COR1C_HUMAN
ID COR1C_HUMAN Reviewed; 474 AA.
AC Q9ULV4; A7MAP0; A7MAP1; B3KU12; Q9NSK5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Coronin-1C;
DE AltName: Full=Coronin-3 {ECO:0000303|PubMed:12377779};
DE AltName: Full=hCRNN4;
GN Name=CORO1C {ECO:0000303|PubMed:10828594, ECO:0000312|HGNC:HGNC:2254};
GN Synonyms=CRN2 {ECO:0000303|PubMed:19651142}, CRNN4;
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 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10828594; DOI=10.1159/000015555;
RA Iizaka M., Han H.-J., Akashi H., Furukawa Y., Nakajima Y., Sugano S.,
RA Ogawa M., Nakamura Y.;
RT "Isolation and chromosomal assignment of a novel human gene, CORO1C,
RT homologous to coronin-like actin-binding proteins.";
RL Cytogenet. Cell Genet. 88:221-224(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION (ISOFORM 3),
RP ALTERNATIVE SPLICING, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19651142; DOI=10.1016/j.jmb.2009.07.079;
RA Xavier C.P., Rastetter R.H., Stumpf M., Rosentreter A., Muller R.,
RA Reimann J., Cornfine S., Linder S., van Vliet V., Hofmann A., Morgan R.O.,
RA Fernandez M.P., Schroder R., Noegel A.A., Clemen C.S.;
RT "Structural and functional diversity of novel coronin 1C (CRN2) isoforms in
RT muscle.";
RL J. Mol. Biol. 393:287-299(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [8]
RP SUBUNIT, COILED-COIL REGION, WD REPEATS, INTERACTION WITH F-ACTIN, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12377779; DOI=10.1074/jbc.m205136200;
RA Spoerl Z., Stumpf M., Noegel A.A., Hasse A.;
RT "Oligomerization, F-actin interaction, and membrane association of the
RT ubiquitous mammalian coronin 3 are mediated by its carboxyl terminus.";
RL J. Biol. Chem. 277:48858-48867(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-446, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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 [12]
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 [13]
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 [14]
RP ACTIN BINDING, AND SUBUNIT.
RX PubMed=22364218; DOI=10.1042/bj20120209;
RA Chan K.T., Roadcap D.W., Holoweckyj N., Bear J.E.;
RT "Coronin 1C harbours a second actin-binding site that confers co-operative
RT binding to F-actin.";
RL Biochem. J. 444:89-96(2012).
RN [15]
RP INTERACTION WITH RCC2 AND RAC1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25074804; DOI=10.1242/jcs.154864;
RA Williamson R.C., Cowell C.A., Hammond C.L., Bergen D.J., Roper J.A.,
RA Feng Y., Rendall T.C., Race P.R., Bass M.D.;
RT "Coronin-1C and RCC2 guide mesenchymal migration by trafficking Rac1 and
RT controlling GEF exposure.";
RL J. Cell Sci. 127:4292-4307(2014).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25925950; DOI=10.1074/jbc.m115.640367;
RA Williamson R.C., Cowell C.A., Reville T., Roper J.A., Rendall T.C.,
RA Bass M.D.;
RT "Coronin-1C Protein and Caveolin Protein Provide Constitutive and Inducible
RT Mechanisms of Rac1 Protein Trafficking.";
RL J. Biol. Chem. 290:15437-15449(2015).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30220460; DOI=10.1016/j.cell.2018.08.030;
RA Hoyer M.J., Chitwood P.J., Ebmeier C.C., Striepen J.F., Qi R.Z., Old W.M.,
RA Voeltz G.K.;
RT "A novel class of ER membrane proteins regulates ER-associated endosome
RT fission.";
RL Cell 175:254-265(2018).
RN [18]
RP FUNCTION, AND INTERACTION WITH MICAL2.
RX PubMed=34106209; DOI=10.1083/jcb.202102043;
RA Galloni C., Carra D., Abella J.V.G., Kjaer S., Singaravelu P., Barry D.J.,
RA Kogata N., Guerin C., Blanchoin L., Way M.;
RT "MICAL2 enhances branched actin network disassembly by oxidizing Arp3B-
RT containing Arp2/3 complexes.";
RL J. Cell Biol. 220:0-0(2021).
CC -!- FUNCTION: Plays a role in directed cell migration by regulating the
CC activation and subcellular location of RAC1 (PubMed:25074804,
CC PubMed:25925950). Increases the presence of activated RAC1 at the
CC leading edge of migrating cells (PubMed:25074804, PubMed:25925950).
