ID   CP131_DANRE             Reviewed;        1113 AA.
AC   U3JAG9; Q08CN2;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Centrosomal protein of 131 kDa;
DE   AltName: Full=5-azacytidine-induced protein 1;
GN   Name=cep131; Synonyms=azi1;
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 GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-779.
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION IN CILIOGENESIS, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=19254375; DOI=10.1186/1471-2121-10-17;
RA   Wilkinson C.J., Carl M., Harris W.A.;
RT   "Cep70 and Cep131 contribute to ciliogenesis in zebrafish embryos.";
RL   BMC Cell Biol. 10:17-17(2009).
RN   [4]
RP   POSSIBLE FUNCTION IN MELANOSOME TRAFFICKING.
RX   PubMed=24550735; DOI=10.1371/journal.pgen.1004083;
RA   Chamling X., Seo S., Searby C.C., Kim G., Slusarski D.C., Sheffield V.C.;
RT   "The centriolar satellite protein AZI1 interacts with BBS4 and regulates
RT   ciliary trafficking of the BBSome.";
RL   PLoS Genet. 10:E1004083-E1004083(2014).
CC   -!- FUNCTION: Cilium-specific protein required for the regulation of
CC       cilium/flagellum formation (PubMed:19254375). Involved in centriole
CC       duplication (By similarity). May play a role in melanosome trafficking
CC       (PubMed:24550735). {ECO:0000250|UniProtKB:Q9UPN4,
CC       ECO:0000269|PubMed:19254375, ECO:0000305|PubMed:24550735}.
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC       {ECO:0000269|PubMed:19254375}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriolar satellite
CC       {ECO:0000250|UniProtKB:Q9UPN4}. Cytoplasm, cytoskeleton, cilium basal
CC       body. Cytoplasmic vesicle, secretory vesicle, acrosome
CC       {ECO:0000250|UniProtKB:Q62036}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in cilia cells in the spinal canal,
CC       pronephros and Kupffer's vesicle. {ECO:0000269|PubMed:19254375}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein leads to
CC       truncated cilia formation and impaired intraflagellar transport
CC       processes. {ECO:0000269|PubMed:19254375}.
CC   -!- SIMILARITY: Belongs to the CEP131 family. {ECO:0000305}.
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DR   EMBL; CT573318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC124167; AAI24168.1; -; mRNA.
DR   AlphaFoldDB; U3JAG9; -.
DR   SMR; U3JAG9; -.
DR   STRING; 7955.ENSDARP00000080097; -.
DR   PaxDb; 7955-ENSDARP00000127237; -.
DR   AGR; ZFIN:ZDB-GENE-090508-16; -.
DR   ZFIN; ZDB-GENE-090508-16; cep131.
DR   eggNOG; ENOG502QT0Q; Eukaryota.
DR   InParanoid; U3JAG9; -.
DR   OMA; MACTRER; -.
DR   Reactome; R-DRE-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-DRE-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-DRE-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-DRE-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-DRE-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-DRE-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-DRE-8854518; AURKA Activation by TPX2.
DR   PRO; PR:U3JAG9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0034451; C:centriolar satellite; IBA:GO_Central.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005929; C:cilium; IEA:GOC.
DR   GO; GO:0005576; C:extracellular region; IEA:GOC.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR   GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; IMP:ZFIN.
DR   GO; GO:0035721; P:intraciliary retrograde transport; IMP:UniProtKB.
DR   GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IEA:InterPro.
DR   GO; GO:0070121; P:Kupffer's vesicle development; IMP:UniProtKB.
DR   GO; GO:0032402; P:melanosome transport; IMP:UniProtKB.
DR   GO; GO:0090317; P:negative regulation of intracellular protein transport; IMP:UniProtKB.
DR   GO; GO:0010824; P:regulation of centrosome duplication; IBA:GO_Central.
DR   GO; GO:0050953; P:sensory perception of light stimulus; IMP:UniProtKB.
