MYO5A_HUMAN
ID MYO5A_HUMAN Reviewed; 1855 AA.
AC Q9Y4I1; A8MZC5; O60653; Q07902; Q16249; Q9UE30; Q9UE31;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Unconventional myosin-Va;
DE AltName: Full=Dilute myosin heavy chain, non-muscle;
DE AltName: Full=Myosin heavy chain 12;
DE AltName: Full=Myosin-12;
DE AltName: Full=Myoxin;
GN Name=MYO5A; Synonyms=MYH12;
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 AND 2).
RC TISSUE=Skin;
RA Meurers B.H., Zimmermann R., Vosberg H.P.;
RT "The complete cDNA for human myosin heavy chain 12, a class V myosin.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT CYS-1246.
RX PubMed=9207796; DOI=10.1038/ng0797-289;
RA Pastural E., Barrat F.J., Dufourcq-Lagelouse R., Certain S., Sanal O.,
RA Jabado N., Seger R., Griscelli C., Fischer A., de Saint Basile G.;
RT "Griscelli disease maps to chromosome 15q21 and is associated with
RT mutations in the myosin-Va gene.";
RL Nat. Genet. 16:289-292(1997).
RN [3]
RP ERRATUM OF PUBMED:9207796.
RA Pastural E., Barrat F.J., Dufourcq-Lagelouse R., Certain S., Sanal O.,
RA Jabado N., Seger R., Griscelli C., Fischer A., de Saint Basile G.;
RL Nat. Genet. 23:373-373(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 638-1477 (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=8188282; DOI=10.1006/geno.1994.1088;
RA Engle L.J., Kennett R.H.;
RT "Cloning, analysis, and chromosomal localization of myoxin (MYH12), the
RT human homologue to the mouse dilute gene.";
RL Genomics 19:407-416(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1061-1498 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=7835087; DOI=10.1159/000133937;
RA Moore K.J., Testa J.R., Francke U., Milatovich A., Copeland N.G.,
RA Jenkins N.A.;
RT "Cloning and regional assignment of the human myosin heavy chain 12 (MYH12)
RT gene to chromosome band 15q21.";
RL Cytogenet. Cell Genet. 69:53-58(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1358-1460 (ISOFORM 3).
RA Edgar A.J., Bennett J.P.;
RT "Inhibition of dendrite formation in melanocytes transiently transfected
RT with antisense DNA to myosin V.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX PubMed=10448864; DOI=10.1038/23072;
RA Mehta A.D., Rock R.S., Rief M., Spudich J.A., Mooseker M.S., Cheney R.E.;
RT "Myosin-V is a processive actin-based motor.";
RL Nature 400:590-593(1999).
RN [9]
RP INTERACTION WITH MLPH.
RX PubMed=12062444; DOI=10.1016/s0014-5793(02)02634-0;
RA Nagashima K., Torii S., Yi Z., Igarashi M., Okamoto K., Takeuchi T.,
RA Izumi T.;
RT "Melanophilin directly links Rab27a and myosin Va through its distinct
RT coiled-coil regions.";
RL FEBS Lett. 517:233-238(2002).
RN [10]
RP IDENTIFICATION BY 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 [11]
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 [12]
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1452, AND IDENTIFICATION BY
RP 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 [14]
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 [15]
RP INTERACTION WITH RAB10.
RX PubMed=22908308; DOI=10.1083/jcb.201111091;
RA Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S.,
RA Hammer J.A., Xu T., Lippincott-Schwartz J.;
RT "Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle
RT translocation in adipocytes.";
RL J. Cell Biol. 198:545-560(2012).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600 AND SER-1652, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [18]
RP VARIANT CYS-1246.
RX PubMed=10733681; DOI=10.1046/j.1523-1747.2000.00933.x;
RA Lambert J., Naeyaert J.-M., De Paepe A., Van Coster R., Ferster A.,
RA Song M., Messiaen L.;
RT "Arg-Cys substitution at codon 1246 of the human myosin Va gene is not
RT associated with Griscelli syndrome.";
RL J. Invest. Dermatol. 114:731-733(2000).