CC Required for normal organization of the cytoskeleton, including the
CC actin cytoskeleton, microtubules and the vimentin intermediate
CC filaments (By similarity). Plays a role in endoplasmic reticulum-
CC associated endosome fission: localizes to endosome membrane tubules and
CC promotes recruitment of TMCC1, leading to recruitment of the
CC endoplasmic reticulum to endosome tubules for fission
CC (PubMed:30220460). Endosome membrane fission of early and late
CC endosomes is essential to separate regions destined for lysosomal
CC degradation from carriers to be recycled to the plasma membrane
CC (PubMed:30220460). Required for normal cell proliferation, cell
CC migration, and normal formation of lamellipodia (By similarity).
CC Required for normal distribution of mitochondria within cells (By
CC similarity). {ECO:0000250|UniProtKB:Q9WUM4,
CC ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:25925950,
CC ECO:0000269|PubMed:30220460, ECO:0000269|PubMed:34106209}.
CC -!- FUNCTION: [Isoform 3]: Involved in myogenic differentiation.
CC {ECO:0000269|PubMed:19651142}.
CC -!- SUBUNIT: Binds F-actin (PubMed:12377779, PubMed:22364218). Interacts
CC with RCC2 (PubMed:25074804). Interacts preferentially with nucleotide-
CC free and GDP-bound RAC1 (PubMed:25074804). Interacts with VIM (via head
CC domain) (By similarity). Isoform 1 and isoform 2 appear as homotrimers,
CC while isoform 3 seems to exist as monomers (PubMed:19651142). Interacts
CC with MICAL2; this interaction recruits MICAL2 to the actin filaments
CC (PubMed:34106209). {ECO:0000250|UniProtKB:Q9WUM4,
CC ECO:0000269|PubMed:12377779, ECO:0000269|PubMed:19651142,
CC ECO:0000269|PubMed:22364218, ECO:0000269|PubMed:25074804,
CC ECO:0000269|PubMed:34106209}.
CC -!- INTERACTION:
CC Q9ULV4; Q9BR76: CORO1B; NbExp=3; IntAct=EBI-351384, EBI-351152;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12377779,
CC ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:25074804,
CC ECO:0000269|PubMed:25925950}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:25074804,
CC ECO:0000269|PubMed:25925950}; Cytoplasmic side
CC {ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:25074804,
CC ECO:0000269|PubMed:25925950}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:12377779, ECO:0000269|PubMed:19651142}. Cell
CC projection, ruffle membrane {ECO:0000269|PubMed:25074804}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:10828594, ECO:0000269|PubMed:12377779,
CC ECO:0000269|PubMed:19651142, ECO:0000269|PubMed:25074804}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:10828594, ECO:0000269|PubMed:19651142}.
CC Endosome membrane {ECO:0000269|PubMed:30220460}. Note=All isoforms
CC colocalize with the actin cytoskeleton in the cytosol, and especially
CC in the cell cortex (PubMed:10828594, PubMed:19651142, PubMed:25074804).
CC Colocalizes with F-actin at the leading edge of lamellipodia. Partially
CC colocalizes with microtubules and vimentin intermediate filaments
CC (PubMed:10828594, PubMed:19651142, PubMed:25074804). Localizes to
CC endosome membrane tubules/buds (PubMed:30220460).
CC {ECO:0000269|PubMed:10828594, ECO:0000269|PubMed:19651142,
CC ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:30220460}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:19651142}. Cytoplasm, myofibril, sarcomere
CC {ECO:0000269|PubMed:19651142}. Synapse {ECO:0000269|PubMed:19651142}.
CC Cell membrane {ECO:0000269|PubMed:19651142}; Peripheral membrane
CC protein {ECO:0000269|PubMed:19651142}; Cytoplasmic side
CC {ECO:0000269|PubMed:19651142}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19651142}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:19651142}. Note=Colocalizes with the thin filaments
CC of the sarcomere and with the postsynaptic area and the junctional
CC sarcoplasm of motor end plates. Colocalizes with the actin cytoskeleton
CC in the cytosol, and especially in the cell cortex.
CC {ECO:0000269|PubMed:19651142}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9ULV4-1; Sequence=Displayed;
CC Name=2; Synonyms=CRN2i2;
CC IsoId=Q9ULV4-2; Sequence=VSP_047727;
CC Name=3; Synonyms=CRN2i3;
CC IsoId=Q9ULV4-3; Sequence=VSP_047728;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10828594}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is essential for cortical
CC membrane localization and oligomerization.
