ID F8WE88_HUMAN Unreviewed; 1855 AA.
AC F8WE88;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Unconventional myosin-Va {ECO:0000313|Ensembl:ENSP00000382179};
GN Name=MYO5A {ECO:0000313|Ensembl:ENSP00000382179};
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 {ECO:0000313|Ensembl:ENSP00000382179, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000382179, ECO:0000313|Proteomes:UP000005640}
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., Stewart S.,
RA Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R.,
RA 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 [2] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [3] {ECO:0007829|PubMed:19413330}
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 [4] {ECO:0007829|PubMed:19690332}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [5] {ECO:0007829|PubMed:20068231}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [6] {ECO:0007829|PubMed:21269460}
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., Burckstummer 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 [7] {ECO:0000313|Ensembl:ENSP00000382179}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [8] {ECO:0007829|PubMed:22814378}
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [9] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
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).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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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; KF459554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; F8WE88; -.
DR MassIVE; F8WE88; -.
DR PeptideAtlas; F8WE88; -.
DR ProteomicsDB; 31758; -.
DR Antibodypedia; 686; 189 antibodies from 32 providers.
DR Ensembl; ENST00000399233; ENSP00000382179; ENSG00000197535.
DR UCSC; uc059jiv.1; human.
DR HGNC; HGNC:7602; MYO5A.
DR OpenTargets; ENSG00000197535; -.
DR VEuPathDB; HostDB:ENSG00000197535; -.
DR ChiTaRS; MYO5A; human.
DR Proteomes; UP000005640; Chromosome 15.
DR Bgee; ENSG00000197535; Expressed in lateral nuclear group of thalamus and 192 other cell types or tissues.
DR ExpressionAtlas; F8WE88; baseline and differential.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
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.
PE 1: Evidence at protein level;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Proteomics identification {ECO:0007829|EPD:F8WE88,
KW ECO:0007829|MaxQB:F8WE88};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT DOMAIN 8..60
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 69..763
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1534..1810
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
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:0000256|PROSITE-ProRule:PRU00782"
FT COILED 915..1098
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1155..1231
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1339..1439
FT /evidence="ECO:0000256|SAM:Coils"
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:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1855 AA; 215359 MW; ECBC628A6AB8096C 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 QPKPSQNTMT 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
//