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Database: UniProt
Entry: E9Q1F5_MOUSE
LinkDB: E9Q1F5_MOUSE
Original site: E9Q1F5_MOUSE 
ID   E9Q1F5_MOUSE            Unreviewed;      1742 AA.
AC   E9Q1F5;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=Myosin VC {ECO:0000313|Ensembl:ENSMUSP00000042229.7};
GN   Name=Myo5c {ECO:0000313|Ensembl:ENSMUSP00000042229.7,
GN   ECO:0000313|MGI:MGI:2442485};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000042229.7, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000042229.7, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000042229.7,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000042229.7}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000042229.7};
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; NP_001074791.1; NM_001081322.1.
DR   AlphaFoldDB; E9Q1F5; -.
DR   SMR; E9Q1F5; -.
DR   STRING; 10090.ENSMUSP00000042229; -.
DR   iPTMnet; E9Q1F5; -.
DR   PhosphoSitePlus; E9Q1F5; -.
DR   jPOST; E9Q1F5; -.
DR   MaxQB; E9Q1F5; -.
DR   PaxDb; 10090-ENSMUSP00000042229; -.
DR   PeptideAtlas; E9Q1F5; -.
DR   ProteomicsDB; 349036; -.
DR   Antibodypedia; 24945; 79 antibodies from 16 providers.
DR   Ensembl; ENSMUST00000036555.8; ENSMUSP00000042229.7; ENSMUSG00000033590.9.
DR   GeneID; 208943; -.
DR   KEGG; mmu:208943; -.
DR   UCSC; uc009qru.1; mouse.
DR   AGR; MGI:2442485; -.
DR   CTD; 55930; -.
DR   MGI; MGI:2442485; Myo5c.
DR   VEuPathDB; HostDB:ENSMUSG00000033590; -.
DR   eggNOG; KOG0160; Eukaryota.
DR   GeneTree; ENSGT00940000157971; -.
DR   HOGENOM; CLU_000192_9_1_1; -.
DR   InParanoid; E9Q1F5; -.
DR   OMA; EIMFDDR; -.
DR   OrthoDB; 1094820at2759; -.
DR   PhylomeDB; E9Q1F5; -.
DR   TreeFam; TF328771; -.
DR   BioGRID-ORCS; 208943; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Myo5c; mouse.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; E9Q1F5; Protein.
DR   Bgee; ENSMUSG00000033590; Expressed in left lung lobe and 117 other cell types or tissues.
DR   ExpressionAtlas; E9Q1F5; baseline and differential.
DR   Genevisible; E9Q1F5; MM.
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:0030141; C:secretory granule; ISO:MGI.
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:0032254; P:establishment of secretory granule localization; ISO:MGI.
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:SF706; MYOSIN-11; 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   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}; Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Proteomics identification {ECO:0007829|MaxQB:E9Q1F5,
KW   ECO:0007829|PeptideAtlas:E9Q1F5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
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          1421..1697
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   COILED          884..1098
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1211..1245
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1303..1344
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   1742 AA;  202702 MW;  751DA32B1CE39498 CRC64;
     MAVAELYAQY NRVWIPDPEE VWKSAEIAKD YRAGDRVLRL LLEDGMELEY PVDPGSLPPL
     RNPDILVGEN DLTALSYLHE PAVLHNLRIR FAESKLIYTY SGIILVAMNP YKQLPIYGDA
     IIHAYSGQNM GDMDPHIFAV AEEAYKQMAR NNRNQSIIVS GESGAGKTVS ARYAMRYFAT
     VSKSSSNAHV EDKVLASNPI TEAVGNAKTT RNDNSSRFGK YTEISFDERN QIIGANMRTY
     LLEKSRVVFQ SENERNYHIF YQLCASAQQS EFKHLKLGSA EEFNYTRMGG NTVIEGVNDR
     ADMVETQKTF TLLGFKKDFQ MDVFKILAAI LHLGNVQVTT VGNERSSVSE DDSHLKVFCE
     LLGLETSKVA QWLCNRKIVT SSETVVKPMT RPQAINARDA LAKKIYAHLF DFIVEQINQA
     LHFSGKQHTF IGVLDIYGFE TFDVNSFEQF CINYANEKLQ QQFNLHVFKL EQEEYMKEDI
     PWTLIDFYDN QPVIDLIEAK MGILELLDEE CLLPHGTDEN WLQKLYNNFV NKNSLFEKPR
     MSNSSFIIQH FADKVEYQCE GFLEKNRDTV YDMLVEILRA SKFHLCAAFF QESPVPSSPF
     GAMITVKSAK QVIKPNTKHF RTTVGNKFRS SLYLLMETLN ATTPHYVRCI KPNDEKMPFE
     FDSKRIVQQL RACGVLETIR ISAQSYPSRW TYLEFYSRYG ILMTQQELSL SDKKEVCKVV
     LHRLIQDSNQ YQFGRTKIFF RAGQVAYLEK LRLDKLRQDC IMIQKHVRGW LQRRKFLRER
     QAALTIQRYF RGQQTVRKAI TATALKEAWA AIILQKYCRG YLVRNLYQLI RVATITIQAH
     TRGFLARRRY RKLLQEHKAV ILQKYARAWL ARRRFQNIRR FVLNIQLTYR VQRLQKKLED
     QNRENHGLVE KLTSLAALRV GDLEKVQKLE AELEKAATHR HSYEEKGRRY RDTVEERLSK
     LQKHNAELEL QRERAEQMLQ EKSEELKEKM DKLTRQLFDD VQKEEQQRLV LEKGFELKTQ
     AYEKQIESLR EEIKALKDER SQLHHQLEEG QVTSDRLKGE VARLSKQAKT ISEFEKEIEL
     LQAQKIDVEK HVQSQKREMR ERMSEVTKQL LESYDIEDVR SRLSVEDLEH LNEDGELWFA
     YEGLKKATRV LESHFQSQKD CYEKEIEGLN FKVVHLSQEI NHLQKLFREE TDINESIRHE
     VTRLTSENMM IPDFKQQISE LERQKQDLES RLKEQAEKIE GKLEEPFSHL NRIREEERMQ
     GRAVEAQSEM HPEGKERLVG AIHEPHEAIK FPKKQPEAEE EVESILQQEA SRLSLEKRDL
     EEELDMKDRM IRRLQDQVKT LTKTTEKANH VHLPSGSREY LGMLEYKKED EGKLIQNLIL
     DLKPRGVVVN MIPGLPAHIL FMCVRYADSL NDANMLKSLM NSAINGIKHV VKEHFEDLEM
     LSFWLSNTCH FLNCLKQYSG EEEFMKYNSP QQNKNCLNNF DLTEYRQILS DVAIRIYHQF
     IIVMENNLQP IIVPGMLEYE SLQGISGLKP TGFRKRSSSI DDTDAYTMTS ILQQLSYFYS
     TMCQNGLDPE IVRQAVKQLF YLVGAVTLNS LLLRKDMCSC RKGMQIRCNI SFLEEWLKDK
     NVQSSLAKET LEPLSQAAWL LQVKKTTDSD AKEIAQCCTS LSAVQIIKIL NSYTPIDDFE
     KRVNPSFVRK VQALLNNRGD SAQLMLDTKY LFQVTFPFTA SPHALEMTQI PSSFKLGFLR
     RL
//
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