MY1CA_XENLA
ID MY1CA_XENLA Reviewed; 1028 AA.
AC A0MP03; Q6PA28;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Unconventional myosin-Ic-A;
DE AltName: Full=Myosin I beta-A;
DE Short=MMI-beta-A;
DE Short=MMIb-A;
GN Name=myo1c-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17084356; DOI=10.1016/j.devcel.2006.09.002;
RA Sokac A.M., Schietroma C., Gundersen C.B., Bement W.M.;
RT "Myosin-1c couples assembling actin to membranes to drive compensatory
RT endocytosis.";
RL Dev. Cell 11:629-640(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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). Involved in
CC egg activation by coupling dynamic actin to membrane. {ECO:0000250,
CC ECO:0000269|PubMed:17084356}.
CC -!- SUBUNIT: Interacts (via its IQ motifs) with calmodulin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane. Cell
CC projection, stereocilium membrane {ECO:0000250}. Note=Colocalizes with
CC cortical F-actin to the plasma membrane. Colocalizes with exocytosing
CC corticale granules upon egg activation.
CC -!- DEVELOPMENTAL STAGE: Expressed during oogenesis and eggs. Up-regulated
CC by polyadenylation during meiotic maturation (at protein level).
CC {ECO:0000269|PubMed:17084356}.
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; EF026164; ABK55765.1; -; mRNA.
DR EMBL; BC060477; AAH60477.1; -; mRNA.
DR RefSeq; NP_001083453.1; NM_001089984.1.
DR AlphaFoldDB; A0MP03; -.
DR SMR; A0MP03; -.
DR PRIDE; A0MP03; -.
DR GeneID; 398934; -.
DR KEGG; xla:398934; -.
DR CTD; 398934; -.
DR Xenbase; XB-GENE-6254925; myo1c.S.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 398934; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
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 1: Evidence at protein level;
KW Acetylation; Actin-binding; ATP-binding; Cell membrane; Cell projection;
KW Cytoplasm; Membrane; Methylation; Motor protein; Myosin;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1028
FT /note="Unconventional myosin-Ic-A"
FT /id="PRO_0000369413"
FT DOMAIN 12..696
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 699..728
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 722..751
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 850..1024
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 573..595
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250"
FT MOD_RES 348
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1028 AA; 118835 MW; 02DBD48F6F9DA33B CRC64;
MENALTARDR VGVQDFVLLE NYTSEAAFIE NLRKRFKENL IYTYIGSVLV SVNPYKDLEI
YSKQHMERYR GVSFYEVSPH IYAIADNSYR SLRTERKDQC ILISGESGSG KTEASKKILQ
YYAVTCPASD QVETVKDRLL QSNPVLEAFG NAKTLRNDNS SRFGKYMDVQ FDYKGAPVGG
HILNYLLEKS RVVHQNHGER NFHIFYQLLE GGEEELLRRL GLDKNAQNYQ YLVKGQCARV
SSINDKSDWK TVRRALSIIN FNEEDIEELL SIVASVLHLG NVQFASDDHS HAQVTTENQI
KYIARLLAVD ATAFRESLIH KKIIAKGEEL NSPLNLEQAA YARDAFAKAI YGRTFSWLVR
NINKSLAYKG SDIQSIGNAS VIGLLDIYGF EVFQHNSFEQ FCINYCNEKL QQLFIELTLK
SEQEEYESEG IAWEPVQYFN NKIICDLVEE KYKGIISILD EECLRPGEAT DMTFLEKLED
TVKNHPHFVT HKFGDQKLRK SLGRDEFRPL HYAGEVNYSV VGFLDKNNDL LFRNLKEVMC
DSGNPIVHQC FDRTELTDKK RPETVATQFK NSLSKLMEIL MSKEPSYVRC IKPNDAKQAA
RFDEVLIRHQ VKYLGLIENV RVRRAGFAYR RKYEIFLHRY KSLCPETWPN WDGRAQDGVA
VLVKSLGYKP EEYKMGRTKI FIRFPKTLFA TEDALEERKQ GIATFLQARW KGYVQRRNFL
HMKHSAINIQ SWWRGNIGRK KAAKKRWAVD VVRRFVKGFI YRNNPRCPEN EYFLDYIRYS
FLMNLRRNMP KSVLDKSWPV PPPSLQEASE LLREMCMNNM VWAYCKRISP EMKQQLEQKV
VASEIFKDKK DNYPQSVPRL FINTRLGNEE INTKILQNME NQALTYAVPV VKYDRKGYKP
RRRQLLLTHN TAYIVEEAKL KQRIDYANLT GISVSSLSDN LFVLHVKCED NKQKGDVVLQ
SDHVIETLTK IAITAEKIHN INIIQGSIKF IVGNGKEGII DFTPGSELLV AKAKNGHLSV
VAPRLNSR
