ID   CEP89_DANRE             Reviewed;         695 AA.
AC   Q6P402;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Centrosomal protein of 89 kDa;
DE            Short=Cep89;
DE   AltName: Full=Coiled-coil domain-containing protein 123;
GN   Name=cep89; Synonyms=ccdc123; ORFNames=zgc:63648;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=SJD;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for ciliogenesis. Also plays a role in mitochondrial
CC       metabolism where it may modulate complex IV activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC       Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome, centriole
CC       {ECO:0000250}. Mitochondrion intermembrane space {ECO:0000250}.
CC       Note=Localizes to the distal appendage region of the centriole, which
CC       anchors the mother centriole to the plasma membrane. {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC063747; AAH63747.1; -; mRNA.
DR   RefSeq; NP_957172.1; NM_200878.1.
DR   AlphaFoldDB; Q6P402; -.
DR   SMR; Q6P402; -.
DR   STRING; 7955.ENSDARP00000121321; -.
DR   PaxDb; Q6P402; -.
DR   PRIDE; Q6P402; -.
DR   GeneID; 393852; -.
DR   KEGG; dre:393852; -.
DR   CTD; 84902; -.
DR   ZFIN; ZDB-GENE-040426-1210; cep89.
DR   eggNOG; ENOG502QWK8; Eukaryota.
DR   InParanoid; Q6P402; -.
DR   OrthoDB; 476357at2759; -.
DR   PhylomeDB; Q6P402; -.
DR   Reactome; R-DRE-5620912; Anchoring of the basal body to the plasma membrane.
DR   PRO; PR:Q6P402; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0097539; C:ciliary transition fiber; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR   InterPro; IPR033545; CEP89.
DR   PANTHER; PTHR36170; PTHR36170; 1.
PE   2: Evidence at transcript level;
KW   Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Mitochondrion; Reference proteome.
FT   CHAIN           1..695
FT                   /note="Centrosomal protein of 89 kDa"
FT                   /id="PRO_0000288811"
FT   REGION          24..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          276..368
FT                   /evidence="ECO:0000255"
FT   COILED          406..632
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        33..49
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..144
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   695 AA;  79305 MW;  AB10572F5A2385FA CRC64;
     MSSKFNFSLR RKEKREFRNI AHGLIPAATI APRPAVPRTP PPRSPNPSPE RPRSALAAAI
     LSSSLTGRTV AIPSPRQRSY SESDCSRADS QADFEPYATA LYTRDRWPGS VTGRPPVPSP
     GRTDEDDDED DEGNDIDELE GLEGDEDHVY QSLERQSRAD DINVVYAVPL KHKKSEIDSD
     VDEETEDSAF DIVSPLQTEE ETVVPEGAGQ TQPSSLPQPR SVSRRSMASP ELDDWSSPRS
     LKTSKRKSSR TNKESPVRVN ERDRSSEDSE VLRSTLEVQH ALVKELKEQN QILSQEKETL
     EKRCLQQSQH MKHLQQELCH THRERGNSTG EGSELSSLRQ QAQELVDEND GLKMTVHRLN
     VELSRYQARF RPLTKDENAQ LKGLPVKGPA PPWLLDMKYL SPLLLAYEDH LNAKDKLLKS
     CEEELQSLRV RAEEVIQENE KLHTQVSKSS TVSNKEWRQL QEQARLVLEE NQVLIEQLEL
     QHAKAKEAHS KHAQEVCKVS KKVMLLEAEK QSLEKELEVE RKEHRALKTE FQRVRLALEH
     SLSLAEHQTV TDKLKRQLQD HEKVKTCEVE DLQVRLSALE VERKTLLLDK TNLNTHIKHL
     ETELQLSQQA NRKAQRRVSV LKQQVEDSLE KELIAHQYLA NIVTLAEKTT HERDQLMLMA
     STLEKDKQGV LTRIIESTVN LGKLQEKVKV FLLQS