RBCC

Full text data of MYO1C

MYO1C [Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Unconventional myosin-Ic (Myosin I beta; MMI-beta; MMIb)

UniProt O00159
ID MYO1C_HUMAN Reviewed; 1063 AA.
AC O00159; Q4LE56; Q6NVJ7; Q86Y95;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 4.
DT 22-JAN-2014, entry version 137.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS ILE-795 AND
RP 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.,
RA Weil D., Pujol R., Petit C.;
RT "Cloning of the genes encoding two murine and human cochlear
RT unconventional type I myosins.";
RL Genomics 40:332-341(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP ILE-795 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP ILE-795 AND ARG-826.
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
RA Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long
RT cDNAs 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.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA 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
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP VARIANTS 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
RT project: 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;
RP 648-656; 666-674; 715-734; 814-822; 827-841; 875-884; 886-894;
RP 901-930; 937-956 AND 988-1047, ACETYLATION AT MET-36, METHYLATION AT
RP LYS-383, AND 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
RT nuclear proteins in transcription.";
RL J. Biol. Chem. 281:16264-16271(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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
RP 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 IDENTIFICATION 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase
CC activity. Unconventional myosins serve in intracellular movements.
CC Their highly divergent tails are presumed to bind to membranous
CC compartments, which would be moved relative to actin filaments.
CC Involved in glucose transporter recycling in response to insulin
CC by regulating movement of intracellular GLUT4-containing vesicles
CC to the plasma membrane. Component of the hair cell's (the sensory
CC cells of the inner ear) adaptation-motor complex. Acts as a
CC mediator of adaptation of mechanoelectrical transduction in
CC stereocilia of vestibular hair cells. Binds phosphoinositides and
CC links the actin cytoskeleton to cellular membranes (By
CC similarity).
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
CC phosphodiester bond during transcription initiation (By
CC similarity).
CC -!- SUBUNIT: Interacts (via its IQ motifs) with calmodulin. Interacts
CC (via its IQ motifs) with CABP1 and CIB1; the interaction with
CC CABP1 and CIB1 is calcium-dependent. Interacts (via tail domain)
CC with PLEKHB1 (via PH domain); the interaction is not affected by
CC the presence or absence of calcium and calmodulin. Interacts with
CC POLR1A and POLR2A. Component of the B-WICH complex, at least
CC composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6,
CC MYBBP1A and DDX21 (By similarity). Interacts with RPS6 and actin.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus.
CC Note=Colocalizes with RNA polymerase II. Absent from nucleoli and
CC does not colocalize with RNA polymerase I. Translocates to nuclear
CC speckles upon exposure to inhibitors of RNA polymerase II
CC transcription.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Cell membrane (By
CC similarity). Cell projection, stereocilium membrane (By
CC similarity). Note=Colocalizes with CABP1 and CIB1 at cell margin,
CC membrane ruffles and punctate regions on the cell membrane.
CC Colocalizes in adipocytes with GLUT4 in actin-based membranes.
CC Localizes transiently at cell membrane to region known to be
CC enriched in PIP2. Activation of phospholipase C results in its
CC redistribution to the cytoplasm (By similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 3: Nucleus, nucleoplasm. Nucleus,
CC nucleolus. Nucleus, nuclear pore complex. Note=Colocalizes with
CC RNA polymerase II in the nucleus. Colocalizes with RNA polymerase
CC I in nucleoli (By similarity). In the nucleolus, is localized
CC predominantly in dense fibrillar component (DFC) and in granular
CC component (GC). Accumulates strongly in DFC and GC during
CC activation of transcription. Colocalizes with transcription sites.
CC Colocalizes in the granular cortex at the periphery of the
CC nucleolus with RPS6. Colocalizes in nucleoplasm with RPS6 and
CC actin that are in contact with RNP particles. Colocalizes with
