MYO1D_CANLF
ID MYO1D_CANLF Reviewed; 1006 AA.
AC F1PRN2;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Unconventional myosin-Id;
DE AltName: Full=Unconventional myosin Myr 4 {ECO:0000303|PubMed:11208135};
GN Name=MYO1D;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615 {ECO:0000312|Proteomes:UP000002254};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CALMODULIN.
RX PubMed=11208135; DOI=10.1034/j.1600-0854.2000.010607.x;
RA Huber L.A., Fialka I., Paiha K., Hunziker W., Sacks D.B., Baehler M.,
RA Way M., Gagescu R., Gruenberg J.;
RT "Both calmodulin and the unconventional myosin Myr4 regulate membrane
RT trafficking along the recycling pathway of MDCK cells.";
RL Traffic 1:494-503(2000).
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 (PubMed:11208135). Required for
CC normal planar cell polarity in ciliated tracheal cells, for normal
CC rotational polarity of cilia, and for coordinated, unidirectional
CC ciliary movement in the trachea. Required for normal, polarized cilia
CC organization in brain ependymal epithelial cells (By similarity).
CC {ECO:0000250|UniProtKB:Q63357, ECO:0000269|PubMed:11208135}.
CC -!- SUBUNIT: Interacts (via the two IQ motifs) with calmodulin
CC (PubMed:11208135). Binds an additional calmodulin chain via a third, C-
CC terminal region. Interacts with F-actin (By similarity).
CC {ECO:0000250|UniProtKB:Q63357, ECO:0000269|PubMed:11208135}.
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:0000269|PubMed:11208135}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:11208135}. Note=Colocalizes with the actin
CC cytoskeleton in the cell cortex close to the apical cell membrane
CC (PubMed:11208135). Colocalizes with cytoplasmic puncta that are
CC reminiscent of transport vesicles (By similarity).
CC {ECO:0000250|UniProtKB:Q63357, ECO:0000269|PubMed:11208135}.
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:0000255|PROSITE-ProRule:PRU00782}.
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; AAEX03006641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX03006642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_548273.3; XM_548273.5.
DR AlphaFoldDB; F1PRN2; -.
DR SMR; F1PRN2; -.
DR STRING; 9612.ENSCAFP00000027140; -.
DR PaxDb; F1PRN2; -.
DR PRIDE; F1PRN2; -.
DR Ensembl; ENSCAFT00000107115; ENSCAFP00000068611; ENSCAFG00000018370.
DR Ensembl; ENSCAFT00030030180; ENSCAFP00030026319; ENSCAFG00030016064.
DR Ensembl; ENSCAFT00040021996; ENSCAFP00040019081; ENSCAFG00040011926.
DR Ensembl; ENSCAFT00845020951; ENSCAFP00845016461; ENSCAFG00845011784.
DR GeneID; 491153; -.
DR KEGG; cfa:491153; -.
DR CTD; 4642; -.
DR VEuPathDB; HostDB:ENSCAFG00845011784; -.
DR VGNC; VGNC:43563; MYO1D.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000157411; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; F1PRN2; -.
DR OMA; QDVKYGH; -.
DR OrthoDB; 122881at2759; -.
DR TreeFam; TF312960; -.
DR Proteomes; UP000002254; Chromosome 9.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0061502; P:early endosome to recycling endosome transport; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; 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; 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; Endocytosis; 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_0000446321"
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: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; 116036 MW; 532B0B4957A07112 CRC64;
MAEQESLEFG KADFVLMDTV SMPEFMANLR LRFEKGRIYT FIGEVVVSVN PYKALNIYGR
DTIEQYKGRE LYERPPHLFA IADAAYKAMK RRSKDTCIVI SGESGAGKTE ASKYIMQYIA
AITNPSQRAE VERVKNMLLK SNCVLEAFGN AKTNRNDNSS RFGKYMDINF DFKGDPIGGH
INNYLLEKSR VIVQQPGERS FHSFYQLLQG GSEQMLRSLH LQKSLSSYNY IHVGAQLKSS
INDAAEFKVV ADAMKVIGFK PEETQTVYKI LAAILHLGNL KFMVDGDTPL IENGKVVSII
AELLSTKTDM VEKALLYRTV ATGRDIIDKQ HTEQEASYGR DAFAKAIYER LFCWIVTRIN
DIIEVKNYDT TIHGKNTVIG VLDIYGFEIF DNNSFEQFCI NYCNEKLQQL FIQLVLKQEQ
EEYQREGIPW KHIDYFNNQI IVDLVEQQHK GIIAILDDAC MNVGKVTDEM FLEALNSKLG
KHGHFSSRKL CASDKILEFD RDFRIRHYAG DVVYSVIGFI DKNKDTLFQD FKRLLYNSSN
PVLKNMWPEG KLSITEVTKR PLTAATLFKN SMIALVDNLA SKEPYYVRCI KPNDKKSPQI
FDDERCRHQV EYLGLLENVR VRRAGFAFRQ TYEKFLHRYK MISEFTWPNH DLPSDKEAVK
KLIEHCGFQD DVAYGKTKIF IRTPRTLFTL EELRAQMLIR IVLFLQKVWR GTLARMRYKR
TKAALTIIRY YRHYKVKSYI QEVARRFHGV KTMKDHGKHV KWPTPPKVLR RFEEALQAIF
NRWRASQLIK SLPASDLPQV RAKVAAMEML KGQRADLGLQ RAWEGNYLAS KPDTPQTSGT
FVPVANELKR KDKYMNVLFS CHVRKVNRFS KVEDRAIFVT DRHLYKMDPT KQYKVMKTIP
LYNLTGLSVS NGKDQLVVFH TKDNKDLIVC LFSKQPTHES RIGELVGVLV NHFKSEKRHL
QVNVTNPVQC SLHGKKCTVS VETRLNQPEP DFTKNRSGFI LSVPGN