RN [19]
RP INVOLVEMENT IN GS1.
RX PubMed=10704277; DOI=10.1006/geno.1999.6081;
RA Pastural E., Ersoy F., Yalman N., Wulffraat N., Grillo E., Ozkinay F.,
RA Tezcan I., Gedikoglu G., Philippe N., Fischer A., de Saint Basile G.;
RT "Two genes are responsible for Griscelli syndrome at the same 15q21
RT locus.";
RL Genomics 63:299-306(2000).
RN [20]
RP INVOLVEMENT IN ELEJAS.
RX PubMed=12058346; DOI=10.1086/341606;
RA Anikster Y., Huizing M., Anderson P.D., Fitzpatrick D.L., Klar A.,
RA Gross-Kieselstein E., Berkun Y., Shazberg G., Gahl W.A., Hurvitz H.;
RT "Evidence that Griscelli syndrome with neurological involvement is caused
RT by mutations in RAB27A, not MYO5A.";
RL Am. J. Hum. Genet. 71:407-414(2002).
RN [21]
RP ERRATUM OF PUBMED:12058346.
RA Anikster Y., Huizing M., Anderson P.D., Fitzpatrick D.L., Klar A.,
RA Gross-Kieselstein E., Berkun Y., Shazberg G., Gahl W.A., Hurvitz H.;
RL Am. J. Hum. Genet. 71:1007-1007(2002).
RN [22]
RP INVOLVEMENT IN GS3.
RX PubMed=12897212; DOI=10.1172/jci200318264;
RA Menasche G., Ho C.H., Sanal O., Feldmann J., Tezcan I., Ersoy F.,
RA Houdusse A., Fischer A., de Saint Basile G.;
RT "Griscelli syndrome restricted to hypopigmentation results from a
RT melanophilin defect (GS3) or a MYO5A F-exon deletion (GS1).";
RL J. Clin. Invest. 112:450-456(2003).
CC -!- FUNCTION: Processive actin-based motor that can move in large steps
CC approximating the 36-nm pseudo-repeat of the actin filament. Involved
CC in melanosome transport. Also mediates the transport of vesicles to the
CC plasma membrane. May also be required for some polarization process
CC involved in dendrite formation. {ECO:0000269|PubMed:10448864}.
CC -!- SUBUNIT: May be a homodimer, which associates with multiple calmodulin
CC or myosin light chains (By similarity). Interacts with RIPL2, the
CC interaction is required for its role in dendrite formation (By
CC similarity). Interacts with MLPH (PubMed:12062444). Interacts with
CC SYTL4 (By similarity). Interacts with MYRIP (By similarity). Interacts
CC with RAB10; mediates the transport to the plasma membrane of
CC SLC2A4/GLUT4 storage vesicles (PubMed:22908308). Interacts with FMR1;
CC this interaction occurs in association with polyribosome (By
CC similarity). {ECO:0000250|UniProtKB:Q99104,
CC ECO:0000269|PubMed:12062444, ECO:0000269|PubMed:22908308}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y4I1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4I1-2; Sequence=VSP_003351;
CC Name=3;
CC IsoId=Q9Y4I1-3; Sequence=VSP_003352;
CC -!- TISSUE SPECIFICITY: Detected in melanocytes.
