MYO1C_RAT
ID MYO1C_RAT Reviewed; 1044 AA.
AC Q63355;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Unconventional myosin-Ic;
DE AltName: Full=Myosin I beta;
DE Short=MMI-beta;
DE Short=MMIb;
DE AltName: Full=Myosin heavy chain myr 2;
GN Name=Myo1c; Synonyms=Myr2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Ruppert C., Godel J., Reinhard J., Baehler M.;
RT "MYR-2 a novel class-I myosin identified in rat brain.";
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GLUT4.
RX PubMed=22918957; DOI=10.1091/mbc.e12-04-0263;
RA Boguslavsky S., Chiu T., Foley K.P., Osorio-Fuentealba C., Antonescu C.N.,
RA Bayer K.U., Bilan P.J., Klip A.;
RT "Myo1c binding to submembrane actin mediates insulin-induced tethering of
RT GLUT4 vesicles.";
RL Mol. Biol. Cell 23:4065-4078(2012).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389; SER-517; SER-845 AND
RP SER-1022, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Involved in glucose
CC transporter recycling in response to insulin by regulating movement of
CC intracellular GLUT4-containing vesicles to the plasma membrane.
CC Component of the hair cell's (the sensory cells of the inner ear)
CC adaptation-motor complex. Acts as a mediator of adaptation of
CC mechanoelectrical transduction in stereocilia of vestibular hair cells.
CC Binds phosphoinositides and links the actin cytoskeleton to cellular
CC membranes (By similarity). {ECO:0000250, ECO:0000269|PubMed:22918957}.
CC -!- SUBUNIT: Interacts (via its IQ motifs) with CALM; this precludes
CC interaction with YWHAB. Interacts with YWHAB; this precludes
CC interaction with CALM. Interacts with RPS6 and actin. Interacts (via
CC its IQ motifs) with CABP1 and CIB1; the interaction with CABP1 and CIB1
CC is calcium-dependent. Interacts (via tail domain) with PLEKHB1 (via PH
CC domain); the interaction is not affected by the presence or absence of
CC calcium and CALM. Interacts with BAZ1B, SMARCA5, POLR1A and POLR2A.
CC Component of the B-WICH complex, at least composed of SMARCA5/SNF2H,
CC BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 (By
CC similarity). Interacts with GLUT4. Interacts with LLPH (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q9WTI7,
CC ECO:0000269|PubMed:22918957}.
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}. Cell
CC projection, stereocilium membrane {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:22918957}. Note=Colocalizes with CABP1 and CIB1 at
CC cell margin, membrane ruffles and punctate regions on the cell
CC membrane. Colocalizes in adipocytes with GLUT4 at actin-based
CC membranes. Colocalizes with GLUT4 at insulin-induced ruffles at the
CC cell membrane. Localizes transiently at cell membrane to region known
CC to be enriched in PIP2. Activation of phospholipase C results in its
CC redistribution to the cytoplasm (By similarity). {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA52807.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X74800; CAA52807.1; ALT_INIT; mRNA.
DR PIR; S37146; S37146.
DR RefSeq; NP_075580.2; NM_023092.1.
DR AlphaFoldDB; Q63355; -.
DR SMR; Q63355; -.
DR BioGRID; 249326; 2.
DR IntAct; Q63355; 3.
DR STRING; 10116.ENSRNOP00000028929; -.
DR iPTMnet; Q63355; -.
DR PhosphoSitePlus; Q63355; -.
DR jPOST; Q63355; -.
DR PaxDb; Q63355; -.
DR PRIDE; Q63355; -.
DR GeneID; 65261; -.
DR KEGG; rno:65261; -.
DR CTD; 4641; -.
DR RGD; 620443; Myo1c.
DR VEuPathDB; HostDB:ENSRNOG00000004072; -.
DR eggNOG; KOG0164; Eukaryota.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; Q63355; -.
DR OMA; ENRDQCI; -.
DR OrthoDB; 122881at2759; -.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-5250924; B-WICH complex positively regulates rRNA expression.