CC RPS6 at the nuclear pore level.
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 Note=Contains a N-acetylmethionine at position 1;
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)
CC containing phosphatidylinositol 4,5-bisphosphate (PIP2) or
CC inositol 1,4,5-trisphosphate (InsP3). The PIP2-binding site
CC corresponds to a putative PH domain present in its tail domain (By
CC similarity).
CC -!- PTM: Isoform 2 contains a N-acetylmethionine at position 1.
CC -!- SIMILARITY: Contains 2 IQ domains.
CC -!- SIMILARITY: Contains 1 myosin head-like domain.
CC -!- CAUTION: Represents a unconventional myosin. This protein should
CC not be confused with the conventional myosin-1 (MYH1).
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH68013.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAE06097.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAF85599.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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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 PIR; A59253; A59253.
DR RefSeq; NP_001074248.1; NM_001080779.1.
DR RefSeq; NP_001074419.1; NM_001080950.1.
DR RefSeq; NP_203693.3; NM_033375.4.
DR UniGene; Hs.286226; -.
DR ProteinModelPortal; O00159; -.
DR SMR; O00159; 47-732.
DR DIP; DIP-33109N; -.
DR IntAct; O00159; 15.
DR MINT; MINT-1149702; -.
DR STRING; 9606.ENSP00000352834; -.
DR PhosphoSite; O00159; -.
DR PaxDb; O00159; -.
DR PeptideAtlas; O00159; -.
DR PRIDE; O00159; -.
DR Ensembl; ENST00000359786; ENSP00000352834; ENSG00000197879.
DR Ensembl; ENST00000361007; ENSP00000354283; ENSG00000197879.
DR Ensembl; ENST00000438665; ENSP00000412197; ENSG00000197879.
DR Ensembl; ENST00000575158; ENSP00000459174; ENSG00000197879.
DR GeneID; 4641; -.
DR KEGG; hsa:4641; -.
DR UCSC; uc002fso.3; human.
DR CTD; 4641; -.
DR GeneCards; GC17M001367; -.
DR H-InvDB; HIX0202539; -.
DR HGNC; HGNC:7597; MYO1C.
DR HPA; HPA001768; -.
DR MIM; 606538; gene.
DR neXtProt; NX_O00159; -.
DR PharmGKB; PA31399; -.
DR eggNOG; COG5022; -.
DR HOGENOM; HOG000260264; -.
DR InParanoid; O00159; -.
DR KO; K10356; -.
DR OMA; YAETCPA; -.
DR OrthoDB; EOG7V49XQ; -.
DR PhylomeDB; O00159; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; MYO1C; human.
DR GeneWiki; MYO1C; -.
DR GenomeRNAi; 4641; -.
DR NextBio; 17880; -.
DR PRO; PR:O00159; -.
DR ArrayExpress; O00159; -.
DR Bgee; O00159; -.
DR CleanEx; HS_MYO1C; -.
DR Genevestigator; O00159; -.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0045160; C:myosin I complex; IEA:Ensembl.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:motor activity; IEA:InterPro.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0038089; P:positive regulation of cell migration by vascular endothelial growth factor signaling pathway; IMP:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:UniProtKB.
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 tight junction assembly; IMP:UniProtKB.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_tail_2.
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.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; ATP-binding;
KW Calmodulin-binding; Cell membrane; Cell projection; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Membrane; Methylation;
KW Motor protein; mRNA transport; Myosin; Nuclear pore complex;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Repeat; Translocation;
KW Transport.
FT CHAIN 1 1063 Unconventional myosin-Ic.
FT /FTId=PRO_0000123445.
FT DOMAIN 36 718 Myosin head-like.
FT DOMAIN 734 757 IQ 1.
FT DOMAIN 758 786 IQ 2.
FT NP_BIND 140 147 ATP (Potential).
FT MOD_RES 383 383 N6-methyllysine.
FT MOD_RES 408 408 Phosphoserine.
FT VAR_SEQ 1 35 Missing (in isoform 2).
FT /FTId=VSP_036861.
FT VAR_SEQ 1 25 MALQVELVPTGEIIRVVHPHRPCKL -> MRYRAS (in
FT isoform 3).
FT /FTId=VSP_036862.
FT VARIANT 795 795 V -> I (in dbSNP:rs8081370).
FT /FTId=VAR_054855.
FT VARIANT 826 826 Q -> R (in dbSNP:rs9905106).
FT /FTId=VAR_054856.
FT CONFLICT 37 37 E -> D (in Ref. 1; CAA67131).
FT CONFLICT 152 152 R -> K (in Ref. 1; CAA67131).
FT CONFLICT 165 165 E -> Q (in Ref. 1; CAA67131).
FT CONFLICT 200 200 K -> E (in Ref. 6; BU855623).
FT CONFLICT 324 324 E -> D (in Ref. 1; CAA67131).
FT CONFLICT 379 379 D -> N (in Ref. 1; CAA67131).
FT CONFLICT 453 453 T -> P (in Ref. 1; CAA67131).
FT CONFLICT 832 832 S -> Y (in Ref. 1; CAA67131).
FT CONFLICT 986 986 N -> I (in Ref. 1; CAA67131).
FT CONFLICT 1062 1062 S -> Y (in Ref. 1; CAA67131).
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
//

