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 27-MAR-2024, entry version 224. 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 (ISOFORM 3). 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 (ISOFORM 3). 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 INTERACTION WITH SH3BGRL3, AND SUBCELLULAR LOCATION. RX PubMed=34380438; DOI=10.1186/s12860-021-00379-1; RA Di Pisa F., Pesenti E., Bono M., Mazzarello A.N., Bernardi C., RA Lisanti M.P., Renzone G., Scaloni A., Ciccone E., Fais F., Bruno S., RA Scartezzini P., Ghiotto F.; RT "SH3BGRL3 binds to myosin 1c in a calcium dependent manner and modulates RT migration in the MDA-MB-231 cell line."; RL BMC Mol. Cell Biol. 22:41-41(2021). RN [20] 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]: 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. {ECO:0000250|UniProtKB:Q9WTI7}. CC -!- SUBUNIT: Interacts (via its IQ motifs) with CABP1 and CIB1; the CC interaction with CABP1 and CIB1 is calcium-dependent (By similarity). CC Interacts (via tail domain) with PLEKHB1 (via PH domain); the CC interaction is not affected by the presence or absence of calcium and CC CALM (By similarity). Interacts with POLR1A (By similarity). Interacts CC with POLR2A (By similarity). Component of the B-WICH complex, at least CC composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, CC MYBBP1A and DDX21 (PubMed:16603771). Interacts (via its IQ motifs) with CC CALM; this precludes interaction with YWHAB (PubMed:24636949). CC Interacts with YWHAB; this precludes interaction with CALM CC (PubMed:24636949). Interacts with RPS6 (PubMed:16877530). Interacts CC with actin (PubMed:16877530). Interacts with LLPH (By similarity). CC Interacts with GLUT4 (By similarity). Interacts (via its IQ motifs) CC with SH3BGRL3; the interaction is dependent on calcium and takes place CC at membrane ruffles (PubMed:34380438). {ECO:0000250|UniProtKB:Q63355, CC ECO:0000250|UniProtKB:Q9WTI7, ECO:0000269|PubMed:16603771, CC ECO:0000269|PubMed:16877530, ECO:0000269|PubMed:24636949, CC ECO:0000269|PubMed:34380438}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22736583}. Nucleus CC {ECO:0000269|PubMed:22736583}. Cytoplasm, cell cortex CC {ECO:0000250|UniProtKB:Q9WTI7}. Cell projection, stereocilium membrane CC {ECO:0000250|UniProtKB:Q92002}. Cytoplasmic vesicle CC {ECO:0000250|UniProtKB:Q9WTI7}. Cell projection, ruffle membrane CC {ECO:0000269|PubMed:34380438}. Note=Colocalizes with CABP1 and CIB1 at CC cell margin, membrane ruffles and punctate regions on the cell membrane CC (By similarity). Colocalizes in adipocytes with GLUT4 at actin-based CC membranes (By similarity). Colocalizes with GLUT4 at insulin-induced CC ruffles at the cell membrane (By similarity). Localizes transiently at CC cell membrane to region known to be enriched in PIP2 (By similarity). CC Activation of phospholipase C results in its redistribution to the CC cytoplasm (By similarity). Colocalizes with RNA polymerase II CC (PubMed:22736583). Translocates to nuclear speckles upon exposure to CC inhibitors of RNA polymerase II transcription (PubMed:22736583). CC {ECO:0000250|UniProtKB:Q9WTI7, ECO:0000269|PubMed:22736583}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleoplasm CC {ECO:0000269|PubMed:16133118}. Nucleus, nucleolus CC {ECO:0000269|PubMed:16133118, ECO:0000269|PubMed:16877530}. CC Note=Colocalizes with RNA polymerase II in the nucleus (By similarity). CC Colocalizes with RNA polymerase I in nucleoli (By similarity). In the CC nucleolus, is localized predominantly in dense fibrillar component CC (DFC) and in granular component (GC) (PubMed:16133118, CC PubMed:16877530). Accumulates strongly in DFC and GC during activation CC of transcription (PubMed:16133118). Colocalizes with transcription CC sites (By similarity). Colocalizes in the granular cortex at the CC periphery of the nucleolus with RPS6 (PubMed:16877530). Colocalizes in CC nucleoplasm with RPS6 and actin that are in contact with RNP particles CC (PubMed:16877530). Colocalizes with RPS6 at the nuclear pore level CC (PubMed:16877530). {ECO:0000250|UniProtKB:Q9WTI7, CC ECO:0000269|PubMed:16133118, ECO:0000269|PubMed:16877530}. 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|UniProtKB:Q9WTI7}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 408. DR ComplexPortal; CPX-1099; B-WICH chromatin remodelling complex. [O00159-3] DR CORUM; O00159; -. DR DIP; DIP-33109N; -. DR IntAct; O00159; 221. DR MINT; O00159; -. DR STRING; 9606.ENSP00000496954; -. 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; 9606-ENSP00000352834; -. DR PeptideAtlas; O00159; -. DR ProteomicsDB; 47744; -. [O00159-1] DR ProteomicsDB; 47745; -. [O00159-2] DR ProteomicsDB; 47746; -. [O00159-3] DR Pumba; O00159; -. DR Antibodypedia; 953; 200 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 AGR; HGNC:7597; -. 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; Rare 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; FICRGNC; -. DR OrthoDB; 1094820at2759; -. 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; 17 hits in 1164 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 210 other cell types or tissues. DR ExpressionAtlas; O00159; baseline and differential. 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:0005938; C:cell cortex; IEA:UniProtKB-SubCell. 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:0005730; C:nucleolus; NAS: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:HPA. DR GO; GO:0032587; C:ruffle membrane; 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:0031982; C:vesicle; 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: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 type II interferon; IEA:Ensembl. DR GO; GO:0006338; P:chromatin remodeling; NAS:ComplexPortal. 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; NAS: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; NAS:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; NAS: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; 1.10.10.820; -; 1. DR Gene3D; 1.20.5.190; -; 1. DR Gene3D; 1.20.58.530; -; 1. DR Gene3D; 6.20.240.20; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 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 PANTHER; PTHR13140; MYOSIN; 1. DR PANTHER; PTHR13140:SF255; UNCONVENTIONAL MYOSIN-IC; 1. 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; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50096; IQ; 2. DR PROSITE; PS51456; MYOSIN_MOTOR; 1. DR PROSITE; PS51757; TH1; 1. DR Genevisible; O00159; HS. 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; Myosin; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat. 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 //