CC -!- DISEASE: Griscelli syndrome 1 (GS1) [MIM:214450]: Rare autosomal
CC recessive disorder that results in pigmentary dilution of the skin and
CC hair, the presence of large clumps of pigment in hair shafts, silvery-
CC gray hair and accumulation of melanosomes in melanocytes. GS1 patients
CC show developmental delay, hypotonia and intellectual disability,
CC without apparent immune abnormalities. {ECO:0000269|PubMed:10704277}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Griscelli syndrome 3 (GS3) [MIM:609227]: Rare autosomal
CC recessive disorder characterized by pigmentary dilution of the skin and
CC hair, the presence of large clumps of pigment in hair shafts, and an
CC accumulation of melanosomes in melanocytes, without other clinical
CC manifestations. {ECO:0000269|PubMed:12897212}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Elejalde syndrome (ELEJAS) [MIM:256710]: Autosomal recessive
CC condition characterized by skin hypopigmentation, the presence of large
CC clumps of pigment in hair shafts, silvery-gray hair, accumulation of
CC melanosomes in melanocytes and primary neurological abnormalities.
CC Elejalde syndrome may be the same entity as Griscelli syndrome type I.
CC {ECO:0000269|PubMed:12058346}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=MYO5Abase; Note=MYO5A mutation db;
CC URL="http://structure.bmc.lu.se/idbase/MYO5Abase/";
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DR EMBL; Y07759; CAA69035.1; -; mRNA.
DR EMBL; Y07759; CAA69036.1; -; mRNA.
DR EMBL; U90942; AAD00702.1; -; mRNA.
DR EMBL; AC010674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC018902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z22957; CAA80533.1; -; mRNA.
DR EMBL; S74799; AAB33211.1; -; mRNA.
DR EMBL; AF055459; AAC14188.1; -; mRNA.
DR CCDS; CCDS42037.1; -. [Q9Y4I1-1]
DR CCDS; CCDS45262.1; -. [Q9Y4I1-2]
DR PIR; A53016; A53016.
DR PIR; A59254; A59254.
DR PIR; B59254; B59254.
DR PIR; I52966; I52966.
DR RefSeq; NP_000250.3; NM_000259.3.
DR RefSeq; XP_005254454.1; XM_005254397.3.
DR PDB; 4D07; X-ray; 1.85 A; B=1275-1297.
DR PDB; 4J5L; X-ray; 2.20 A; A/B=1448-1855.
DR PDB; 4LLI; X-ray; 2.20 A; A/B=1467-1855.
DR PDB; 4LX1; X-ray; 1.87 A; A/B=1464-1855.
DR PDB; 4LX2; X-ray; 1.50 A; A=1464-1855.
DR PDB; 5JCY; X-ray; 1.80 A; A=1464-1855.
DR PDB; 5JCZ; X-ray; 2.06 A; B/C/E=1464-1855.
DR PDBsum; 4D07; -.
DR PDBsum; 4J5L; -.
DR PDBsum; 4LLI; -.
DR PDBsum; 4LX1; -.
DR PDBsum; 4LX2; -.
DR PDBsum; 5JCY; -.
DR PDBsum; 5JCZ; -.
DR AlphaFoldDB; Q9Y4I1; -.
DR SMR; Q9Y4I1; -.
DR BioGRID; 110728; 179.
DR CORUM; Q9Y4I1; -.
DR IntAct; Q9Y4I1; 69.
DR MINT; Q9Y4I1; -.
DR STRING; 9606.ENSP00000382177; -.
DR CarbonylDB; Q9Y4I1; -.
DR iPTMnet; Q9Y4I1; -.
DR MetOSite; Q9Y4I1; -.
DR PhosphoSitePlus; Q9Y4I1; -.
DR SwissPalm; Q9Y4I1; -.
DR BioMuta; MYO5A; -.
DR DMDM; 296439234; -.
DR EPD; Q9Y4I1; -.
DR jPOST; Q9Y4I1; -.
DR MassIVE; Q9Y4I1; -.
DR MaxQB; Q9Y4I1; -.
DR PaxDb; Q9Y4I1; -.
DR PeptideAtlas; Q9Y4I1; -.
DR PRIDE; Q9Y4I1; -.
