ID   CEP43_MACFA             Reviewed;         379 AA.
AC   Q4R7V3;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Centrosomal protein 43 {ECO:0000305};
DE   AltName: Full=FGFR1 oncogene partner;
GN   Name=CEP43; Synonyms=FGFR1OP; ORFNames=QtsA-14293;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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; AB168708; BAE00819.1; -; mRNA.
DR   RefSeq; NP_001270441.1; NM_001283512.1.
DR   AlphaFoldDB; Q4R7V3; -.
DR   SMR; Q4R7V3; -.
DR   STRING; 9541.XP_005551501.1; -.
DR   GeneID; 101865789; -.
DR   CTD; 11116; -.
DR   eggNOG; ENOG502QR70; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0034453; P:microtubule anchoring; IEA:InterPro.
DR   InterPro; IPR018993; FOP_dimerisation-dom_N.
DR   InterPro; IPR006594; LisH.
DR   Pfam; PF09398; FOP_dimer; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..379
FT                   /note="Centrosomal protein 43"
FT                   /id="PRO_0000233294"
FT   DOMAIN          70..102
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   REGION          139..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..251
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         182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95684"
FT   MOD_RES         214
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O95684"
FT   MOD_RES         281
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95684"
FT   MOD_RES         306
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95684"
FT   MOD_RES         317
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q66JX5"
SQ   SEQUENCE   379 AA;  40815 MW;  97074CC1D19A07B6 CRC64;
     MAATAAAVVA EEDTELRDLL VQTLENSGVL NRIKAELRAA VFLALEEQEK VENKTPLVNE
     SLKKFLNTKD GRLVASLVAE FLQFFNLDFT LAVFQPETST LQGLEGRENL ARDLGIIEAE
     GTVGGPLLLE VIRRCQQKEK GPTTGEGALD LSDVHPPPKS PEGKTSAQTT PSKKANNEAN
     QSDTSVSLSE PKSKSSLHLL SHETKIGSFL SNKTLDGKDK AGLCPDEDDM EGDSFFDDPI
     PKPEKTYGLR SEPRKQPGSL ASLSDAPPLK SGLSSLAGAP SLKDSESKRG NTVLKDLKLI
     SGKIGSLGLG TGEDDDYVDD FNSTSHRSEK SEISIGEEIE EDLSVEIDDI NTSDKLDDLT
     QDLTVSQLSD VADYLEDVA