MYO1C_BOVIN
ID MYO1C_BOVIN Reviewed; 1063 AA.
AC Q27966; A5D7F3; Q28138;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Unconventional myosin-Ic;
DE AltName: Full=Myosin I beta;
DE Short=MMI-beta;
DE Short=MMIb;
GN Name=MYO1C;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH CALM, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Adrenal gland;
RX PubMed=8313976; DOI=10.1016/0014-5793(94)80378-1;
RA Zhu T., Ikebe M.;
RT "A novel myosin I from bovine adrenal gland.";
RL FEBS Lett. 339:31-36(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-164 (ISOFORM 3).
RC TISSUE=Lens;
RA Wistow G.;
RT "NEIBank analysis of cow lens.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-1063 (ISOFORM 1/2), AND INTERACTION WITH
RP CALM.
RC TISSUE=Brain;
RX PubMed=8022785; DOI=10.1073/pnas.91.14.6349;
RA Reizes O., Barylko B., Li C., Suedhof T.C., Albenisi J.P.;
RT "Domain Structure of a mammalian myosin I-beta.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6349-6353(1994).
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}.
CC -!- FUNCTION: Isoform 3 is involved in regulation of transcription.
CC Associated with transcriptional active ribosomal genes. Appears to
CC cooperate with the WICH chromatin-remodeling complex to facilitate
CC transcription. Necessary for the formation of the first phosphodiester
CC bond during transcription initiation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RPS6 and actin. Interacts (via its IQ motifs)
CC with CABP1 and CIB1; the interaction with CABP1 and CIB1 is calcium-
CC dependent. Interacts (via tail domain) with PLEKHB1 (via PH domain);
CC the interaction is not affected by the presence or absence of calcium
CC and CALM. Interacts with POLR1A and POLR2A. Component of the B-WICH
CC complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK,
CC MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with YWHAB; this precludes
CC interaction with CALM. Likewise, interaction with CALM precludes
CC interaction with YWHAB (By similarity). Interacts (via its IQ motifs)
CC with CALM. Interacts with LLPH (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9WTI7, ECO:0000269|PubMed:8022785,
CC ECO:0000269|PubMed:8313976}.
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}. Note=Colocalizes with CABP1 and CIB1 at cell margin,
CC membrane ruffles and punctate regions on the cell membrane. Colocalizes
CC in adipocytes with GLUT4 at actin-based membranes. Colocalizes with
CC GLUT4 at insulin-induced ruffles at the cell membrane. Localizes
CC transiently at cell membrane to region known to be enriched in PIP2.
CC Activation of phospholipase C results in its redistribution to the
CC cytoplasm (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleolus {ECO:0000250}.
CC Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nuclear pore complex
CC {ECO:0000250}. Note=In the nucleolus, is localized predominantly in
CC dense fibrillar component (DFC) and in granular component (GC).
CC Accumulates strongly in DFC and GC during activation of transcription.
CC Colocalizes with transcription sites. Colocalizes in the granular
CC cortex at the periphery of the nucleolus with RPS6. Colocalizes in
CC nucleoplasm with RPS6 and actin that are in contact with RNP particles.
CC Colocalizes with RPS6 at the nuclear pore level. Colocalizes with RNA
CC polymerase II in the nucleus. Colocalizes with RNA polymerase I in
CC nucleoli (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q27966-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q27966-2; Sequence=VSP_036860;
CC Name=3;
CC IsoId=Q27966-3; Sequence=VSP_036859;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8313976}.
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 the myosin
CC tail domain (PH-like) present in its tail domain (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Isoform 2 contains a N-acetylmethionine at position 1.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI40535.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U03420; AAA17565.1; -; mRNA.
DR EMBL; BC140534; AAI40535.1; ALT_INIT; mRNA.
DR EMBL; EG705719; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; Z22852; CAA80476.1; -; mRNA.
DR PIR; S41749; S41749.
DR RefSeq; NP_776821.3; NM_174396.3. [Q27966-1]
DR RefSeq; XP_005220121.1; XM_005220064.1. [Q27966-3]
DR RefSeq; XP_005220122.1; XM_005220065.2. [Q27966-2]
DR AlphaFoldDB; Q27966; -.
DR SMR; Q27966; -.
DR STRING; 9913.ENSBTAP00000029554; -.
DR PaxDb; Q27966; -.
DR PeptideAtlas; Q27966; -.
DR PRIDE; Q27966; -.