MIM 606538
*RECORD*
*FIELD* NO
606538
*FIELD* TI
*606538 MYOSIN IC; MYO1C
;;MYOSIN 2, RAT, HOMOLOG OF; MYR2;;
NUCLEAR MYOSIN I; NMI
read more*FIELD* TX
Myosins are molecular motors that, upon interaction with actin
filaments, utilize energy from ATP hydrolysis to generate mechanical
force. For further background information on myosins, see MYO1A
(601478).

CLONING

By screening a kidney cDNA library with a mouse Myo1c probe, Crozet et
al. (1997) obtained a human cDNA encoding MYO1C. The deduced 1,028-amino
acid protein, which is 96% identical to the mouse protein, contains ATP-
and actin-binding sequences in the motor (or head) domain, followed by
three 23-residue IQ motifs and a tail domain rich in basic residues that
is expected to interact with negatively charged membrane phospholipids.
Northern blot analysis revealed ubiquitous expression of Myo1c in adult
mouse tissues.

GENE FUNCTION

MYO1C, also known as myosin I-beta and MYR2, was thought to mediate the
slow component of adaptation by hair cells, the sensory cells of the
inner ear. To test this hypothesis, Holt et al. (2002) mutated tyr61 of
MYO1C to gly, conferring susceptibility to inhibition by N6-modified ADP
analogs. They expressed the mutant MYO1C in utricular hair cells of
transgenic mice, delivered an ADP analog through a whole-cell recording
pipette, and found that the analog rapidly blocked adaptation to
positive and negative deflections in transgenic cells but not in
wildtype cells. The speed and specificity of inhibition suggested that
MYO1C participates in adaptation in hair cells.

Bose et al. (2002) reported that the unconventional myosin MYO1C is
present in GLUT4 (138190)-containing vesicles purified from 3T3-L1
adipocytes. MYO1C is highly expressed in primary and cultured
adipocytes. Insulin (176730) enhances the localization of MYO1C with
GLUT4 in cortical tubulovesicular structures associated with actin
filaments, and this colocalization is insensitive to wortmannin.
Insulin-stimulated translocation of GLUT4 to the adipocyte plasma
membrane is augmented by the expression of wildtype MYO1C and inhibited
by a dominant-negative cargo domain of MYO1C. A decrease in the
expression of endogenous MYO1C mediated by small interfering RNAs
inhibited insulin-stimulated uptake of 2-deoxyglucose. Thus, Bose et al.
(2002) concluded that MYO1C functions in a
phosphatidylinositol-3-hydroxykinase (PI3K; see 601232)-independent
insulin signaling pathway that controls the movement of intracellular
GLUT4-containing vesicles to the plasma membrane.

MAPPING

Using PCR and radiation hybrid analysis, Crozet et al. (1997) mapped the
MYO1C gene to 17p13.

HISTORY

A report by Nunez et al. (2008) indicating that 3-dimensional
motor-dependent interchromosomal interactions involving MYO1C are
required to achieve enhanced transcription of specific estrogen-receptor
target genes was retracted.

*FIELD* RF
1. Bose, A.; Guilherme, A.; Robida, S. I.; Nicoloro, S. M. C.; Zhou,
Q. L.; Jiang, Z. Y.; Pomerleau, D. P.; Czech, M. P.: Glucose transporter
recycling in response to insulin is facilitated by myosin Myo1c. Nature 420:
821-824, 2002.

2. Crozet, F.; Amraoui, A. E.; Blanchard, S.; Lenoir, M.; Ripoll,
C.; Vago, P.; Hamel, C.; Fizames, C.; Levi-Acobas, F.; Depetris, D.;
Mattei, M.-G.; Weil, D.; Pujol, R.; Petit, C.: Cloning of the genes
encoding two murine and human cochlear unconventional type I myosins. Genomics 40:
332-341, 1997.

3. Holt, J. R.; Gillespie, S. K. H.; Provance, D. W., Jr.; Shah, K.;
Shokat, K. M.; Corey, D. P.; Mercer, J. A.; Gillespie, P. G.: A chemical-genetic
strategy implicates myosin-1c in adaptation by hair cells. Cell 108:
371-381, 2002.

4. Nunez, E.; Kwon, Y.-S.; Hutt, K. R.; Hu, Q.; Cardamone, M. D.;
Ohgi, K. A.; Garcia-Bassets, I.; Rose, D. W.; Glass, C. K.; Rosenfeld,
M. G.; Fu, X.-D.: Nuclear receptor-enhanced transcription requires
motor- and LSD1-dependent gene networking in interchromatin granules. Cell 132:
996-1010, 2008. Note: Retraction: Cell 134: 189 only, 2008.

*FIELD* CN
Patricia A. Hartz - updated: 6/2/2008
Ada Hamosh - updated: 2/5/2003
Stylianos E. Antonarakis - updated: 3/25/2002

*FIELD* CD
Paul J. Converse: 12/7/2001

*FIELD* ED
carol: 01/02/2013
mgross: 6/2/2008
alopez: 2/6/2003
terry: 2/5/2003
mgross: 3/25/2002
mgross: 12/7/2001

RBCC Red Blood Cell Collection

Full text data of MYO1C