DR   InterPro; IPR030465; CEP131.
DR   PANTHER; PTHR31540; CENTROSOMAL PROTEIN OF 131 KDA; 1.
DR   PANTHER; PTHR31540:SF1; CENTROSOMAL PROTEIN OF 131 KDA; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Centromere; Chromosome; Cilium biogenesis/degradation;
KW   Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Differentiation;
KW   Reference proteome; Transport.
FT   CHAIN           1..1113
FT                   /note="Centrosomal protein of 131 kDa"
FT                   /id="PRO_0000429319"
FT   DOMAIN          276..296
FT                   /note="IQ"
FT   REGION          78..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          259..371
FT                   /evidence="ECO:0000255"
FT   COILED          580..1111
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        232..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        188
FT                   /note="A -> T (in Ref. 2; AAI24168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234
FT                   /note="Q -> R (in Ref. 2; AAI24168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        299
FT                   /note="I -> T (in Ref. 2; AAI24168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="K -> R (in Ref. 2; AAI24168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        365
FT                   /note="A -> P (in Ref. 2; AAI24168)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        746
FT                   /note="K -> R (in Ref. 2; AAI24168)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1113 AA;  128302 MW;  318907F080E7688B CRC64;
     MHTTRSPSAS IQAGAAGDAL DLSLNGSQLT MGRRPSSASP GKHFSRSISV SVAYDGRGKR
     NTLTDAGLGS SRAIKNLRRS NSTTQVNQQA NTSLSSEGHT EDFLALFNSS SDGRRKLASL
     SKMSKDRTTW NILDDQPRVF PVPSSSHSTC SMDSPTGLKK REAGVSLAAN FTANNRSNKA
     AVGNAVTAIL HNNHSEKPLT PKSSNQKPSF NNLIKATVND DVTLDVSGSL TKSQKNFSSA
     SSSSNNNAPR SPRSPGQPRR REVTEEEAER YIQQVNHAAI IIQRWYRRHV NSKRANENII
     KQLLASKKKE REQRAEEAKT TESLKKKEDD RKRIREEKAR LARLTAIQEL QQKRAQRAAE
     VQQIAEQETE ALRHPGKVGR KKLTKSSPTS PTDIKAKNTD SNVNVVSDLD DVTNLRAASP
     AGSACRVSQC SQEILQRSVS MEDQRQGASS SRAQSKTTLN DLLDTLKLLE EEPERLSEPK
     SYRKDKYSWI DEDGDSNSLT TDNVERHRQL SQTPALPDGG ALLSEAKLQS IMSFLDEMEK
     SEQERPRSVT SGSHREVVLS EEDLAVVEQA SATAAEVTGS MMRLRLELDE KKRTVNMLQT
     ALAQQRELTI RHVKETEKEL NHTFQLQKEQ YEATIQRHLT FIDQLIDDKK ALSERCEEVV
     GELKQVDQKY TKKIAQMQEQ HELVWQILGP MCEEIKKLKE LMSATEKVRR EKWINEKTKK
     IKEITVKGLE PEIQKLISKH KQELKKLRVL HEAELLQADE RAAQRYVRQS EELRQQLEKE
     KDEQCQRERE LAKQRFEKQL QEEENVLQQQ RRRLYKEVSE EKERLTQLAA RQHAELEDLR
     KQLEDNSSLA GRALREELEK SRDEQERRHQ VEIKALKERL EIEKQTWEEN YMKKEEAWLL
     SRERELKEEV RRGRDKEIEL AIQRLEVETR EAREECERAA DNRMKRVREK YEAELRDLER
     SERTSLQKQQ EMREKHSEME AELLRLQSLL RQREQEISDL TQVTARDKLS EERRSLSEVI
     RQEFAERLIE LEEENRRMKM EVSEAKARLR LEVERVTREK EEELAEVHQR VKSAILKKEE
     TVNNLRKQHE AAVKRADHLE SLLEQQRKQL LGK
//