CC -!- MISCELLANEOUS: [Isoform 3]: Exclusively expressed in well-
CC differentiated myoblasts as well as in mature skeletal muscle.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB82406.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB030656; BAA83077.1; -; mRNA.
DR EMBL; AM849477; CAO94662.1; -; mRNA.
DR EMBL; AM849478; CAO94663.1; -; mRNA.
DR EMBL; AK096363; BAG53274.1; -; mRNA.
DR EMBL; AL162070; CAB82406.1; ALT_INIT; mRNA.
DR EMBL; AC007569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97826.1; -; Genomic_DNA.
DR EMBL; BC002342; AAH02342.1; -; mRNA.
DR CCDS; CCDS61236.1; -. [Q9ULV4-3]
DR CCDS; CCDS9120.1; -. [Q9ULV4-1]
DR RefSeq; NP_001098707.1; NM_001105237.2. [Q9ULV4-3]
DR RefSeq; NP_001263400.1; NM_001276471.1. [Q9ULV4-1]
DR RefSeq; NP_055140.1; NM_014325.3. [Q9ULV4-1]
DR RefSeq; XP_016874610.1; XM_017019121.1. [Q9ULV4-3]
DR RefSeq; XP_016874611.1; XM_017019122.1. [Q9ULV4-1]
DR RefSeq; XP_016874612.1; XM_017019123.1. [Q9ULV4-1]
DR PDB; 7STY; X-ray; 2.00 A; A=1-474.
DR PDBsum; 7STY; -.
DR AlphaFoldDB; Q9ULV4; -.
DR SMR; Q9ULV4; -.
DR BioGRID; 117136; 288.
DR DIP; DIP-33138N; -.
DR IntAct; Q9ULV4; 91.
DR MINT; Q9ULV4; -.
DR STRING; 9606.ENSP00000394496; -.
DR GlyConnect; 1157; 1 N-Linked glycan (1 site).
DR GlyGen; Q9ULV4; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q9ULV4; -.
DR MetOSite; Q9ULV4; -.
DR PhosphoSitePlus; Q9ULV4; -.
DR SwissPalm; Q9ULV4; -.
DR BioMuta; CORO1C; -.
DR DMDM; 12643898; -.
DR OGP; Q9ULV4; -.
DR CPTAC; CPTAC-49; -.
DR CPTAC; CPTAC-50; -.
DR EPD; Q9ULV4; -.
DR jPOST; Q9ULV4; -.
DR MassIVE; Q9ULV4; -.
DR MaxQB; Q9ULV4; -.
DR PaxDb; Q9ULV4; -.
DR PeptideAtlas; Q9ULV4; -.
DR PRIDE; Q9ULV4; -.
DR ProteomicsDB; 1808; -.
DR ProteomicsDB; 85134; -. [Q9ULV4-1]
DR Antibodypedia; 30774; 295 antibodies from 33 providers.
DR DNASU; 23603; -.
DR Ensembl; ENST00000261401.8; ENSP00000261401.3; ENSG00000110880.11. [Q9ULV4-1]
DR Ensembl; ENST00000420959.6; ENSP00000394496.2; ENSG00000110880.11. [Q9ULV4-3]
DR Ensembl; ENST00000541050.5; ENSP00000438341.1; ENSG00000110880.11. [Q9ULV4-1]
DR Ensembl; ENST00000549772.5; ENSP00000447534.1; ENSG00000110880.11. [Q9ULV4-2]
DR GeneID; 23603; -.
DR KEGG; hsa:23603; -.
DR MANE-Select; ENST00000261401.8; ENSP00000261401.3; NM_014325.4; NP_055140.1.
DR UCSC; uc001tnj.6; human. [Q9ULV4-1]
DR CTD; 23603; -.
DR DisGeNET; 23603; -.
DR GeneCards; CORO1C; -.
DR HGNC; HGNC:2254; CORO1C.
DR HPA; ENSG00000110880; Low tissue specificity.
DR MIM; 605269; gene.
DR neXtProt; NX_Q9ULV4; -.
DR OpenTargets; ENSG00000110880; -.
DR PharmGKB; PA26770; -.
DR VEuPathDB; HostDB:ENSG00000110880; -.
DR eggNOG; KOG0303; Eukaryota.
DR GeneTree; ENSGT00940000156488; -.
DR HOGENOM; CLU_026859_0_1_1; -.
DR InParanoid; Q9ULV4; -.
DR OrthoDB; 552726at2759; -.