DR Ensembl; ENSBTAT00000029555; ENSBTAP00000029554; ENSBTAG00000001332. [Q27966-1]
DR Ensembl; ENSBTAT00000084966; ENSBTAP00000067851; ENSBTAG00000001332. [Q27966-3]
DR GeneID; 281937; -.
DR KEGG; bta:281937; -.
DR CTD; 4641; -.
DR VEuPathDB; HostDB:ENSBTAG00000001332; -.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000157915; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; Q27966; -.
DR OMA; ENRDQCI; -.
DR OrthoDB; 122881at2759; -.
DR TreeFam; TF312960; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000001332; Expressed in trachea and 107 other tissues.
DR ExpressionAtlas; Q27966; baseline and differential.
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:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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:0005516; F:calmodulin 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:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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; 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; Alternative splicing; ATP-binding;
KW Calmodulin-binding; Cell membrane; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Membrane; Methylation; Motor protein; mRNA transport;
KW Myosin; Nuclear pore complex; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..1063
FT /note="Unconventional myosin-Ic"
FT /id="PRO_0000226048"
FT DOMAIN 47..731
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 734..757
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 758..786
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 885..1059
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 608..630
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 139..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 192..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 383
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00159"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00159"
FT MOD_RES 486
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTI7"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63355"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63355"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63355"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8313976"
FT /id="VSP_036860"
FT VAR_SEQ 1..25
FT /note="MALQVELIPTGEIIRVVHPHRPCKL -> MRYRAS (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_036859"
FT CONFLICT 42
FT /note="A -> C (in Ref. 4; CAA80476)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="R -> G (in Ref. 1; AAA17565)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="H -> N (in Ref. 4; CAA80476)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="N -> K (in Ref. 4; CAA80476)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="D -> G (in Ref. 1; AAA17565)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="N -> I (in Ref. 4; CAA80476)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="C -> F (in Ref. 4; CAA80476)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="D -> S (in Ref. 1; AAA17565)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="P -> R (in Ref. 1; AAA17565)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="G -> A (in Ref. 4; CAA80476)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="V -> L (in Ref. 4; CAA80476)"
FT /evidence="ECO:0000305"
FT MOD_RES Q27966-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1063 AA; 121936 MW; 682486667418FA51 CRC64;
MALQVELIPT GEIIRVVHPH RPCKLALGSD GVRVTMESAL TARDRVGVQD FVLLENFTSE
AAFIENLRRR FRENLIYTYI GPVLVSVNPY RDLQIYSRQH MERYRGVSFY EVPPHLFAVA
DTVYRALRTE RRDQAVMISG ESGAGKTEAT KRLLQFYAET CPAPERGGAV RDRLLQSNPV
LEAFGNAKTL RNDNSSRFGK YMDVQFDFKG APVGGHILSY LLEKSRVVHQ NHGERNFHIF
YQLLEGGEEE TLRRLGLERN PQSYLYLVKG QCAKVSSIND KSDWKVVRKA LTVIDFTEDE
VEDLLSIVAS VLHLGNTHFA ADEESNAQVT TENQLKYLTR LLGVEGSTLR EALTHRKIIA
KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVAKINRS LASKDAESPS WRSTTVLGLL
DIYGFEVFQH NSFEQFCINY CNEKLQQLFI ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC
DLVEEKFKGI ISILDEECLR PGEATDLTFL EKLEDTIKQH PHFLTHKLAD QRTRKSLDRG
EFRLLHYAGE VTYNVTGFLD KNNDLLFRNL KETMCSSENP ILGQCFDRSE LSDKKRPETV
ATQFKMSLLE LVEILKSKEP AYVRCIKPND SKQPGRFDEV LIRHQVKYLG LMENLRVRRA
GFAYRRKYEA FLQRYKSLCP ETWPTWTGRP QDGVTVLVRH LGYKPEEYKM GRTKIFIRFP
KTLFATEDAL EIRRQSLATK IQATWRGFHC RQKFLRVKRS AICIQSWWRG TLGRRKAAKR
KWAAQTIRRL IQGFILRHAP RCPENAFFVD HVRTSFLLNL RRQLPRNILD TSWPTPPPAL
REASELLREL CRKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR
LGADEINPRV LQALGSEPIQ YAVPVVKYDR KGYKPRSRQL LLTPNAVVIV EDAKVKQRIE
YTNLTGISVS SLSDSLFVLH VQREDNKQKG DVVLQSDHVI ETLTKTALSA DRVNNININQ
GSITFAGGPG RDGIIDFTPG SELLITKAKN GHLAVVAPRL NSR
