CEP43_RAT
ID CEP43_RAT Reviewed; 399 AA.
AC Q4V7C1;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Centrosomal protein 43 {ECO:0000305};
DE AltName: Full=FGFR1 oncogene partner;
GN Name=Cep43; Synonyms=Fgfr1op;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SIMILARITY: Belongs to the CEP43 family. {ECO:0000305}.
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DR EMBL; BC098026; AAH98026.1; -; mRNA.
DR RefSeq; NP_001094478.1; NM_001101008.1.
DR AlphaFoldDB; Q4V7C1; -.
DR SMR; Q4V7C1; -.
DR STRING; 10116.ENSRNOP00000017590; -.
DR iPTMnet; Q4V7C1; -.
DR PhosphoSitePlus; Q4V7C1; -.
DR jPOST; Q4V7C1; -.
DR PRIDE; Q4V7C1; -.
DR GeneID; 683722; -.
DR KEGG; rno:683722; -.
DR CTD; 11116; -.
DR RGD; 1583370; Fgfr1op.
DR VEuPathDB; HostDB:ENSRNOG00000055093; -.
DR eggNOG; ENOG502QR70; Eukaryota.
DR HOGENOM; CLU_039837_2_0_1; -.
DR InParanoid; Q4V7C1; -.
DR OMA; DITQDHT; -.
DR OrthoDB; 1316797at2759; -.
DR PhylomeDB; Q4V7C1; -.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR PRO; PR:Q4V7C1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000055093; Expressed in thymus and 20 other tissues.
DR Genevisible; Q4V7C1; RN.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005814; C:centriole; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0030292; F:protein tyrosine kinase inhibitor activity; ISO:RGD.
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:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
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 Cell projection; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..399
FT /note="Centrosomal protein 43"
FT /id="PRO_0000233296"
FT DOMAIN 70..102
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REGION 139..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..357
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..217
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 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95684"
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 234
FT /note="Phosphothreonine"
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 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 337
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q66JX5"
SQ SEQUENCE 399 AA; 43012 MW; F0A49604CABF15B5 CRC64;
MAATTAAVVA EEDTELRDLL VQTLENSGVL NRIKAELRAA VFLALEEQEK VENKTPLVNE
SLKKFLNTKD GRLVASLVAE FLQFFNLDFT LAVFHPETST IQGLEGRENL ARDLGIIEAE
GTVGGPLLLE VIRRCQQKEK GPTSVEGALD LSDGHPPSKS PEGKTSVNST PSKIPRYKGQ
GKKKTSGQKS GDKKTSSETS QSEPSVSLSE SKSKSSLHSL VHETRIASFL SNSTVDAKDK
SALCPDEDDV EGDSFFDDPI PKPEKTYGWR SEPRKQVGGL ASLSDKPHLR SGLSSLAGAP
SLTDAESKRG STVLKDLKLV GEKIGSLGLG SGEDEDYVDD FNSASHRSEK SELSIGEEIE
EDLSMGVEDV NTSDKLDDLT QDLTVSQLSD VADYLEDVA
