ID   CEP43_BOVIN             Reviewed;         399 AA.
AC   Q2YDD1;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Centrosomal protein 43 {ECO:0000305};
DE   AltName: Full=FGFR1 oncogene partner;
GN   Name=CEP43; Synonyms=FGFR1OP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-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; BC110279; AAI10280.1; -; mRNA.
DR   RefSeq; NP_001071327.1; NM_001077859.1.
DR   AlphaFoldDB; Q2YDD1; -.
DR   SMR; Q2YDD1; -.
DR   STRING; 9913.ENSBTAP00000019271; -.
DR   PaxDb; Q2YDD1; -.
DR   PRIDE; Q2YDD1; -.
DR   GeneID; 506246; -.
DR   KEGG; bta:506246; -.
DR   CTD; 11116; -.
DR   eggNOG; ENOG502QR70; Eukaryota.
DR   InParanoid; Q2YDD1; -.
DR   OrthoDB; 1316797at2759; -.
DR   Proteomes; UP000009136; 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..399
FT                   /note="Centrosomal protein 43"
FT                   /id="PRO_0000233292"
FT   DOMAIN          70..102
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   REGION          143..311
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        179..214
FT                   /note="Polar 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         156
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         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:0000250|UniProtKB:Q66JX5"
SQ   SEQUENCE   399 AA;  42764 MW;  C79E57AAEC340ADB CRC64;
     MAATAAAVVA EEDTELRYLL VQTLENSGVL NRIKAELRAA VFLALEEQEK VENKTPLVNE
     SLKKFLNTKD GRLVASLVAE FLQFFNLDFT LAVFQPETST FQGLEGRENL ARDLGIIEAE
     GTVGGPLLLE VIRRCQQKEK ALTSGEGALD LSDVHSPPKS PEGKTGAHTP PSKIPRYKGQ
     GNKKTSGQQP GAKKASNDAS HSDTSISSSE PKSRSGLHLL AHETKIGSLL SNNSLDVNAK
     AGPGPEEDDL EGDSFFDDPI PKPEAAYGWR SEPSKQAGSL ASLSDAPPLK SGLSSLAGAP
     SLKESESKRG NTVLKDLKLV NDKIGSLGLG TGEEDDYVDD FNSTSHRSEK SELSIGEEIE
     EDLSVEMDDV NTSDKLDDLT QDLTVSQLSD VADYLEDVA