DR ProteomicsDB; 86207; -. [Q9Y4I1-1]
DR ProteomicsDB; 86208; -. [Q9Y4I1-2]
DR ProteomicsDB; 86209; -. [Q9Y4I1-3]
DR Antibodypedia; 686; 172 antibodies from 32 providers.
DR DNASU; 4644; -.
DR Ensembl; ENST00000399231.8; ENSP00000382177.3; ENSG00000197535.16. [Q9Y4I1-1]
DR Ensembl; ENST00000399233.7; ENSP00000382179.4; ENSG00000197535.16. [Q9Y4I1-3]
DR Ensembl; ENST00000687574.1; ENSP00000510312.1; ENSG00000197535.16. [Q9Y4I1-2]
DR GeneID; 4644; -.
DR KEGG; hsa:4644; -.
DR MANE-Select; ENST00000399233.7; ENSP00000382179.4; NM_001382347.1; NP_001369276.1. [Q9Y4I1-3]
DR UCSC; uc002abx.5; human. [Q9Y4I1-1]
DR CTD; 4644; -.
DR DisGeNET; 4644; -.
DR GeneCards; MYO5A; -.
DR HGNC; HGNC:7602; MYO5A.
DR HPA; ENSG00000197535; Tissue enhanced (parathyroid).
DR MalaCards; MYO5A; -.
DR MIM; 160777; gene.
DR MIM; 214450; phenotype.
DR MIM; 256710; phenotype.
DR MIM; 609227; phenotype.
DR neXtProt; NX_Q9Y4I1; -.
DR OpenTargets; ENSG00000197535; -.
DR Orphanet; 79476; Griscelli syndrome type 1.
DR Orphanet; 79478; Griscelli syndrome type 3.
DR Orphanet; 33445; Neuroectodermal melanolysosomal disease.
DR PharmGKB; PA31407; -.
DR VEuPathDB; HostDB:ENSG00000197535; -.
DR eggNOG; KOG0160; Eukaryota.
DR GeneTree; ENSGT00940000155347; -.
DR HOGENOM; CLU_000192_9_2_1; -.
DR InParanoid; Q9Y4I1; -.
DR OMA; CEIFHND; -.
DR OrthoDB; 311886at2759; -.
DR PhylomeDB; Q9Y4I1; -.
DR TreeFam; TF328771; -.
DR PathwayCommons; Q9Y4I1; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-264876; Insulin processing.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q9Y4I1; -.
DR SIGNOR; Q9Y4I1; -.
DR BioGRID-ORCS; 4644; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; MYO5A; human.
DR GeneWiki; MYO5A; -.
DR GenomeRNAi; 4644; -.
DR Pharos; Q9Y4I1; Tbio.
DR PRO; PR:Q9Y4I1; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9Y4I1; protein.
DR Bgee; ENSG00000197535; Expressed in lateral nuclear group of thalamus and 190 other tissues.
DR ExpressionAtlas; Q9Y4I1; baseline and differential.
DR Genevisible; Q9Y4I1; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0032433; C:filopodium tip; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; NAS:UniProtKB.
