG SILPSVGSSV GSVNGYHTCK DLTEIQCDMS DVNLKYEKLG GVLHERQESL QAILNRMEEV HKEANSVLQW LESKEEVLKS MDAMSSPTKT ETVKAQAESN KAFLAELEQN SPKIQKVKEA LAGLLVTYPN SQEAENWKKI QEELNSRWER ATEVTVARQR QLEESASHLA CFQAAESQLR PWLMEKELMM GVLGPLSIDP NMLNAQKQQV QFMLKEFEAR RQQHEQLNEA AQGILTGPGD VSLSTSQVQK ELQSINQKWV ELTDKLNSRS SQIDQAIVKS TQYQELLQDL SEKVRAVGQR LSVQSAISTQ PEAVKQQLEE TSEIRSDLEQ LDHEVKEAQT LCDELSVLIG EQYLKDELKK RLETVALPLQ GLEDLAADRI NRLQAALAST QQFQQMFDEL RTWLDDKQSQ QAKNCPISAK LERLQSQLQE NEEFQKSLNQ HSGSYEVIVA EGESLLLSVP PGEEKRTLQN QLVELKNHWE ELSKKTADRQ SRLKDCMQKA QKYQWHVEDL VPWIEDCKAK MSELRVTLDP VQLESSLLRS KAMLNEVEKR RSLLEILNSA ADILINSSEA DEDGIRDEKA GINQNMDAVT EELQAKTGSL EEMTQRLREF QESFKNIEKK VEGAKHQLEI FDALGSQACS NKNLEKLRAQ QEVLQALEPQ VDYLRNFTQG LVEDAPDGSD ASQLLHQAEV AQQEFLEVKQ RVNSGCVMME NKLEGIGQFH CRVREMFSQL ADLDDELDGM GAIGRDTDSL QSQIEDVRLF LNKIHVLKLD IEASEAECRH MLEEEGTLDL LGLKRELEAL NKQCGKLTER GKARQEQLEL TLGRVEDFYR KLKGLNDATT AAEEAEALQW VVGTEVEIIN QQLADFKMFQ KEQVDPLQMK LQQVNGLGQG LIQSAGKDCD VQGLEHDMEE INARWNTLNK KVAQRIAQLQ EALLHCGKFQ DALEPLLSWL ADTEELIANQ KPPSAEYKVV KAQIQEQKLL QRLLDDRKAT VDMLQAEGGR IAQSAELADR EKITGQLESL ESRWTELLSK AAARQKQLED ILVLAKQFHE TAEPISDFLS VTEKKLANSE PVGTQTAKIQ QQIIRHKALN EEIVNRKKNV DQAIKNGQAL LKQTTGEEVL LIQEKLDGIK TRYADITVTS SKALRTLEQA RQLATKFQST YEELTGWLRE VEEELATSGG QSPTGEQIPQ FQQRQKELKK EVMEHRLVLD TVNEVSRALL ELVPWRAREG LDKLVSDANE QYKLVSDTIG QRVDEIDAAI QRSQQYEQAA DAELAWVAET KRKLMALGPI RLEQDQTTAQ LQVQKAFSID IIRHKDSMDE LFSHRSEIFG TCGEEQKTVL QEKTESLIQQ YEAISLLNSE RYARLERAQV LVNQFWETYE ELSPWIEETR ALIAQLPSPA IDHEQLRQQQ EEMRQLRESI AEHKPHIDKL LKIGPQLKEL NPEEGEMVEE KYQKAENMYA QIKEEVRQRA LALDEAVSQS TQITEFHDKI EPMLETLENL SSRLRMPPLI PAEVDKIREC ISDNKSATVE LEKLQPSFEA LKRRGEELIG RSQGADKDLA AKEIQDKLDQ MVFFWEDIKA RAEEREIKFL DVLELAEKFW YDMAALLTTI KDTQDIVHDL ESPGIDPSII KQQVEAAETI KEETDGLHEE LEFIRILGAD LIFACGETEK PEVRKSIDEM NNAWENLNKT WKERLEKLED AMQAAVQYQD TLQAMFDWLD NTVIKLCTMP PVGTDLNTVK DQLNEMKEFK VEVYQQQIEM EKLNHQGELM LKKATDETDR DIIREPLTEL KHLWENLGEK IAHRQHKLEG ALLALGQFQH ALEELMSWLT HTEELLDAQR PISGDPKVIE VELAKHHVLK NDVLAHQATV ETVNKAGNEL LESSAGDDAS SLRSRLEAMN QCWESVLQKT EEREQQLQST LQQAQGFHSE IEDFLLELTR MESQLSASKP TGGLPETARE QLDTHMELYS QLKAKEETYN QLLDKGRLML LSRDDSGSGS KTEQSVALLE QKWHVVSSKM EERKSKLEEA LNLATEFQNS LQEFINWLTL AEQSLNIASP PSLILNTVLS QIEEHKVFAN EVNAHRDQII ELDQTGNQLK FLSQKQDVVL IKNLLVSVQS RWEKVVQRSI ERGRSLDDAR KRAKQFHEAW KKLIDWLEDA ESHLDSELEI SNDPDKIKLQ LSKHKEFQKT LGGKQPVYDT TIRTGRALKE KTLLPEDSQK LDNFLGEVRD KWDTVCGKSV ERQHKLEEAL LFSGQFMDAL QALVDWLYKV EPQLAEDQPV HGDLDLVMNL MDAHKVFQKE LGKRTGTVQV LKRSGRELIE NSRDDTTWVK GQLQELSTRW DTVCKLSVSK QSRLEQALKQ AEVFRDTVHM LLEWLSEAEQ TLRFRGALPD DTEALQSLID THKEFMKKVE EKRVDVNSAV AMGEVILAVC HPDCITTIKH WITIIRARFE EVLTWAKQHQ QRLETALSEL VANAELLEEL LAWIQWAETT LIQRDQEPIP QNIDRVKALI AEHQTFMEEM TRKQPDVDRV TKTYKRKNIE PTHAPFIEKS RSGGRKSLSQ PTPPPMPILS QSEAKNPRIN QLSARWQQVW LLALERQRKL NDALDRLEEL KEFANFDFDV WRKKYMRWMN HKKSRVMDFF RRIDKDQDGK ITRQEFIDGI LASKFPTTKL EMTAVADIFD RDGDGYIDYY EFVAALHPNK DAYRPTTDAD KIEDEVTRQV AQCKCAKRFQ VEQIGENKYR FGDSQQLRLV RILRSTVMVR VGGGWMALDE FLVKNDPCRA RGRTNIELRE KFILPEGASQ GMTPFRSRGR RSKPSSRAAS PTRSSSSASQ SNHSCTSMPS SPATPASGTK VIPSSGSKLK RPTPTFHSSR TSLAGDTSNS SSPASTGAKT NRADPKKSAS RPGSRAGSRA GSRASSRRGS DASDFDLLET QSACSDTSES SAAGGQGNSR RGLNKPSKIP TMSKKTTTAS PRTPGPKR //