MYO1C_DANRE
ID MYO1C_DANRE Reviewed; 1026 AA.
AC A5PF48;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Unconventional myosin-Ic;
DE AltName: Full=Myosin I beta;
DE Short=MMI-beta;
DE Short=MMIb;
GN Name=myo1c; ORFNames=si:ch211-69i14.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Their highly
CC divergent tails are presumed to bind to membranous compartments, which
CC would be moved relative to actin filaments (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via its IQ motifs) with calm. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasmic
CC vesicle {ECO:0000250}. Cell projection, stereocilium membrane
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-1 (MYH1). {ECO:0000305}.
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DR EMBL; AL935065; CAN88202.1; -; Genomic_DNA.
DR RefSeq; NP_001093501.1; NM_001100031.1.
DR AlphaFoldDB; A5PF48; -.
DR SMR; A5PF48; -.
DR STRING; 7955.ENSDARP00000053510; -.
DR PaxDb; A5PF48; -.
DR PeptideAtlas; A5PF48; -.
DR Ensembl; ENSDART00000189812; ENSDARP00000146110; ENSDARG00000020924.
DR GeneID; 567536; -.
DR KEGG; dre:567536; -.
DR CTD; 567536; -.
DR ZFIN; ZDB-GENE-070705-190; myo1ca.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000166539; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; A5PF48; -.
DR PhylomeDB; A5PF48; -.
DR TreeFam; TF312960; -.
DR PRO; PR:A5PF48; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000020924; Expressed in swim bladder and 24 other tissues.
DR ExpressionAtlas; A5PF48; baseline.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0032835; P:glomerulus development; IMP:ZFIN.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 3: Inferred from homology;
KW Acetylation; Actin-binding; ATP-binding; Cell membrane; Cell projection;
KW Cytoplasm; Cytoplasmic vesicle; Membrane; Methylation; Motor protein;
KW Myosin; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1026
FT /note="Unconventional myosin-Ic"
FT /id="PRO_0000369411"
FT DOMAIN 12..695
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 698..727
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 721..750
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 849..1024
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 572..594
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 104..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 157..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250"
FT MOD_RES 349
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1026 AA; 118063 MW; C34081C18098F8A5 CRC64;
MESALSARDR VGVQDFLLLE NHNSEAAFIE NLRRRYREGL IYTYIGSVLV SVNPYKELEI
YSKQNMERHR GVNFYEISPH IFALADNSYR ALRTERRDQC ILISGESGAG KTEASKKILQ
YYTHICPTRN NTHTIRERLL QSNPVLEAFG NAKTLRNDNS SRFGKYMDIQ FDYKGAPIGG
HILNYLLEKS RVAHQNHGER NFHIFYQLLE GGEDLLLKRL GLDKTNPQHY HYLIKGNCPR
VSSISDKNGW KVVRNALTII GFEDEEIQAL MEIVASVLHL GNTQFGEDEE GETHITTEAQ
LQFLSQLLGV DGSVLKAALT HKKIVAKGEE MISPLSLEQA LSARDSFAKA IYGRAFTWLV
QKLNRSLAFK DEIYYSSKCS SVIGLLDIYG FEVFQHNSFE QFCINYCNEK LQQLFIELTL
KSEQEEYEAE GWERVEYFNN KIICDLVEEK HKGIIAILDE ECLRRGDASD ITFLEKLEDT
LGGHAHFITH KMANGKIRKA IGREEFRLVH YAGEVNYNVN GFLDKNNDLL YRHLKEVLCQ
STNHIVSQCF HADELMDQRR PETAATQFKL SLAKLMDILM SKEPSYVRCI KPNDGKQPGR
FDEVLVRHQV KYLGLMENLR VRRAGFAYRR SYEAFLERYK SLCPDTWPNW HGNLPEGVAT
LVKHLNYKPE EFKLGRSKIF IRFPRTLFIT EDALEAQKQT IAVTLQKSWR GYRERANYHR
IRHAVIVIQS WWRGVKGRRK AKHRRQAADT IRNFIKGFIL RNEPRCPDNE YFLDHVRFSF
LMKVKRNLPK SVLDKSWPKP PPSLTEASEH IHRICIRNLV NDYCRRIQPE WRKQLEQKVV
ASGIFKGQKD GYSRSVPKLF VATRLEAEEI NLKVLQTLGS DNKVKYGIAV TKYDRHGFRP
RVRQLLLTTS SAVLVQEAKI KQRIDYGALL GISVSSLSDG FFVLHIPTAD SKQKGDLVLQ
CDHVIEAVTK LAIMADKIHN VNISQDSIRF AIARGKEGVI DFTSGSDLRV VKSKNGHLSV
TTPRIS
