MYO1C_HUMAN
ID MYO1C_HUMAN Reviewed; 1063 AA.
AC O00159; Q4LE56; Q6NVJ7; Q86Y95;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Unconventional myosin-Ic;
DE AltName: Full=Myosin I beta;
DE Short=MMI-beta;
DE Short=MMIb;
GN Name=MYO1C;
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] (ISOFORM 2), AND VARIANTS ILE-795 AND ARG-826.
RC TISSUE=Kidney;
RX PubMed=9119401; DOI=10.1006/geno.1996.4526;
RA Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P.,
RA Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G., Weil D.,
RA Pujol R., Petit C.;
RT "Cloning of the genes encoding two murine and human cochlear unconventional
RT type I myosins.";
RL Genomics 40:332-341(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ILE-795
RP AND ARG-826.
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ILE-795
RP AND ARG-826.
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ILE-795 AND ARG-826.
RC TISSUE=Eye, and Liver;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-206 (ISOFORM 3).
RC TISSUE=Teratocarcinoma;
RA Strausberg R.L.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 36-43; 92-98; 104-125; 133-146; 172-188; 198-209;
RP 255-269; 341-350; 357-396; 400-412; 562-568; 606-624; 633-643; 648-656;
RP 666-674; 715-734; 814-822; 827-841; 875-884; 886-894; 901-930; 937-956 AND
RP 988-1047, ACETYLATION AT MET-1 (ISOFORM 2), METHYLATION AT LYS-383, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F.;
RL Submitted (FEB-2008) to UniProtKB.
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16133118; DOI=10.1007/s00418-005-0042-8;
RA Kysela K., Philimonenko A.A., Philimonenko V.V., Janacek J., Kahle M.,
RA Hozak P.;
RT "Nuclear distribution of actin and myosin I depends on transcriptional
RT activity of the cell.";
RL Histochem. Cell Biol. 124:347-358(2005).
RN [9]
RP INTERACTION WITH RPS6 AND ACTIN, AND SUBCELLULAR LOCATION.
RX PubMed=16877530; DOI=10.1096/fj.05-5278fje;
RA Cisterna B., Necchi D., Prosperi E., Biggiogera M.;
RT "Small ribosomal subunits associate with nuclear myosin and actin in
RT transit to the nuclear pores.";
RL FASEB J. 20:1901-1903(2006).
RN [10]
RP IDENTIFICATION IN THE B-WICH COMPLEX.
RX PubMed=16603771; DOI=10.1074/jbc.m600233200;
RA Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.;
RT "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear
RT proteins in transcription.";
RL J. Biol. Chem. 281:16264-16271(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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).
RN [14]
RP ALTERNATIVE SPLICING (ISOFORM 1), AND SUBCELLULAR LOCATION (ISOFORM 1).
RX PubMed=22736583; DOI=10.1002/cm.21040;
RA Ihnatovych I., Migocka-Patrzalek M., Dukh M., Hofmann W.A.;
RT "Identification and characterization of a novel myosin Ic isoform that
RT localizes to the nucleus.";
RL Cytoskeleton 69:555-565(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS) OF 36-760 (ISOFORM 2) IN COMPLEX
RP WITH ADP ORTHOVANADATE AND CALM, INTERACTION WITH CALM AND YWHAB, FUNCTION,
RP ACTIN-BINDING, FUNCTION IN ACTIN-DEPENDENT ATP HYDROLYSIS, AND MUTAGENESIS
RP OF SER-736.
RX PubMed=24636949; DOI=10.1016/j.jmb.2014.03.004;
RA Stefan Munnich M.H., Manstein D.J.;
RT "Crystal structure of human myosin 1c - the motor in GLUT4 exocytosis:
RT implications for Ca(2+)-regulation and 14-3-3 binding.";
RL J. Mol. Biol. 426:2070-2081(2014).
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. {ECO:0000269|PubMed:24636949}.
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 GLUT4 (By similarity). Interacts (via its IQ
CC motifs) with CABP1 and CIB1; the interaction with CABP1 and CIB1 is
CC 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 POLR1A and POLR2A. Component of the B-
CC WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1,
CC DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts (via its IQ motifs)
CC with CALM; this precludes interaction with YWHAB. Interacts with YWHAB;
CC this precludes interaction with CALM. Interacts with RPS6 and actin.
CC Interacts with LLPH (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9WTI7, ECO:0000269|PubMed:16603771,
CC ECO:0000269|PubMed:16877530, ECO:0000269|PubMed:24636949}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:22736583}. Nucleus {ECO:0000269|PubMed:22736583}.
CC Note=Colocalizes with RNA polymerase II. Absent from nucleoli and does
CC not colocalize with RNA polymerase I. Translocates to nuclear speckles
CC upon exposure to inhibitors of RNA polymerase II transcription.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cell projection, stereocilium membrane
CC {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasmic
CC vesicle {ECO:0000250}. Note=Colocalizes with CABP1 and CIB1 at cell
CC margin, membrane ruffles and punctate regions on the cell membrane.
CC Colocalizes in adipocytes with GLUT4 at actin-based membranes.