DR GO; GO:0032593; C:insulin-responsive compartment; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; NAS:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030048; P:actin filament-based movement; NAS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0032402; P:melanosome transport; NAS:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030050; P:vesicle transport along actin filament; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR CDD; cd15478; Myo5a_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR037988; Myo5a_CBD.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 6.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 6.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW ATP-binding; Calmodulin-binding; Coiled coil; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1855
FT /note="Unconventional myosin-Va"
FT /id="PRO_0000123456"
FT DOMAIN 8..60
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 69..763
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 766..788
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 789..818
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 814..836
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 837..861
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 862..883
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 885..914
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1534..1810
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 598..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..665
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT COILED 914..1237
FT /evidence="ECO:0000255"
FT COILED 1338..1445
FT /evidence="ECO:0000255"
FT COMPBIAS 598..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1032
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYF3"
FT MOD_RES 1452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1760
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1321..1347
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7835087,
FT ECO:0000303|PubMed:8188282, ECO:0000303|Ref.1"
FT /id="VSP_003351"
FT VAR_SEQ 1413
FT /note="L -> LYFEELYADDPKKYQSYRISLYKRMI (in isoform 3)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_003352"
FT VARIANT 627
FT /note="M -> T (in dbSNP:rs16964944)"
FT /id="VAR_056180"
FT VARIANT 1246
FT /note="R -> C (in dbSNP:rs1058219)"
FT /evidence="ECO:0000269|PubMed:10733681,
FT ECO:0000269|PubMed:9207796"
FT /id="VAR_010645"
FT VARIANT 1673
FT /note="S -> L (in dbSNP:rs9282796)"
FT /id="VAR_056181"
FT CONFLICT 198
FT /note="A -> T (in Ref. 1; CAA69035/CAA69036 and 2;
FT AAD00702)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="E -> D (in Ref. 1; CAA69035/CAA69036 and 2;
FT AAD00702)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="F -> L (in Ref. 1; CAA69035/CAA69036)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="Missing (in Ref. 5; CAA80533)"
FT /evidence="ECO:0000305"
FT CONFLICT 863
FT /note="E -> G (in Ref. 1; CAA69035/CAA69036)"
FT /evidence="ECO:0000305"
FT CONFLICT 922
FT /note="H -> R (in Ref. 1; CAA69035/CAA69036)"
FT /evidence="ECO:0000305"
FT CONFLICT 1061
FT /note="V -> L (in Ref. 6; AAB33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 1089
FT /note="E -> Q (in Ref. 5; CAA80533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1177
FT /note="D -> E (in Ref. 6; AAB33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 1465..1477
FT /note="NIPRKEKDFQGML -> SVLCACCVSVTVR (in Ref. 5;
FT CAA80533)"
FT /evidence="ECO:0000305"
FT CONFLICT 1471
FT /note="K -> N (in Ref. 6; AAB33211)"
FT /evidence="ECO:0000305"
FT CONFLICT 1484
FT /note="E -> D (in Ref. 6; AAB33211)"
FT /evidence="ECO:0000305"
FT STRAND 1285..1289
FT /evidence="ECO:0007829|PDB:4D07"
FT STRAND 1475..1478
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1481..1483
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1484..1491
