UniProt: F1M111

Database: UniProt
Entry: F1M111_RAT

LinkDB:  F1M111_RAT 
Original site:  F1M111_RAT

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Ontology (10)   
   GO (10)   
Gene (5)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
   RGD (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
Protein domain (18)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (4)   
   SMART (3)   
Literature (1)   
   PubMed (1)   
All databases (36)   

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ID   F1M111_RAT              Unreviewed;      1749 AA.
AC   F1M111;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Myosin VC {ECO:0000313|Ensembl:ENSRNOP00000011768.7};
GN   Name=Myo5c {ECO:0000313|Ensembl:ENSRNOP00000011768.7,
GN   ECO:0000313|RGD:1309994};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000011768.7, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000011768.7, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000011768.7,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000011768.7}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000011768.7};
RG   Ensembl;
RL   Submitted (NOV-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   RefSeq; XP_006226541.1; XM_006226479.2.
DR   RefSeq; XP_006243475.1; XM_006243413.2.
DR   AlphaFoldDB; F1M111; -.
DR   STRING; 10116.ENSRNOP00000011768; -.
DR   iPTMnet; F1M111; -.
DR   PhosphoSitePlus; F1M111; -.
DR   PaxDb; 10116-ENSRNOP00000011768; -.
DR   Ensembl; ENSRNOT00000011768.8; ENSRNOP00000011768.7; ENSRNOG00000008356.8.
DR   GeneID; 315820; -.
DR   UCSC; RGD:1309994; rat.
DR   AGR; RGD:1309994; -.
DR   CTD; 55930; -.
DR   RGD; 1309994; Myo5c.
DR   VEuPathDB; HostDB:ENSRNOG00000008356; -.
DR   eggNOG; KOG0160; Eukaryota.
DR   GeneTree; ENSGT00940000157971; -.
DR   HOGENOM; CLU_000192_9_4_1; -.
DR   InParanoid; F1M111; -.
DR   OMA; EIMFDDR; -.
DR   OrthoDB; 1094820at2759; -.
DR   TreeFam; TF328771; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000008356; Expressed in lung and 16 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR   CDD; cd15476; Myo5c_CBD; 1.
DR   CDD; cd01380; MYSc_Myo5; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 2.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 6.10.220.10; -; 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; IPR037991; Myo5c_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:SF313; UNCONVENTIONAL MYOSIN-VC; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 5.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 5.
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:UP000002494};
KW   Transport {ECO:0000256|ARBA:ARBA00022927}.
FT   DOMAIN          8..62
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          67..753
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1428..1704
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          632..654
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1232..1263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          884..1098
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1310..1358
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         161..168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1749 AA;  203144 MW;  6B108B732A4EA12B CRC64;
     MAVAELYAQY NRVWIPDPEE VWKSAEIAKD YRVGDQVLRL LLEDGTELDY PVDPGSLPPL
     RNPDILVGEN DLTALSYLHE PAVLHNLRIR FAESKLIYTY SGIILVAMNP YKQLPIYGDA
     IIHAYSGQNM GDMDPHIFAV AEEAYKQMAR NNRNQSIIVS GESGAGKTVS ARYAMRYFAT
     VSKSSSNAHV EEKVLASNPI TEAVGNAKTT RNDNSSRFGK YTEISFDERN QIIGANMRTY
     LLEKSRVVFQ SENERNYHIF YQLCASAQQS EFKHLKLGSA EEFNYTRMGG NTVIEGVDDR
     ADMAETQKTF TLLGFKKDFQ MDVFKILAAI LHLGNVQVTT VGNERSAVSE DDSHLKVFCE
     LLGLETIKVA QWLCNRKIVT SSETVVKPMT RPQAINARDA LAKKIYAHLF DFIVEQINQA
     LHFSGKQHTF IGVLDIYGFE TFDVNSFEQF CINYANEKLQ QQFNLHVFKL EQEEYMKEDI
     PWTLIDFYDN QPVIDLIEAK MGILELLDEE CLLPHGTDEN WLQKLYNNFV NKNSLFEKPR
     MSNSSFIIQH FADKVEYQCE GFLEKNRDTV YDMLVEVLRA SKFHLCAAFF QESPVPSSPF
     GAMITVKSAK QVIKPNTKHF RTTVGNKFRS SLFLLMETLN ATTPHYVRCI KPNDEKLPFE
     FDSKRIVQQL RACGVLETIR ISAQSYPSRW TYLEFYSRYG VLMTQQELSL SDKKEVCKVV
     LHRLIQDSNQ YQFGRTKIFF RAGQVAYLEK LRLDKLRQGC IVIQKHVRGW LQRKKFLRER
     RAALTIQQYF RGQQTVRKAI TATALKEAWA AIILQKHCRG YLVRNLYQLI RVATITIQAH
     TRGFLARRRY RKLLQEHKAV ILQKYARAWL ARRRFQNIRR FVLNIQLTYR VQRLQKKLED
     QNRENHGLVE KLTSLAALRV GDLEKVQRLE AELEKAATHR HSYEEKGRRY RDSMEERLSK
     LQKHNAELES QRERAEQSLQ ERTEELKEKM DQLTRQLFDD VQKEEQQRLL LEKSFELKTQ
     AYEKEIESLR EEIKALKDER TQLHHQLEEG RVTSDSLKGE VARLSKQAKT ISEFEKEIEL
     LQAQKIDVEK HVQSQKREMR ERMSEVTKQL LESYDIEDVR SRLSVEDLEH LNEDGELWFA
     YEGLKKATRV LESHFQSQKD CYEKEIEGLN FKVVHLSQEI NHLQKLFREE TDINESIRHE
     VTRLTSENMM IPDFKQQISE LERQKQDLES RLKEQAEKME GKQEEPFSHL NRGLEEEGRQ
     GKAPRPFLRA VEAQSETHPE GKERLVGKIQ EPQEAIKFPK KQAEAEEEVE SILRQEASRL
     SLENRDLEEE LDMKDRMIRK LQDQVKTLTR TIEKANSVPL PSGSREYLGM LEYKKEDETK
     LIQNLILDLK PRGVVVNMIP GLPAHILFMC VRYADSLNDA NMLKSLMNSA INGIKHVVKE
     HFEDLEMLSF WLSNTCHFLN CLKQYSGEEE FMKCNSPQQN KNCLNNFDLT EYRQILSDVA
     IRIYHQFILV MENNLQPIIV PGMLEYESLQ GISGLKPTGF RKRSSSIDDT DAYTMTSILQ
     QLSYFYSTMC QNGLDPEIVR QAVKQLFYLI GAVTLNSLLL RKDMCSCRKG MQIRCNISFL
     EEWLKDKNLQ NSLAKETLEP LSQAAWLLQV KKTTDSDAKE ISQCCTSLSA VQIIKILNSY
     TPIDDFEKRV NPSFVRKVQA LLNNRGDSSQ LMLDTKYLFQ VTFPFTASPH ALEMTQIPSS
     FKLGFLRRL
//

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