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   27-MAR-2024, entry version 218.
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 GS1.
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 GS1.
RX   PubMed=12897212; DOI=10.1172/jci18264;
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       ECO:0000269|PubMed:12058346, ECO:0000269|PubMed:12897212}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry. Some patients who have MYO5A pathogenic variants and originally
CC       diagnosed with Griscelli syndrome 1 may rather have Elejalde syndrome.
CC       {ECO:0000269|PubMed:12058346}.
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   CCDS; CCDS92001.1; -. [Q9Y4I1-3]
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; 204.
DR   CORUM; Q9Y4I1; -.
DR   IntAct; Q9Y4I1; 79.
DR   MINT; Q9Y4I1; -.
DR   STRING; 9606.ENSP00000382177; -.
DR   CarbonylDB; Q9Y4I1; -.
DR   GlyGen; Q9Y4I1; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000382177; -.
DR   PeptideAtlas; Q9Y4I1; -.
DR   ProteomicsDB; 86207; -. [Q9Y4I1-1]
DR   ProteomicsDB; 86208; -. [Q9Y4I1-2]
DR   ProteomicsDB; 86209; -. [Q9Y4I1-3]
DR   Pumba; Q9Y4I1; -.
DR   Antibodypedia; 686; 189 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   AGR; HGNC:7602; -.
DR   CTD; 4644; -.
DR   DisGeNET; 4644; -.
DR   GeneCards; MYO5A; -.
DR   HGNC; HGNC:7602; MYO5A.
DR   HPA; ENSG00000197535; Tissue enhanced (brain, parathyroid gland).
DR   MalaCards; MYO5A; -.
DR   MIM; 160777; gene.
DR   MIM; 214450; 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; GKSKHFE; -.
DR   OrthoDB; 1094820at2759; -.
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 1147 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 192 other cell types or tissues.
DR   ExpressionAtlas; Q9Y4I1; baseline and differential.
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; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 3.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 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   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   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF273; UNCONVENTIONAL MYOSIN-VA; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 6.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
DR   Genevisible; Q9Y4I1; HS.
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
//