FT /evidence="ECO:0007829|PDB:4LX2"
FT TURN 1492..1494
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1500..1502
FT /evidence="ECO:0007829|PDB:4LX2"
FT TURN 1505..1507
FT /evidence="ECO:0007829|PDB:4LLI"
FT HELIX 1508..1522
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1526..1547
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1551..1570
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1575..1577
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1583..1586
FT /evidence="ECO:0007829|PDB:4LX2"
FT STRAND 1591..1594
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1596..1621
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1622..1624
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1625..1629
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1661..1677
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1682..1706
FT /evidence="ECO:0007829|PDB:4LX2"
FT STRAND 1708..1710
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1713..1732
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1740..1743
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1745..1755
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1761..1770
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1776..1785
FT /evidence="ECO:0007829|PDB:4LX2"
FT STRAND 1790..1792
FT /evidence="ECO:0007829|PDB:5JCZ"
FT HELIX 1798..1807
FT /evidence="ECO:0007829|PDB:4LX2"
FT TURN 1808..1810
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1838..1840
FT /evidence="ECO:0007829|PDB:4LX2"
FT HELIX 1845..1847
FT /evidence="ECO:0007829|PDB:4LX2"
FT STRAND 1852..1855
FT /evidence="ECO:0007829|PDB:4LX2"
SQ SEQUENCE 1855 AA; 215405 MW; 78FD3B1D08D90A0A CRC64;
MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEEGKDLEY HLDPKTKELP
HLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFIDSKLIY TYCGIVLVAI NPYEQLPIYG
EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM ARDERNQSII VSGESGAGKT VSAKYAMRYF
ATVSGSASEA NVEEKVLASN PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR
TYLLEKSRVV FQAEEERNYH IFYQLCASAK LPEFKMLRLG NADNFNYTKQ GGSPVIEGVD
DAKEMAHTRQ ACTLLGISES HQMGIFRILA GILHLGNVGF TSRDADSCTI PPKHEPLCIF
CELMGVDYEE MCHWLCHRKL ATATETYIKP ISKLQATNAR DALAKHIYAK LFNWIVDNVN
QALHSAVKQH SFIGVLDIYG FETFEINSFE QFCINYANEK LQQQFNMHVF KLEQEEYMKE
QIPWTLIDFY DNQPCINLIE SKLGILDLLD EECKMPKGTD DTWAQKLYNT HLNKCALFEK
PRLSNKAFII QHFADKVEYQ CEGFLEKNKD TVFEEQIKVL KSSKFKMLPE LFQDDEKAIS
PTSATSSGRT PLTRTPAKPT KGRPGQMAKE HKKTVGHQFR NSLHLLMETL NATTPHYVRC
IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR WTYQEFFSRY RVLMKQKDVL
SDRKQTCKNV LEKLILDKDK YQFGKTKIFF RAGQVAYLEK LRADKLRAAC IRIQKTIRGW
LLRKKYLRMR KAAITMQRYV RGYQARCYAK FLRRTKAATI IQKYWRMYVV RRRYKIRRAA
TIVLQSYLRG FLARNRYRKI LREHKAVIIQ KRVRGWLART HYKRSMHAII YLQCCFRRMM
AKRELKKLKI EARSVERYKK LHIGMENKIM QLQRKVDEQN KDYKCLVEKL TNLEGIYNSE
TEKLRSDLER LQLSEEEAKV ATGRVLSLQE EIAKLRKDLE QTRSEKKCIE EHADRYKQET
EQLVSNLKEE NTLLKQEKEA LNHRIVQQAK EMTETMEKKL VEETKQLELD LNDERLRYQN
LLNEFSRLEE RYDDLKEEMT LMVHVPKPGH KRTDSTHSSN ESEYIFSSEI AEMEDIPSRT
EEPSEKKVPL DMSLFLKLQK RVTELEQEKQ VMQDELDRKE EQVLRSKAKE EERPQIRGAE
LEYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVTAP GAPAYRVLME QLTSVSEELD
VRKEEVLILR SQLVSQKEAI QPKDDKNTMT DSTILLEDVQ KMKDKGEIAQ AYIGLKETNR
SSALDYHELN EDGELWLVYE GLKQANRLLE SQLQSQKRSH ENEAEALRGE IQSLKEENNR
QQQLLAQNLQ LPPEARIEAS LQHEITRLTN ENLDLMEQLE KQDKTVRKLK KQLKVFAKKI
GELEVGQMEN ISPGQIIDEP IRPVNIPRKE KDFQGMLEYK KEDEQKLVKN LILELKPRGV
AVNLIPGLPA YILFMCVRHA DYLNDDQKVR SLLTSTINSI KKVLKKRGDD FETVSFWLSN
TCRFLHCLKQ YSGEEGFMKH NTSRQNEHCL TNFDLAEYRQ VLSDLAIQIY QQLVRVLENI
LQPMIVSGML EHETIQGVSG VKPTGLRKRT SSIADEGTYT LDSILRQLNS FHSVMCQHGM
DPELIKQVVK QMFYIIGAIT LNNLLLRKDM CSWSKGMQIR YNVSQLEEWL RDKNLMNSGA
KETLEPLIQA AQLLQVKKKT DDDAEAICSM CNALTTAQIV KVLNLYTPVN EFEERVSVSF
IRTIQMRLRD RKDSPQLLMD AKHIFPVTFP FNPSSLALET IQIPASLGLG FISRV
