MYO3B_HUMAN
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 03-AUG-2022, entry version 172.
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}.
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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; 14.
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; Q8WXR4; -.
DR PeptideAtlas; Q8WXR4; -.
DR PRIDE; 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; 165 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 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; GKDMALQ; -.
DR OrthoDB; 36742at2759; -.
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 1108 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 60 other tissues.
DR ExpressionAtlas; Q8WXR4; baseline and differential.
DR Genevisible; Q8WXR4; HS.
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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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 Gene3D; 3.40.850.10; -; 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 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; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
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; AAL57233/AAO13799/AAO13800/
FT 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
