ID MYO3B_HUMAN Reviewed; 1341 AA. AC Q8WXR4; B8ZZR2; Q53QE1; Q53T08; Q8IX64; Q8IX65; Q8IX66; Q8IX67; Q8IX68; AC Q96N94; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 4. DT 24-JAN-2024, entry version 180. DE RecName: Full=Myosin-IIIb; DE EC=2.7.11.1; GN Name=MYO3B; 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] (ISOFORMS 1; 2; 3; 4; 5 AND 6), ALTERNATIVE RP SPLICING, AND VARIANT LYS-1082. RX PubMed=11991710; DOI=10.1006/geno.2002.6749; RA Dose A.C., Burnside B.; RT "A class III myosin expressed in the retina is a potential candidate for RT Bardet-Biedl syndrome."; RL Genomics 79:621-624(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1104 (ISOFORM 7), AND VARIANTS RP GLU-309; ILE-770; GLY-773 AND LYS-1082. RC TISSUE=Kidney; 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 [4] RP VARIANTS [LARGE SCALE ANALYSIS] SER-21; HIS-185; SER-267; VAL-275; GLU-309; RP LEU-316; GLN-352; SER-388; THR-406; PRO-638; ILE-770; GLY-773; GLN-918; RP CYS-969; CYS-990; VAL-1092; ILE-1137 AND CYS-1165. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Probable actin-based motor with a protein kinase activity. CC Required for normal cochlear hair bundle development and hearing. Plays CC an important role in the early steps of cochlear hair bundle CC morphogenesis. Influences the number and lengths of stereocilia to be CC produced and limits the growth of microvilli within the forming CC auditory hair bundles thereby contributing to the architecture of the CC hair bundle, including its staircase pattern. Involved in the CC elongation of actin in stereocilia tips by transporting the actin CC regulatory factor ESPN to the plus ends of actin filaments. CC {ECO:0000250|UniProtKB:Q1EG27}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; CC -!- SUBUNIT: Interacts (via C-terminus) with ESPN. Interacts (via C- CC terminus) with ESPNL. {ECO:0000250|UniProtKB:Q1EG27}. CC -!- INTERACTION: CC Q8WXR4; P08238: HSP90AB1; NbExp=2; IntAct=EBI-350672, EBI-352572; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection, CC stereocilium {ECO:0000250|UniProtKB:Q1EG27}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=MYO3B.2; CC IsoId=Q8WXR4-1; Sequence=Displayed; CC Name=2; Synonyms=MYO3B.0; CC IsoId=Q8WXR4-2; Sequence=VSP_010163; CC Name=3; Synonyms=MYO3B.1; CC IsoId=Q8WXR4-3; Sequence=VSP_010162, VSP_010163; CC Name=4; Synonyms=MYO3B.3; CC IsoId=Q8WXR4-4; Sequence=VSP_010162; CC Name=5; Synonyms=MYO3B.4; CC IsoId=Q8WXR4-5; Sequence=VSP_010164; CC Name=6; Synonyms=MYO3B.5; CC IsoId=Q8WXR4-6; Sequence=VSP_010165; CC Name=7; CC IsoId=Q8WXR4-7; Sequence=VSP_023111; CC -!- TISSUE SPECIFICITY: Expressed in retina, kidney and testis. CC -!- SIMILARITY: In the C-terminal section; belongs to the TRAFAC class CC myosin-kinesin ATPase superfamily. Myosin family. {ECO:0000305}. CC -!- SIMILARITY: In the N-terminal section; belongs to the protein kinase CC superfamily. STE Ser/Thr protein kinase family. {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; AF369908; AAL57233.1; -; mRNA. DR EMBL; AF391554; AAO13799.1; -; mRNA. DR EMBL; AF391555; AAO13800.1; -; mRNA. DR EMBL; AF391556; AAO13801.1; -; mRNA. DR EMBL; AF391557; AAO13802.1; -; mRNA. DR EMBL; AF391558; AAO13803.1; -; mRNA. DR EMBL; AC007277; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC012594; AAY24324.1; -; Genomic_DNA. DR EMBL; AC068280; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC093402; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC114794; AAY24159.1; -; Genomic_DNA. DR