MYO1C_CHICK
ID MYO1C_CHICK Reviewed; 1028 AA.
AC Q5ZLA6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Unconventional myosin-Ic;
DE AltName: Full=Myosin I beta;
DE Short=MMI-beta;
DE Short=MMIb;
GN Name=MYO1C; ORFNames=RCJMB04_6o17;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 -!- DOMAIN: Binds directly to large unilamellar vesicles (LUVs) containing
CC phosphatidylinositol 4,5-bisphosphate (PIP2) or inositol 1,4,5-
CC trisphosphate (InsP3). The PIP2-binding site corresponds to a putative
CC PH domain present in its tail domain (By similarity). {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; AJ719828; CAG31487.1; -; mRNA.
DR RefSeq; NP_001006220.2; NM_001006220.2.
DR AlphaFoldDB; Q5ZLA6; -.
DR SMR; Q5ZLA6; -.
DR STRING; 9031.ENSGALP00000004265; -.
DR PaxDb; Q5ZLA6; -.
DR GeneID; 417555; -.
DR KEGG; gga:417555; -.
DR CTD; 4641; -.
DR VEuPathDB; HostDB:geneid_417555; -.
DR eggNOG; KOG0164; Eukaryota.
DR InParanoid; Q5ZLA6; -.
DR PhylomeDB; Q5ZLA6; -.
DR PRO; PR:Q5ZLA6; -.
DR Proteomes; UP000000539; Unplaced.
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: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; 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 2: Evidence at transcript level;
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..1028
FT /note="Unconventional myosin-Ic"
FT /id="PRO_0000369410"
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 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 348
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1028 AA; 118907 MW; 12336594355B3F2E CRC64;
MESALTARDR VGVQDFVLLE NFTSEAAFIE NLRKRFKENL IYTYIGSVLV SVNPYKELEI
YSKQNMERYR GVSFYEVSPH LYAIADNSYR SLRTERKDQC ILISGESGAG KTEATKKILQ
YYAVTCPASQ QVETVKDRLL QSNPVLEAFG NTKTLRNDNS SRFGKYMDVQ FDYRGAPVGG
HILNYLLEKS RVVHQNHGER NFHIFYQLLE GGEEDLLRRL GLEKNPQQYH YLVKGHCARV
SSINDKNDWK VVRRALSIIS FNDNEVEDLL SIVASVLHLG NVQFAADEQG NAQVTTENQI
KYLARLLAVE GSVLRDALIH KKIIAKGEEL ISPLNLEQAA YARDALAKAI YGRTFSWLVN
KVNKSLAYKE GEFPGWRSTT VLGLLDIYGF EVFQHNSFEQ FCINYCNEKL QQLFIELTLK
SEQEEYESEG IAWEPVQYFN NKIICDLVEE KFKGIISILD EECLRPGDAT DTTFLEKLEE
TVKNHPHFLT HKLADQKTRK SLGREEFRLL HYAGEVTYSV AGFLDKNNDL LFRNLKETMC
NSENPIINQC FDRTELTDKK RPETAATQFK NSLSKLMEIL MSKEPSYIRC IKPNDAKQAD
RFDEVLIRHQ VKYLGLMENL RVRRAGFAYR RKYEVFLQRY KSLCPETWPT WDGRPHDGVA
VLVKHLGYKQ EEYKMGRTKI FIRFPKTLFA TEDALEVRKQ SLATKMQATW RGFYRRKKFL
HMKHSAIAIQ SWWRGTLGRR KAAKRKWAVQ TIRRFIKGFI YRNHPRCPEN EYFLDYIRFS
FLMNLKRNLP KNVLDKSWPT PPPSLCEASQ LLRQLCMQNM VWTYCKRISP EWKQQLEQKV
IASEIFKGKK DNYPQSVPRL FINTRLGNEE INAKVLQALE NEAIKYAVPV IKYDRKGYKA
RSRQLLLTQN AVIIVEDSKI KQRIDYANLT GISVSSLSDN LFVLHVHCED NKQKGDVVLQ
SDHVIETLTK TAMRADKVNN ININQGSIKF TVGQGKEGII DFISGSELLI AKAKNGHLTV
VAPRLNSR