CC Colocalizes with GLUT4 at insulin-induced ruffles at the cell membrane.
CC Localizes transiently at cell membrane to region known to be enriched
CC in PIP2. Activation of phospholipase C results in its redistribution to
CC the cytoplasm (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleoplasm. Nucleus,
CC nucleolus. Nucleus, nuclear pore complex. Note=Colocalizes with RNA
CC polymerase II in the nucleus. Colocalizes with RNA polymerase I in
CC nucleoli (By similarity). In the nucleolus, is localized predominantly
CC in 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. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A;
CC IsoId=O00159-1; Sequence=Displayed;
CC Name=2; Synonyms=C;
CC IsoId=O00159-2; Sequence=VSP_036861;
CC Name=3; Synonyms=B, Nuclear myosin 1, NM1, NMI;
CC IsoId=O00159-3; Sequence=VSP_036862;
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 -!- 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=AAH68013.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE06097.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF85599.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X98507; CAA67131.1; -; mRNA.
DR EMBL; AK292910; BAF85599.1; ALT_INIT; mRNA.
DR EMBL; AB210015; BAE06097.1; ALT_INIT; mRNA.
DR EMBL; AC100748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC044891; AAH44891.2; -; mRNA.
DR EMBL; BC068013; AAH68013.1; ALT_INIT; mRNA.
DR EMBL; BU855623; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS11003.1; -. [O00159-2]
DR CCDS; CCDS42226.1; -. [O00159-1]
DR CCDS; CCDS45562.1; -. [O00159-3]
DR PIR; A59253; A59253.
DR RefSeq; NP_001074248.1; NM_001080779.1. [O00159-1]
DR RefSeq; NP_001074419.1; NM_001080950.1. [O00159-3]
DR RefSeq; NP_203693.3; NM_033375.4. [O00159-2]
DR PDB; 4BYF; X-ray; 2.74 A; A/C=36-760.
DR PDBsum; 4BYF; -.
DR AlphaFoldDB; O00159; -.
DR SMR; O00159; -.
DR BioGRID; 110725; 343.
DR ComplexPortal; CPX-1099; B-WICH chromatin remodelling complex. [O00159-3]
DR CORUM; O00159; -.
DR DIP; DIP-33109N; -.
DR IntAct; O00159; 213.
DR MINT; O00159; -.
DR STRING; 9606.ENSP00000352834; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; O00159; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00159; -.
DR PhosphoSitePlus; O00159; -.
DR SwissPalm; O00159; -.
DR BioMuta; MYO1C; -.
DR EPD; O00159; -.
DR jPOST; O00159; -.
DR MassIVE; O00159; -.
DR MaxQB; O00159; -.
DR PaxDb; O00159; -.
DR PeptideAtlas; O00159; -.
DR PRIDE; O00159; -.
DR ProteomicsDB; 47744; -. [O00159-1]
DR ProteomicsDB; 47745; -. [O00159-2]
DR ProteomicsDB; 47746; -. [O00159-3]
DR Antibodypedia; 953; 177 antibodies from 27 providers.
DR DNASU; 4641; -.
DR Ensembl; ENST00000361007.7; ENSP00000354283.2; ENSG00000197879.17. [O00159-2]
DR Ensembl; ENST00000570984.7; ENSP00000459271.3; ENSG00000197879.17. [O00159-2]
DR Ensembl; ENST00000575158.5; ENSP00000459174.1; ENSG00000197879.17. [O00159-2]
DR Ensembl; ENST00000646049.1; ENSP00000493973.1; ENSG00000197879.17. [O00159-2]
DR Ensembl; ENST00000648446.1; ENSP00000496799.1; ENSG00000197879.17. [O00159-3]
DR Ensembl; ENST00000648651.1; ENSP00000496954.1; ENSG00000197879.17. [O00159-1]
DR GeneID; 4641; -.
DR KEGG; hsa:4641; -.
DR MANE-Select; ENST00000648651.1; ENSP00000496954.1; NM_001080779.2; NP_001074248.1.
DR UCSC; uc002fsn.4; human. [O00159-1]
DR CTD; 4641; -.
DR DisGeNET; 4641; -.
DR GeneCards; MYO1C; -.
DR HGNC; HGNC:7597; MYO1C.
DR HPA; ENSG00000197879; Low tissue specificity.
DR MalaCards; MYO1C; -.
DR MIM; 606538; gene.
DR neXtProt; NX_O00159; -.
DR OpenTargets; ENSG00000197879; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR PharmGKB; PA31399; -.
DR VEuPathDB; HostDB:ENSG00000197879; -.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000157915; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; O00159; -.
DR OMA; ENRDQCI; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; O00159; -.
DR TreeFam; TF312960; -.
DR PathwayCommons; O00159; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression. [O00159-3]
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; O00159; -.
DR SIGNOR; O00159; -.
DR BioGRID-ORCS; 4641; 16 hits in 1085 CRISPR screens.
DR ChiTaRS; MYO1C; human.
DR GeneWiki; MYO1C; -.
DR GenomeRNAi; 4641; -.
DR Pharos; O00159; Tbio.
DR PRO; PR:O00159; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O00159; protein.