EMBL; AK055778; BAB71011.1; -; mRNA. DR CCDS; CCDS42773.1; -. [Q8WXR4-1] DR CCDS; CCDS46446.1; -. [Q8WXR4-4] DR RefSeq; NP_001077084.2; NM_001083615.3. [Q8WXR4-4] DR RefSeq; NP_620482.3; NM_138995.4. [Q8WXR4-1] DR RefSeq; XP_006712362.1; XM_006712299.3. [Q8WXR4-7] DR AlphaFoldDB; Q8WXR4; -. DR SMR; Q8WXR4; -. DR BioGRID; 126621; 47. DR IntAct; Q8WXR4; 37. DR STRING; 9606.ENSP00000386213; -. DR BindingDB; Q8WXR4; -. DR ChEMBL; CHEMBL5654; -. DR DrugCentral; Q8WXR4; -. DR iPTMnet; Q8WXR4; -. DR PhosphoSitePlus; Q8WXR4; -. DR BioMuta; MYO3B; -. DR DMDM; 296439486; -. DR MassIVE; Q8WXR4; -. DR MaxQB; Q8WXR4; -. DR PaxDb; 9606-ENSP00000386213; -. DR PeptideAtlas; Q8WXR4; -. DR ProteomicsDB; 75080; -. [Q8WXR4-1] DR ProteomicsDB; 75081; -. [Q8WXR4-2] DR ProteomicsDB; 75082; -. [Q8WXR4-3] DR ProteomicsDB; 75083; -. [Q8WXR4-4] DR ProteomicsDB; 75084; -. [Q8WXR4-5] DR ProteomicsDB; 75085; -. [Q8WXR4-6] DR ProteomicsDB; 75086; -. [Q8WXR4-7] DR Antibodypedia; 33828; 184 antibodies from 27 providers. DR DNASU; 140469; -. DR Ensembl; ENST00000317935.10; ENSP00000314650.6; ENSG00000071909.19. [Q8WXR4-3] DR Ensembl; ENST00000408978.9; ENSP00000386213.4; ENSG00000071909.19. [Q8WXR4-1] DR Ensembl; ENST00000409044.7; ENSP00000386497.3; ENSG00000071909.19. [Q8WXR4-4] DR GeneID; 140469; -. DR KEGG; hsa:140469; -. DR MANE-Select; ENST00000408978.9; ENSP00000386213.4; NM_138995.5; NP_620482.3. DR UCSC; uc002ufy.4; human. [Q8WXR4-1] DR AGR; HGNC:15576; -. DR CTD; 140469; -. DR DisGeNET; 140469; -. DR GeneCards; MYO3B; -. DR HGNC; HGNC:15576; MYO3B. DR HPA; ENSG00000071909; Tissue enhanced (epididymis, kidney, parathyroid gland, retina). DR MIM; 610040; gene. DR neXtProt; NX_Q8WXR4; -. DR OpenTargets; ENSG00000071909; -. DR PharmGKB; PA31406; -. DR VEuPathDB; HostDB:ENSG00000071909; -. DR eggNOG; KOG0587; Eukaryota. DR eggNOG; KOG4229; Eukaryota. DR GeneTree; ENSGT00940000159309; -. DR InParanoid; Q8WXR4; -. DR OMA; QPDKNIW; -. DR OrthoDB; 1094820at2759; -. DR PhylomeDB; Q8WXR4; -. DR TreeFam; TF326512; -. DR PathwayCommons; Q8WXR4; -. DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea. DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea. DR SignaLink; Q8WXR4; -. DR BioGRID-ORCS; 140469; 6 hits in 1186 CRISPR screens. DR ChiTaRS; MYO3B; human. DR GenomeRNAi; 140469; -. DR Pharos; Q8WXR4; Tchem. DR PRO; PR:Q8WXR4; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8WXR4; Protein. DR Bgee; ENSG00000071909; Expressed in buccal mucosa cell and 61 other cell types or tissues. DR ExpressionAtlas; Q8WXR4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0032433; C:filopodium tip; IBA:GO_Central. DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW. DR GO; GO:0001917; C:photoreceptor inner segment; IBA:GO_Central. DR GO; GO:0032426; C:stereocilium tip; ISS:UniProtKB. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0090103; P:cochlea morphogenesis; ISS:UniProtKB. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0051491; P:positive regulation of filopodium assembly; IBA:GO_Central. DR GO; GO:0030832; P:regulation of actin filament length; IBA:GO_Central. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR CDD; cd01379; MYSc_Myo3; 1. DR CDD; cd06639; STKc_myosinIIIB_N; 1. DR Gene3D; 1.10.10.820; -; 1. DR Gene3D; 1.20.5.190; -; 1. DR Gene3D; 1.20.58.530; -; 1. DR Gene3D; 6.20.240.20; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR036961; Kinesin_motor_dom_sf. DR InterPro; IPR001609; Myosin_head_motor_dom. DR InterPro; IPR036083; MYSc_Myo3. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR46256; AGAP011099-PA; 1. DR PANTHER; PTHR46256:SF1; MYOSIN-IIIB; 1. DR Pfam; PF00612; IQ; 1. DR Pfam; PF00063; Myosin_head; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR00193; MYOSINHEAVY. DR SMART; SM00015; IQ; 2. DR SMART; SM00242; MYSc; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50096; IQ; 2. DR PROSITE; PS51456; MYOSIN_MOTOR; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q8WXR4; HS. PE 1: Evidence at protein level; KW Actin-binding; Alternative splicing; ATP-binding; Cell projection; KW Cytoplasm; Cytoskeleton; Hearing; Kinase; Motor protein; Myosin; KW Nucleotide-binding; Reference proteome; Repeat; Sensory transduction; KW Serine/threonine-protein kinase; Transferase; Vision. FT CHAIN 1..1341 FT /note="Myosin-IIIb" FT /id="PRO_0000086415" FT DOMAIN 27..293 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 343..1058 FT /note="Myosin motor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" FT DOMAIN 1060..1089 FT /note="IQ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT DOMAIN 1087..1116 FT /note="IQ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT REGION 939..961 FT /note="Actin-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" FT REGION 1111..1205 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1232..1266 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1318..1341 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1116..1137 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1149..1171 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1172..1201 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1323..1341 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 156 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 33..41 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 56 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT VAR_SEQ 1 FT /note="M -> MLQSALLSTR (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023111" FT VAR_SEQ 1097..1123 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:11991710" FT /id="VSP_010162" FT VAR_SEQ 1193..1341 FT /note="HSQAQSSPKGCDIFAGHANKHSVSGTDLLSSRICHPAPDQQGLSLWGAPQKP FT GSENGLAQKHRTPRRRCQQPKMLSSPEDTMYYNQLNGTLEYQGSKRKPRKLGQIKVLDG FT EDEYYKSLSPVDCIPEENNSAHPSFFSSSSKGDSFAQH -> WSFTLLLRLECNSMISA FT DCNLRPLGSSDSPASASRVAGITGIHKPRVLQKGAISSQDMQTSTRFLGLICCLLGYAI FT LLQISKD (in isoform 5)" FT /evidence="ECO:0000303|PubMed:11991710" FT /id="VSP_010164" FT VAR_SEQ 1193..1341 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:11991710" FT /id="VSP_010165" FT VAR_SEQ 1245..1341 FT /note="GSENGLAQKHRTPRRRCQQPKMLSSPEDTMYYNQLNGTLEYQGSKRKPRKLG FT QIKVLDGEDEYYKSLSPVDCIPEENNSAHPSFFSSSSKGDSFAQH -> AFPHYGCNFY FT GFRKWSCTEASNTSPTMSAAQNAE (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:11991710" FT /id="VSP_010163" FT VARIANT 21 FT /note="P -> S (in dbSNP:rs35391761)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040886" FT VARIANT 185 FT /note="R -> H (in dbSNP:rs55911154)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040887" FT VARIANT 267 FT /note="N -> S (in dbSNP:rs34509373)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040888" FT VARIANT 275 FT /note="I -> V (in dbSNP:rs10209102)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_030605" FT VARIANT 309 FT /note="K -> E (in dbSNP:rs4668246)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17344846" FT /id="VAR_030606" FT VARIANT 316 FT /note="H -> L (in dbSNP:rs55633190)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040889" FT VARIANT 352 FT /note="E -> Q (in