MYO1D_BOVIN
ID MYO1D_BOVIN Reviewed; 1006 AA.
AC Q17R14;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Unconventional myosin-Id;
GN Name=MYO1D;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Unconventional myosin that functions as actin-based motor
CC protein with ATPase activity (By similarity). Plays a role in endosomal
CC protein trafficking, and especially in the transfer of cargo proteins
CC from early to recycling endosomes (By similarity). Required for normal
CC planar cell polarity in ciliated tracheal cells, for normal rotational
CC polarity of cilia, and for coordinated, unidirectional ciliary movement
CC in the trachea. Required for normal, polarized cilia organization in
CC brain ependymal epithelial cells (By similarity).
CC {ECO:0000250|UniProtKB:F1PRN2, ECO:0000250|UniProtKB:Q63357}.
CC -!- SUBUNIT: Interacts (via the two IQ motifs) with calmodulin. Binds an
CC additional calmodulin chain via a third, C-terminal region. Interacts
CC with F-actin. {ECO:0000250|UniProtKB:Q63357}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q63357}.
CC Perikaryon {ECO:0000250|UniProtKB:Q63357}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q63357}. Early endosome
CC {ECO:0000250|UniProtKB:F1PRN2}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q63357}. Note=Colocalizes with the actin
CC cytoskeleton in the cell cortex close to the apical cell membrane.
CC Colocalizes with cytoplasmic puncta that are reminiscent of transport
CC vesicles. {ECO:0000250|UniProtKB:Q63357}.
CC -!- DOMAIN: Binds a calmodulin chain via each of the two IQ domains. IQ
CC domain 1 mediates interaction with calmodulin both in the presence and
CC in the absence of Ca(2+). IQ domain 2 mediates interaction with
CC calmodulin in the presence of Ca(2+). {ECO:0000250|UniProtKB:Q63357}.
CC -!- DOMAIN: The TH1 domain is required for activity in complementing
CC zebrafish defects in Kupffer's vesicle lumen size.
CC {ECO:0000250|UniProtKB:Q63357}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Contrary to the situation in zebrafish, xenopus and
CC drosophila, mammalian MYO1D defects have no effects on left-right body
CC asymmetry. {ECO:0000250|UniProtKB:Q63357}.
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; BC118080; AAI18081.1; -; mRNA.
DR RefSeq; NP_001069306.1; NM_001075838.2.
DR AlphaFoldDB; Q17R14; -.
DR SMR; Q17R14; -.
DR STRING; 9913.ENSBTAP00000020634; -.
DR PaxDb; Q17R14; -.
DR PRIDE; Q17R14; -.
DR GeneID; 522967; -.
DR KEGG; bta:522967; -.
DR CTD; 4642; -.
DR eggNOG; KOG0164; Eukaryota.
DR InParanoid; Q17R14; -.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0097440; C:apical dendrite; ISS:UniProtKB.
DR GO; GO:0030673; C:axolemma; ISS:UniProtKB.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; ISS:UniProtKB.
DR GO; GO:0016459; C:myosin complex; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
DR GO; GO:0051641; P:cellular localization; ISS:UniProtKB.
DR GO; GO:0061502; P:early endosome to recycling endosome transport; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; ATP-binding; Calmodulin-binding;
KW Cell projection; Cytoplasm; Endosome; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O94832"
FT CHAIN 2..1006
FT /note="Unconventional myosin-Id"
FT /id="PRO_0000274173"
FT DOMAIN 9..695
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 699..719
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 721..741
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 812..1005
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 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O94832"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94832"
FT MOD_RES 536
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5SYD0"
SQ SEQUENCE 1006 AA; 115939 MW; A7777735CA094CCF CRC64;
MAEQESLEFG KADFVLMDTV SMPEFMANLR LRFEKGRIYT FIGEVVVSVN PYKSLNIYGR
DTIEQYKGRE LYERPPHLFA IADAAYKAMK RRSKDTCIVI SGESGAGKTE ASKYIMQYIA
AITNPSQRAE IERVKNMLLK SNCVLEAFGN AKTNRNDNSS RFGKYMDINF DFKGDPIGGH
INNYLLEKSR VIVQQPGERS FHSFYQLLQG GSDQMLRSLH LQKSLSSYSY IHVGAQLKSS
INDAAEFKVV ADAMKVIGFK PEEIQTAYKI LAAILHLGNL KFVVDGDTTL IEDGKLVSII
AELLSTKTDM VEKALLYRTV ATGRDVIDKQ HTEQEASYGR DAFAKAIYER LFCWIVSRIN
DIIAVKNSDT TIHGKNTVIG VLDIYGFEIF DNNSFEQFCI NYCNEKLQQL FIQLVLKQEQ
EEYQREGIPW KHIDYFNNQI IVDLVEQQHK GIIAILDDAC MNVGKVTDEM FLEALNSKLG
KHGHFSSRKL CASDKILEFD RDFRIRHYAG DVVYSVVGFI DKNKDTLFQD FKRLMYNSSN
PVLKNMWPEG KLSITEVTRR PLTAATLFKN SMIALVDNLA SKEPYYVRCI KPNDMKSPQI
FDDERCRHQV EYLGLLENVR VRRAGFAFRQ TYEKFLHRYK MISEFTWPNH DLPSDKEAVK
KLVEYCGFQD DVAYGKTKIF IRTPRTLFTL EELRAQMLVR IVLFLQKVWR GTLARMRYKR
TKAALTIIRY YRRYKVKSYI HEVARRFHGI KTMRDYGKHV QWPTPPKVLH RFEEVLQAVF
NRWRASQLIK TIPASDLPQV RAKVAAVEML KGQRADLGLQ RAWEGNYLAS KPDTPQTSGT
FVPVANELKR KDKYMNVLFS CHVRKVNRFS KVEDRAIFVT DRHLYKMDPT KQYKVMKTIP
LYNLTGLSVS NGKDQLVVFH TKDNKDLIVC LFSKQPTHES RIGELVGVLV NHFKSEKRHL
QVNVTNPVQC SLHGKKCTVS VETRLNQPQP DFTKNRSGFI LSVPGN