DR PRO; PR:Q63355; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000004072; Expressed in lung and 18 other tissues.
DR Genevisible; Q63355; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0009925; C:basal plasma membrane; ISO:RGD.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:RGD.
DR GO; GO:0031941; C:filamentous actin; ISO:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032587; C:ruffle membrane; IDA:RGD.
DR GO; GO:0032420; C:stereocilium; ISO:RGD.
DR GO; GO:0032421; C:stereocilium bundle; IDA:RGD.
DR GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IDA:RGD.
DR GO; GO:0000146; F:microfilament motor activity; IDA:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0038089; P:positive regulation of cell migration by vascular endothelial growth factor signaling pathway; ISO:RGD.
DR GO; GO:1900078; P:positive regulation of cellular response to insulin stimulus; IMP:RGD.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISO:RGD.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; ISO:RGD.
DR GO; GO:0006605; P:protein targeting; ISO:RGD.
DR GO; GO:0006612; P:protein targeting to membrane; ISO:RGD.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0030050; P:vesicle transport along actin filament; ISO:RGD.
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; Calmodulin-binding; Cell membrane;
KW Cell projection; Cytoplasm; Cytoplasmic vesicle; Membrane; Methylation;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..1044
FT /note="Unconventional myosin-Ic"
FT /id="PRO_0000369414"
FT DOMAIN 28..712
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 715..744
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 738..767
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 866..1040
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 589..611
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 120..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 173..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 364
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00159"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 467
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTI7"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1044 AA; 119811 MW; F1BDEDE4CD2159A3 CRC64;
MRYRASALGS DGVRVTMESA LTARDRVGVQ DFVLLENFTS EAAFIENLRR RFRENLIYTY
IGPVLVSVNP YRDLQIYTRQ HMERYRGVSF YEVPPHLFAV ADTVYRALRT ERRDQAVMIS
GESGAGKTEA TKRLLQFYAE TCPAPERGGA VRDRLLQSNP VLEAFGNAKT LRNDNSSRFG
KYMDVQFDFK GAPVGGHILS YLLEKSRVVH QNHGERNFHV FYQLLEGGEE EALRRLGLER
NPQSYLYLVK GQCAKVSSIN DKSDWKVVRK ALSVIDFTED EVEDLLSIVA SVLHLGNIHF
AADEDSNAQV TTENQLKYLT RLLGVEGTTL REALTHRKII AKGEELLSPL NLEQAAYARD
ALAKAVYSRT FTWLVRKINR SLASKDAESP SWRSTTVLGL LDIYGFEVFQ HNSFEQFCIN
YCNEKLQQLF IELTLKSEQE EYEAEGIAWE PVQYFNNKII CDLVEEKFKG IISILDEECL
RPGEATDLTF LEKLEDTIKH HPHFLTHKLA DQKTRKSLDR GEFRLLHYAG EVTYSVTGFL
DKNNDLLFRN LKETMCSSTN PIMAQCFDKS ELSDKKRPET VATQFKMSLL QLVEILRSKE
PAYIRCIKPN DAKQPGRFDE VLIRHQVKYL GLMENLRVRR AGFAYRRKYE AFLQRYKSLC
PETWPVWTGR PQDGVAVLVR HLGYKPEEYK MGRTKIFIRF PKTLFATEDS LEVRRQSLAT
KIQAAWRGFH WRQKFLRVKR SAICIQSWWR GTLGRRKAAK RKWAAQTIRR LIRGFILRHA
PRCPENAFFL DHVRTSFLLN LRRQLPRNVL DTSWPTPPPA LREASELLRE LCMKNMVWKY
CRSISPEWKQ QLQQKAVASE IFKGKKDNYP QSVPRLFIST RLGTEEISPR VLQALGSEPI
QYAVPVVKYD RKGYKPRSRQ LLLTPSAVVI VEDAKVKQRI DYANLTGISV SSLSDSLFVL
HVQREDSKQK GDVVLQSDHV IETLTKTALS ADRVNNININ QGSITFAGGP GRDGIIDFTS
GSELLITKAK NGHLAVVAPR LNSR
