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
//