CEP43_MOUSE
ID CEP43_MOUSE Reviewed; 399 AA.
AC Q66JX5; Q32P17; Q8BH91;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Centrosomal protein 43 {ECO:0000305};
DE AltName: Full=FGFR1 oncogene partner;
GN Name=Cep43 {ECO:0000312|MGI:MGI:1922546};
GN Synonyms=Fgfr1op {ECO:0000312|MGI:MGI:1922546};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Forelimb, Liver, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-20.
RC STRAIN=C57BL/6J, and NMRI; TISSUE=Embryo, and Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-337, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for anchoring microtubules to the centrosomes.
CC Required for ciliation. {ECO:0000250|UniProtKB:O95684}.
CC -!- SUBUNIT: Homodimer. Part of a ternary complex that contains CEP350,
CC CEP43 and MAPRE1. Interacts directly with CEP350 and MAPRE1. Interacts
CC with CEP19. Interacts (via N-terminus) with CEP350 (via C-terminus).
CC {ECO:0000250|UniProtKB:O95684}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:O95684}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:O95684}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:O95684}. Note=Associated with gamma-
CC tubulin. Localizes on both mother and daughter centrioles. Localizes to
CC an axial position on the mother centriole. Localizes to the distal end
CC of the centriole partly to the subdistal appendage region.
CC {ECO:0000250|UniProtKB:O95684}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q66JX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q66JX5-2; Sequence=VSP_018122;
CC -!- SIMILARITY: Belongs to the CEP43 family. {ECO:0000305}.
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DR EMBL; AK028778; BAC26115.1; -; mRNA.
DR EMBL; AK031261; BAC27326.1; -; mRNA.
DR EMBL; AK050389; BAC34230.1; -; mRNA.
DR EMBL; BC080717; AAH80717.1; -; mRNA.
DR EMBL; BC108331; AAI08332.1; -; mRNA.
DR CCDS; CCDS28380.1; -. [Q66JX5-2]
DR CCDS; CCDS57045.1; -. [Q66JX5-1]
DR RefSeq; NP_001183975.1; NM_001197046.1. [Q66JX5-1]
DR RefSeq; NP_957682.1; NM_201230.5. [Q66JX5-2]
DR AlphaFoldDB; Q66JX5; -.
DR SMR; Q66JX5; -.
DR BioGRID; 217370; 49.
DR IntAct; Q66JX5; 50.
DR STRING; 10090.ENSMUSP00000024636; -.
DR iPTMnet; Q66JX5; -.
DR PhosphoSitePlus; Q66JX5; -.
DR EPD; Q66JX5; -.
DR jPOST; Q66JX5; -.
DR MaxQB; Q66JX5; -.
DR PaxDb; Q66JX5; -.
DR PeptideAtlas; Q66JX5; -.
DR PRIDE; Q66JX5; -.
DR ProteomicsDB; 271604; -. [Q66JX5-1]
DR ProteomicsDB; 271605; -. [Q66JX5-2]
DR Antibodypedia; 33532; 296 antibodies from 32 providers.
DR Ensembl; ENSMUST00000024636; ENSMUSP00000024636; ENSMUSG00000069135. [Q66JX5-2]
DR Ensembl; ENSMUST00000097419; ENSMUSP00000095030; ENSMUSG00000069135. [Q66JX5-1]
DR GeneID; 75296; -.
DR KEGG; mmu:75296; -.
DR UCSC; uc008ajb.2; mouse. [Q66JX5-2]
DR UCSC; uc008ajc.2; mouse. [Q66JX5-1]
DR CTD; 11116; -.
DR MGI; MGI:1922546; Cep43.
DR VEuPathDB; HostDB:ENSMUSG00000069135; -.
DR eggNOG; ENOG502QR70; Eukaryota.
DR GeneTree; ENSGT00390000007441; -.
DR HOGENOM; CLU_039837_2_0_1; -.
DR InParanoid; Q66JX5; -.
DR OMA; DITQDHT; -.
DR OrthoDB; 1316797at2759; -.
DR PhylomeDB; Q66JX5; -.
DR TreeFam; TF331893; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 75296; 13 hits in 74 CRISPR screens.
DR ChiTaRS; Fgfr1op; mouse.
DR PRO; PR:Q66JX5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q66JX5; protein.
DR Bgee; ENSMUSG00000069135; Expressed in ear vesicle and 224 other tissues.
DR ExpressionAtlas; Q66JX5; baseline and differential.
DR Genevisible; Q66JX5; MM.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030292; F:protein tyrosine kinase inhibitor activity; ISO:MGI.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0034453; P:microtubule anchoring; IEA:InterPro.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR InterPro; IPR018993; FOP_dimerisation-dom_N.
DR InterPro; IPR006594; LisH.
DR Pfam; PF09398; FOP_dimer; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..399
FT /note="Centrosomal protein 43"
FT /id="PRO_0000233295"
FT DOMAIN 70..102
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REGION 142..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95684"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95684"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95684"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95684"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95684"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95684"
FT MOD_RES 337
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT VAR_SEQ 174..193
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018122"
FT VARIANT 20
FT /note="L -> R (in strain: C57BL/6J)"
FT /evidence="ECO:0000269|PubMed:15489334"
SQ SEQUENCE 399 AA; 42758 MW; 9E3219BD4CC729C3 CRC64;
MAATTAAVVA EEDTELRDLL VQTLENSGVL NRIKAELRAA VFLALEEQEK VENKTPLVNE
NLKKFLNTKD GRLVASLVAE FLQFFNLDFT LAVFHPETST IQGLEGRENL AQDLGIIEAE
GTVGGPLLLE VIRRCQQKEK GPASVEGALD LSDGHPPSKS PEGKSSANST PSKIPRYKGQ
GKKKTIGQKP GDKKTSSETS QSEPSVSLSE SKSKSSLHSL AHETRIASFL SSSAVDARDS
SALCPDGDDV EGDSFFDDPI PKPEKTYGWR AEPRKQVGGL ASLSDKPHLR SGLSSLAGAP
SLTDPESKRG STVLKDLKLV GEKIGSLGLG TGEDEDYADD FNSASHRSEK SELSIGEEIE
EDLSMGVEDG NTSDKLDDLT QDLTVSQLSD VADYLEDVA
