CP131_DANRE
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 03-AUG-2022, entry version 40.
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.ENSDARP00000127237; -.
DR PaxDb; U3JAG9; -.
DR PRIDE; U3JAG9; -.
DR Ensembl; ENSDART00000181478; ENSDARP00000150135; ENSDARG00000109476.
DR ZFIN; ZDB-GENE-090508-16; cep131.
DR eggNOG; ENOG502QT0Q; Eukaryota.
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 Proteomes; UP000814640; Unplaced.
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; PTHR31540; 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