DR PhylomeDB; Q9ULV4; -.
DR TreeFam; TF314280; -.
DR PathwayCommons; Q9ULV4; -.
DR SignaLink; Q9ULV4; -.
DR SIGNOR; Q9ULV4; -.
DR BioGRID-ORCS; 23603; 21 hits in 1078 CRISPR screens.
DR ChiTaRS; CORO1C; human.
DR GeneWiki; CORO1C; -.
DR GenomeRNAi; 23603; -.
DR Pharos; Q9ULV4; Tbio.
DR PRO; PR:Q9ULV4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9ULV4; protein.
DR Bgee; ENSG00000110880; Expressed in saphenous vein and 208 other tissues.
DR ExpressionAtlas; Q9ULV4; baseline and differential.
DR Genevisible; Q9ULV4; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0016600; C:flotillin complex; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IDA:UniProtKB.
DR GO; GO:0140285; P:endosome fission; IDA:UniProtKB.
DR GO; GO:0097750; P:endosome membrane tubulation; IDA:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; ISS:UniProtKB.
DR GO; GO:0090148; P:membrane fission; IDA:UniProtKB.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; TAS:ProtInc.
DR GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; IMP:UniProtKB.
DR GO; GO:0010632; P:regulation of epithelial cell migration; IGI:UniProtKB.
DR GO; GO:0010762; P:regulation of fibroblast migration; ISS:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IGI:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IGI:UniProtKB.
DR GO; GO:1900027; P:regulation of ruffle assembly; IEA:Ensembl.
DR GO; GO:1900024; P:regulation of substrate adhesion-dependent cell spreading; IGI:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR027333; CORO1C.
DR InterPro; IPR015505; Coronin.
DR InterPro; IPR015048; DUF1899.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10856; PTHR10856; 1.
DR PANTHER; PTHR10856:SF10; PTHR10856:SF10; 1.
DR Pfam; PF08953; DUF1899; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM01166; DUF1899; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endosome; Membrane; Reference proteome; Repeat; Synapse; WD repeat.
FT CHAIN 1..474
FT /note="Coronin-1C"
FT /id="PRO_0000050926"
FT REPEAT 25..70
FT /note="WD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT REPEAT 78..118
FT /note="WD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12377779"
FT REPEAT 128..168
FT /note="WD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12377779"
FT REPEAT 172..202
FT /note="WD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12377779"
FT REPEAT 215..249
FT /note="WD 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12377779"
FT REPEAT 263..303
FT /note="WD 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00221,
FT ECO:0000269|PubMed:12377779"
FT COILED 436..474
FT /evidence="ECO:0000269|PubMed:12377779"
FT MOD_RES 446
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1
FT /note="M -> MRWKDTM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19651142"
FT /id="VSP_047727"
FT VAR_SEQ 1
FT /note="M -> MYGPGSQLGKSGNNSWAKERGCSIACQGSLTSARLHAPSIGERPLSH
FT MRWKDTM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19651142"
FT /id="VSP_047728"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:7STY"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:7STY"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:7STY"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:7STY"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 301..308
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:7STY"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:7STY"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 340..349
FT /evidence="ECO:0007829|PDB:7STY"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:7STY"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:7STY"
FT HELIX 374..378
FT /evidence="ECO:0007829|PDB:7STY"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:7STY"
SQ SEQUENCE 474 AA; 53249 MW; C7256797C514BB53 CRC64;
MRRVVRQSKF RHVFGQAVKN DQCYDDIRVS RVTWDSSFCA VNPRFVAIII EASGGGAFLV
LPLHKTGRID KSYPTVCGHT GPVLDIDWCP HNDQVIASGS EDCTVMVWQI PENGLTLSLT
EPVVILEGHS KRVGIVAWHP TARNVLLSAG CDNAIIIWNV GTGEALINLD DMHSDMIYNV
SWNRNGSLIC TASKDKKVRV IDPRKQEIVA EKEKAHEGAR PMRAIFLADG NVFTTGFSRM
SERQLALWNP KNMQEPIALH EMDTSNGVLL PFYDPDTSII YLCGKGDSSI RYFEITDESP
YVHYLNTFSS KEPQRGMGYM PKRGLDVNKC EIARFFKLHE RKCEPIIMTV PRKSDLFQDD
LYPDTAGPEA ALEAEEWFEG KNADPILISL KHGYIPGKNR DLKVVKKNIL DSKPTANKKC
DLISIPKKTT DTASVQNEAK LDEILKEIKS IKDTICNQDE RISKLEQQMA KIAA