dbSNP:rs56179904)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040890" FT VARIANT 388 FT /note="N -> S (in dbSNP:rs34273653)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040891" FT VARIANT 406 FT /note="A -> T (in dbSNP:rs10168181)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_030607" FT VARIANT 638 FT /note="Q -> P (in dbSNP:rs55911627)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040892" FT VARIANT 770 FT /note="V -> I (in dbSNP:rs6736609)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17344846" FT /id="VAR_030608" FT VARIANT 773 FT /note="E -> G (in dbSNP:rs33962844)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17344846" FT /id="VAR_040893" FT VARIANT 798 FT /note="E -> K (in dbSNP:rs11892763)" FT /id="VAR_030609" FT VARIANT 918 FT /note="R -> Q (in dbSNP:rs55769829)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040894" FT VARIANT 969 FT /note="S -> C (in dbSNP:rs35857918)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040895" FT VARIANT 990 FT /note="R -> C (in dbSNP:rs34236931)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040896" FT VARIANT 1082 FT /note="R -> K (in dbSNP:rs10185178)" FT /evidence="ECO:0000269|PubMed:11991710, FT ECO:0000269|PubMed:14702039" FT /id="VAR_030610" FT VARIANT 1092 FT /note="I -> V (in dbSNP:rs34219776)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040897" FT VARIANT 1137 FT /note="V -> I (in dbSNP:rs34546065)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040898" FT VARIANT 1165 FT /note="R -> C (in dbSNP:rs56052422)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040899" FT CONFLICT 261 FT /note="K -> R (in Ref. 3; BAB71011)" FT /evidence="ECO:0000305" FT CONFLICT 573 FT /note="T -> A (in Ref. 3; BAB71011)" FT /evidence="ECO:0000305" FT CONFLICT 870 FT /note="K -> M (in Ref. 1; FT AAL57233/AAO13799/AAO13800/AAO13801/AAO13802/AAO13803)" FT /evidence="ECO:0000305" FT CONFLICT 1081 FT /note="K -> N (in Ref. 3; BAB71011)" FT /evidence="ECO:0000305" SQ SEQUENCE 1341 AA; 151829 MW; 76F84C571DAA269D CRC64; MKHLYGLFHY NPMMLGLESL PDPTDTWEII ETIGKGTYGK VYKVTNKRDG SLAAVKILDP VSDMDEEIEA EYNILQFLPN HPNVVKFYGM FYKADHCVGG QLWLVLELCN GGSVTELVKG LLRCGQRLDE AMISYILYGA LLGLQHLHNN RIIHRDVKGN NILLTTEGGV KLVDFGVSAQ LTSTRLRRNT SVGTPFWMAP EVIACEQQYD SSYDARCDVW SLGITAIELG DGDPPLFDMH PVKTLFKIPR NPPPTLLHPE KWCEEFNHFI SQCLIKDFER RPSVTHLLDH PFIKGVHGKV LFLQKQLAKV LQDQKHQNPV AKTRHERMHT RRPYHVEDAE KYCLEDDLVN LEVLDEDTII HQLQKRYADL LIYTYVGDIL IALNPFQNLS IYSPQFSRLY HGVKRASNPP HIFASADAAY QCMVTLSKDQ CIVISGESGS GKTESAHLIV QHLTFLGKAN NQTLREKILQ VNSLVEAFGN SCTAINDNSS RFGKYLEMMF TPTGVVMGAR ISEYLLEKSR VIKQAAREKN FHIFYYIYAG LHHQKKLSDF RLPEEKPPRY IADETGRVMH DITSKESYRR QFEAIQHCFR IIGFTDKEVH SVYRILAGIL NIGNIEFAAI SSQHQTDKSE VPNAEALQNA ASVLCISPEE LQEALTSHCV VTRGETIIRA NTVDRAADVR DAMSKALYGR LFSWIVNRIN TLLQPDENIC SAGGGMNVGI LDIFGFENFQ RNSFEQLCIN IANEQIQYYF NQHVFALEQM EYQNEGIDAV PVEYEDNRPL LDMFLQKPLG LLALLDEESR FPQATDQTLV DKFEDNLRCK YFWRPKGVEL CFGIQHYAGK VLYDASGVLE KNRDTLPADV VVVLRTSENK LLQQLFSIPL TKTGNLAQTR ARITVASSSL PPHFSAGKAK VDTLEVIRHP EETTNMKRQT VASYFRYSLM DLLSKMVVGQ PHFVRCIKPN DDREALQFSR ERVLAQLRST GILETVSIRR QGYSHRILFE EFVKRYYYLA FTAHQTPLAS KESCVAILEK SRLDHWVLGK TKVFLKYYHV EQLNLLLREV IGRVVVLQAY TKGWLGARRY KRVREKREKG AIAIQSAWRG YDARRKFKKI SNRRNESAAH NQAGDTSNQS SGPHSPVAAG TRGSAEVQDC SEPGDHKVLR GSVHRRSHSQ AESNNGRTQT SSNSPAVTEK NGHSQAQSSP KGCDIFAGHA NKHSVSGTDL LSSRICHPAP DQQGLSLWGA PQKPGSENGL AQKHRTPRRR CQQPKMLSSP EDTMYYNQLN GTLEYQGSKR KPRKLGQIKV LDGEDEYYKS LSPVDCIPEE NNSAHPSFFS SSSKGDSFAQ H //