DR Bgee; ENSG00000197879; Expressed in right lung and 208 other tissues.
DR ExpressionAtlas; O00159; baseline and differential.
DR Genevisible; O00159; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0110016; C:B-WICH complex; IDA:ComplexPortal.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016461; C:unconventional myosin complex; TAS:UniProtKB.
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:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0038089; P:positive regulation of cell migration by vascular endothelial growth factor signaling pathway; IMP:UniProtKB.
DR GO; GO:1900078; P:positive regulation of cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IC:ComplexPortal.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:UniProtKB.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; IMP:UniProtKB.
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; 3.
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 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW ATP-binding; Calmodulin-binding; Cell membrane; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; Membrane; Methylation;
KW Motor protein; mRNA transport; Myosin; Nuclear pore complex;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..1063
FT /note="Unconventional myosin-Ic"
FT /id="PRO_0000123445"
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 BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 139..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 192..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 383
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
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:15489334,
FT ECO:0000303|PubMed:9119401"
FT /id="VSP_036861"
FT VAR_SEQ 1..25
FT /note="MALQVELVPTGEIIRVVHPHRPCKL -> MRYRAS (in isoform 3)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_036862"
FT VARIANT 795
FT /note="V -> I (in dbSNP:rs8081370)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9119401,
FT ECO:0000269|Ref.3"
FT /id="VAR_054855"
FT VARIANT 826
FT /note="Q -> R (in dbSNP:rs9905106)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9119401,
FT ECO:0000269|Ref.3"
FT /id="VAR_054856"
FT MUTAGEN 736
FT /note="S->A: Abolishes interaction with YWHAB."
FT /evidence="ECO:0000269|PubMed:24636949"
FT MUTAGEN 736
FT /note="S->E: Increases affinity for YWHAB."
FT /evidence="ECO:0000269|PubMed:24636949"
FT CONFLICT 37
FT /note="E -> D (in Ref. 1; CAA67131)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="R -> K (in Ref. 1; CAA67131)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="E -> Q (in Ref. 1; CAA67131)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="K -> E (in Ref. 6; BU855623)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="E -> D (in Ref. 1; CAA67131)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="D -> N (in Ref. 1; CAA67131)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="T -> P (in Ref. 1; CAA67131)"
FT /evidence="ECO:0000305"
FT CONFLICT 832
FT /note="S -> Y (in Ref. 1; CAA67131)"
FT /evidence="ECO:0000305"
FT CONFLICT 986
FT /note="N -> I (in Ref. 1; CAA67131)"
FT /evidence="ECO:0000305"
FT CONFLICT 1062
FT /note="S -> Y (in Ref. 1; CAA67131)"
FT /evidence="ECO:0000305"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 146..160
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:4BYF"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 280..293
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 298..316
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 333..342
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 346..354
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 371..401
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 415..421
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 433..453
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 455..464
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 477..484
FT /evidence="ECO:0007829|PDB:4BYF"
FT TURN 486..488
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 490..496
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 499..503
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 506..516
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 539..546
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 549..554
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 558..562
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 568..575
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 580..585
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 600..616
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 618..626
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 639..649
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 651..660
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 663..667
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 668..675
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 676..678
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 690..701
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 707..710
FT /evidence="ECO:0007829|PDB:4BYF"
FT STRAND 712..718
FT /evidence="ECO:0007829|PDB:4BYF"
FT HELIX 720..753
FT /evidence="ECO:0007829|PDB:4BYF"
FT MOD_RES O00159-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 1063 AA; 121682 MW; B105197BA07317B8 CRC64;
MALQVELVPT 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 VLHLGNIHFA ANEESNAQVT TENQLKYLTR LLSVEGSTLR EALTHRKIIA
KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVGKINRS LASKDVESPS WRSTTVLGLL
DIYGFEVFQH NSFEQFCINY CNEKLQQLFI ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC
DLVEEKFKGI ISILDEECLR PGEATDLTFL EKLEDTVKHH PHFLTHKLAD QRTRKSLGRG
EFRLLHYAGE VTYSVTGFLD KNNDLLFRNL KETMCSSKNP IMSQCFDRSE LSDKKRPETV
ATQFKMSLLQ LVEILQSKEP AYVRCIKPND AKQPGRFDEV LIRHQVKYLG LLENLRVRRA
GFAYRRKYEA FLQRYKSLCP ETWPTWAGRP QDGVAVLVRH LGYKPEEYKM GRTKIFIRFP
KTLFATEDAL EVRRQSLATK IQAAWRGFHW RQKFLRVKRS AICIQSWWRG TLGRRKAAKR
KWAAQTIRRL IRGFVLRHAP RCPENAFFLD HVRTSFLLNL RRQLPQNVLD TSWPTPPPAL
REASELLREL CIKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR
LGTDEISPRV LQALGSEPIQ YAVPVVKYDR KGYKPRSRQL LLTPNAVVIV EDAKVKQRID
YANLTGISVS SLSDSLFVLH VQRADNKQKG DVVLQSDHVI ETLTKTALSA NRVNSININQ
GSITFAGGPG RDGTIDFTPG SELLITKAKN GHLAVVAPRL NSR
