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Database: UniProt
Entry: A0A286Y349_CAVPO
LinkDB: A0A286Y349_CAVPO
Original site: A0A286Y349_CAVPO 
ID   A0A286Y349_CAVPO        Unreviewed;      1853 AA.
AC   A0A286Y349;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Myosin VA {ECO:0000313|Ensembl:ENSCPOP00000032261.1};
GN   Name=MYO5A {ECO:0000313|Ensembl:ENSCPOP00000032261.1};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000032261.1, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000032261.1}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000032261.1};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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; AAKN02027809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02027810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSCPOT00000048492.1; ENSCPOP00000032261.1; ENSCPOG00000007886.4.
DR   VEuPathDB; HostDB:ENSCPOG00000007886; -.
DR   GeneTree; ENSGT00940000155347; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000007886; Expressed in cerebellum and 13 other cell types or tissues.
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; 5.
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   3: Inferred from homology;
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}; Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Transport {ECO:0000256|ARBA:ARBA00022927}.
FT   DOMAIN          6..58
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          67..761
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1532..1808
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          594..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..663
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1104..1142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          913..1103
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1153..1229
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1337..1437
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        596..612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         161..168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1853 AA;  214868 MW;  1ECD5BA7E813936E CRC64;
     KILSRIYTRM VWIPDPEEVW RSAELLRDYK PGDKTLLLRL EEGKDLEYRL DPKTKELPHL
     RNPDILVGEN DLTALSYLHE PAVLHNLRVR FIDSKLIYTY CGIVLVAINP YEQLPIYGED
     IINAYSGQNM GDMDPHIFAV AEEAYKQMAR DERNQSIIVS GESGAGKTVS AKYAMRYFAT
     VSGSASEANV EEKVLASNPI MESIGNAKTT RNDNSSRFGK YIEIGFDKRY RIIGANMRTY
     LLEKSRVVFQ AEEERNYHIF YQLCASAKLP EFKMLQLGAA DSFHYTKQGG SPVIEGVDDA
     REMAHTRQAC TLLGISESYQ MGIFRILAGI LHLGNVGFVS RDSDSCTIPP KHEPLSVFCD
     LMGVEYEEMC HWLCHRKLAT ATETYIKPIS KLQATNARDA LAKHIYAKLF GWIVGHVNQA
     LHSAVKQHSF IGVLDIYGFE TFEINSFEQF CINYANEKLQ QQFNMHVFKL EQEEYMKEQI
     PWTLIDFYDN QPCINLIESK LGILDLLDEE CKMPKGTDDT WAQKLYNTHL NKCALFEKPR
     LSNKAFIIQH FADKVEYQCE GFLEKNKDTV FEEQIQVLKS SKFKMLPELF QDDEKAISPT
     SATPSGRTPL SRVPSKPTKG RPGQLTKEHK KTVGHQFRNS LHLLMETLNA TTPHYVRCIK
     PNDFKFPFTF DEKRAVQQLR ACGVLETIRI SAAGFPSRWT YQEFFSRYRV LMKQKDVLGD
     RKQTCKKVLE KLILDKDKYQ FGKTKIFFRA GQVAYLEKLR ADKLRAACIR IQKTIRGWLL
     RKKFLRMRRA AVTMQRFVRG YQARCYAKFL RRTKAATVIQ KYWRMYVVRR RYKTRRAATI
     VLQACLRGYL ARNRYHKMLR EHKAVIIQKW VRGWLARTHY RRCLQAIVYL QCCFRRMMAK
     RELKKLKIEA RSVERYKKLH IGMENKIMQL QRKVDEQNKD YKCLMEKLTS LEGTYNSETE
     KLRSDLERLQ LSEEEAKVAT GRVLSLQEEL ARLQKDLEQT QSEKKSIEER ADRYKQETEQ
     LVSNLKEENT LLKQEKESLN HFIMEQAKEI TETMEKKLVE ETKQLELDLN DERLRYQNLL
     NEFSRLEERY DDLREEMALM ATVSKPGHKR TDSTHSSNES EYTFSSEIAE TEDVPSRAEE
     LSEKKVPLDM SLFLKLQKRV TELEQEKQVM QDELDRKEEQ MLRSKAKEEE RPQIRGAELE
     YESLKRQELE SENKKLKNEL NELRKSLSEK SAPEVTAPGA PAYRVLMEQL TSVSEELDVR
     KEEVLILRSQ LVSQKEAVQP KVSANTMTDA TILLEDVQKM KDKGEIAQAY IGLKETNRPS
     ALDCRELNED GELWLVYEGL KQANRLLESQ LQSQKRSHEN EAEALRGEIQ SLKEENNRQQ
     QLLAQNLQLP PEARIEASLQ HEITRLTNEN LDLMEQLEKQ DKTVRKLKKQ LKVFAKKIGE
     LEVGQMENIS PGQIIDEPIR PVNIPRKEKD FQGMLEYKKE DEQKLVKNLI LELKPRGVAV
     NLIPGLPAYI LFMCVRHADY LNDDQKVRSL LTSTINSIKK VLKKRGDDFE TVSFWLSNTC
     RFLHCLKQYS GEEGFMKHNT ARQNEHCLTN FDLAEYRQVL SDLAIQIYQQ LVRVLENILQ
     PMIVSGMLEH ETIQGVSGVK PTGLRKRTSS IADEGTYTLD SILRQLNSFH SVMCQHGMDP
     ELIKQVVKQM FYIVGAVTLN NLLLRKDMCS WSKGMQIRYN VSQLEEWLRD KNLMNSGAKE
     TLEPLIQAAQ LLQVKKKTDD DAEAICSMCN ALTTAQIVKV LNLYTPVNEF EERVSVAFIR
     TIQMRLRDRK DSPQLLMDAK HIFPVTFPFN PSSLALETIQ IPASLGLGFI SRV
//
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