ID   CEP83_RAT               Reviewed;         692 AA.
AC   Q66H89;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Centrosomal protein of 83 kDa;
DE            Short=Cep83;
DE   AltName: Full=Coiled-coil domain-containing protein 41;
GN   Name=Cep83; Synonyms=Ccdc41;
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=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).
CC   -!- FUNCTION: Component of the distal appendage region of the centriole
CC       involved in the initiation of primary cilium assembly. May collaborate
CC       with IFT20 in the trafficking of ciliary membrane proteins from the
CC       Golgi complex to the cilium during the initiation of primary cilium
CC       assembly (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CEP164 and IFT20. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriole {ECO:0000250}. Note=Localizes
CC       specifically to the distal appendage region of the centriole, which
CC       anchors the mother centriole to the plasma membrane. Localizes to
CC       centrioles at all stages of the cell cycle, including mitosis (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CEP83 family. {ECO:0000305}.
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DR   EMBL; BC081969; AAH81969.1; -; mRNA.
DR   RefSeq; NP_001014288.1; NM_001014266.2.
DR   RefSeq; XP_017450505.1; XM_017595016.1.
DR   AlphaFoldDB; Q66H89; -.
DR   SMR; Q66H89; -.
DR   STRING; 10116.ENSRNOP00000031786; -.
DR   CarbonylDB; Q66H89; -.
DR   PhosphoSitePlus; Q66H89; -.
DR   PaxDb; Q66H89; -.
DR   PRIDE; Q66H89; -.
DR   Ensembl; ENSRNOT00000034639; ENSRNOP00000031786; ENSRNOG00000007859.
DR   GeneID; 366872; -.
DR   KEGG; rno:366872; -.
DR   CTD; 51134; -.
DR   RGD; 1359593; Cep83.
DR   eggNOG; ENOG502QWE2; Eukaryota.
DR   GeneTree; ENSGT00940000154003; -.
DR   HOGENOM; CLU_020145_1_0_1; -.
DR   InParanoid; Q66H89; -.
DR   OMA; KHQTENR; -.
DR   OrthoDB; 1094723at2759; -.
DR   PhylomeDB; Q66H89; -.
DR   TreeFam; TF329199; -.
DR   Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR   PRO; PR:Q66H89; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000007859; Expressed in heart and 19 other tissues.
DR   Genevisible; Q66H89; RN.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0097539; C:ciliary transition fiber; ISO:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0051660; P:establishment of centrosome localization; ISO:RGD.
DR   GO; GO:0071539; P:protein localization to centrosome; ISO:RGD.
DR   GO; GO:0048278; P:vesicle docking; ISO:RGD.
DR   InterPro; IPR029631; Cep83.
DR   PANTHER; PTHR23170:SF2; PTHR23170:SF2; 1.
PE   2: Evidence at transcript level;
KW   Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..692
FT                   /note="Centrosomal protein of 83 kDa"
FT                   /id="PRO_0000234497"
FT   COILED          32..625
FT                   /evidence="ECO:0000255"
FT   COILED          656..689
FT                   /evidence="ECO:0000255"
FT   MOD_RES         689
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D5R3"
SQ   SEQUENCE   692 AA;  81909 MW;  6E890C69E024F419 CRC64;
     MDTFPSIFPP GGDSRLNPEP EFQSMLIDER VRCEHHKHNY QALKIEHKRL QEEYVKSQNE
     LKRVLNEKQT NQEKFQLLLE ELRGELVEKV KDMEAMKLQI LTPQKLELVK AQLQQELEAP
     MRERFRTLDE EVERYRAEYN KLRYEHTFLK SEFEHQKEEL TRISEEEKMK YKSEVARLEK
     DKEELHNQLL SVDPTRDSKR VEQLVREKTH LLQKLKSLEA EVAELRAEKE NSGAQVENVQ
     RIQVRQLAEM QATLRSLEAE KQSAKLQAER LEKELQSSNE QNTCLISKLH KADREISTLT
     SQVKELKHAN KLEITDVKLE AARAKSELER ERNKIQSELD GLQSDNEILK STVEHHKVLL
     VEKDRELIRK VQAAKEEGYQ KLVVLQDEKL ELENRLSDLE KMKVEHDVWR QSEKDQCEEK
     LRASQAAEEA ARRELQSIRL KLQQQIVNTE KAEKEKLENS ELKQQISHLQ IQVTSLTQSE
     NDLLNSNQML KDMVERLKQE CRHLRSQAEK VQLEVEKTLE EKQIQWLEEK HKLHERITDR
     EEKYNQAKEK LQRAATAQKK RKSLHENKLK RLQEKVEVLE AKKEELETEN QVLNRQNVPF
     EEYTRLQKRL KDIQRRHNEF RSLILVPNMP PAASVNPANF QSSAIVPGVE LSFPPHLQEE
     QHQRELSLLR KRLEELETTQ RKQLEELGSP GE