MYO1D_HUMAN
ID MYO1D_HUMAN Reviewed; 1006 AA.
AC O94832; A6H8V3; Q8NHP9;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Unconventional myosin-Id;
GN Name=MYO1D; Synonyms=KIAA0727;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Yamakawa H., Ohara O.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 333-1006.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-11; 239-248; 534-544; 791-801 AND 985-994, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Dozynkiewicz M., Norman J.C.;
RL Submitted (MAR-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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 -!- TISSUE SPECIFICITY: Expressed in many tissues. Highest levels in brain,
CC followed by lung and ovary; expression is lowest in spleen.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34447.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB018270; BAA34447.2; ALT_INIT; mRNA.
DR EMBL; BC146763; AAI46764.1; -; mRNA.
DR CCDS; CCDS32615.1; -.
DR RefSeq; NP_001290208.1; NM_001303279.1.
DR RefSeq; NP_056009.1; NM_015194.2.
DR AlphaFoldDB; O94832; -.
DR SMR; O94832; -.
DR BioGRID; 110726; 175.
DR IntAct; O94832; 55.
DR MINT; O94832; -.
DR STRING; 9606.ENSP00000324527; -.
DR GlyGen; O94832; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O94832; -.
DR PhosphoSitePlus; O94832; -.
DR SwissPalm; O94832; -.
DR BioMuta; MYO1D; -.
DR EPD; O94832; -.
DR jPOST; O94832; -.
DR MassIVE; O94832; -.
DR MaxQB; O94832; -.
DR PaxDb; O94832; -.
DR PeptideAtlas; O94832; -.
DR PRIDE; O94832; -.
DR ProteomicsDB; 50476; -.
DR Antibodypedia; 27274; 109 antibodies from 24 providers.
DR DNASU; 4642; -.
DR Ensembl; ENST00000318217.10; ENSP00000324527.5; ENSG00000176658.17.
DR GeneID; 4642; -.
DR KEGG; hsa:4642; -.
DR MANE-Select; ENST00000318217.10; ENSP00000324527.5; NM_015194.3; NP_056009.1.
DR UCSC; uc002hho.2; human.
DR CTD; 4642; -.
DR DisGeNET; 4642; -.
DR GeneCards; MYO1D; -.
DR HGNC; HGNC:7598; MYO1D.
DR HPA; ENSG00000176658; Tissue enhanced (intestine).
DR MIM; 606539; gene.
DR neXtProt; NX_O94832; -.
DR OpenTargets; ENSG00000176658; -.
DR PharmGKB; PA31400; -.
DR VEuPathDB; HostDB:ENSG00000176658; -.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000157411; -.
DR InParanoid; O94832; -.
DR OMA; QDVKYGH; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; O94832; -.
DR TreeFam; TF312960; -.
DR PathwayCommons; O94832; -.
DR SignaLink; O94832; -.
DR BioGRID-ORCS; 4642; 7 hits in 1072 CRISPR screens.
DR ChiTaRS; MYO1D; human.
DR GenomeRNAi; 4642; -.
DR Pharos; O94832; Tbio.
DR PRO; PR:O94832; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O94832; protein.
DR Bgee; ENSG00000176658; Expressed in ascending aorta and 171 other tissues.
DR ExpressionAtlas; O94832; baseline and differential.
DR Genevisible; O94832; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
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:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
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:0005886; C:plasma membrane; IBA:GO_Central.
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:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
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 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; 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 1: Evidence at protein level;
KW Acetylation; Actin-binding; ATP-binding; Calmodulin-binding;
KW Cell projection; Cytoplasm; Direct protein sequencing; Endosome;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..1006
FT /note="Unconventional myosin-Id"
FT /id="PRO_0000123447"
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|PROSITE-ProRule:PRU00782"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 536
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5SYD0"
FT VARIANT 765
FT /note="P -> S (in dbSNP:rs7209106)"
FT /id="VAR_050210"
FT VARIANT 771
FT /note="R -> H (in dbSNP:rs7215958)"
FT /id="VAR_050211"
SQ SEQUENCE 1006 AA; 116202 MW; A8BB08450887168E CRC64;
MAEQESLEFG KADFVLMDTV SMPEFMANLR LRFEKGRIYT FIGEVVVSVN PYKLLNIYGR
DTIEQYKGRE LYERPPHLFA IADAAYKAMK RRSKDTCIVI SGESGAGKTE ASKYIMQYIA
AITNPSQRAE VERVKNMLLK SNCVLEAFGN AKTNRNDNSS RFGKYMDINF DFKGDPIGGH
INNYLLEKSR VIVQQPGERS FHSFYQLLQG GSEQMLRSLH LQKSLSSYNY IHVGAQLKSS
INDAAEFRVV ADAMKVIGFK PEEIQTVYKI LAAILHLGNL KFVVDGDTPL IENGKVVSII
AELLSTKTDM VEKALLYRTV ATGRDIIDKQ HTEQEASYGR DAFAKAIYER LFCWIVTRIN
DIIEVKNYDT TIHGKNTVIG VLDIYGFEIF DNNSFEQFCI NYCNEKLQQL FIQLVLKQEQ
EEYQREGIPW KHIDYFNNQI IVDLVEQQHK GIIAILDDAC MNVGKVTDEM FLEALNSKLG
KHAHFSSRKL CASDKILEFD RDFRIRHYAG DVVYSVIGFI DKNKDTLFQD FKRLMYNSSN
PVLKNMWPEG KLSITEVTKR PLTAATLFKN SMIALVDNLA SKEPYYVRCI KPNDKKSPQI
FDDERCRHQV EYLGLLENVR VRRAGFAFRQ TYEKFLHRYK MISEFTWPNH DLPSDKEAVK
KLIERCGFQD DVAYGKTKIF IRTPRTLFTL EELRAQMLIR IVLFLQKVWR GTLARMRYKR
TKAALTIIRY YRRYKVKSYI HEVARRFHGV KTMRDYGKHV KWPSPPKVLR RFEEALQTIF
NRWRASQLIK SIPASDLPQV RAKVAAVEML KGQRADLGLQ RAWEGNYLAS KPDTPQTSGT
FVPVANELKR KDKYMNVLFS CHVRKVNRFS KVEDRAIFVT DRHLYKMDPT KQYKVMKTIP
LYNLTGLSVS NGKDQLVVFH TKDNKDLIVC LFSKQPTHES RIGELVGVLV NHFKSEKRHL
QVNVTNPVQC SLHGKKCTVS VETRLNQPQP DFTKNRSGFI LSVPGN
