CP135_DANRE
ID CP135_DANRE Reviewed; 1164 AA.
AC Q5RG45;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Centrosomal protein of 135 kDa;
DE Short=Cep135;
GN Name=cep135; ORFNames=si:dkeyp-117h8.1;
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).
CC -!- FUNCTION: Centrosomal protein involved in centriole biogenesis. Acts as
CC a scaffolding protein during early centriole biogenesis. Required for
CC the targeting of centriole satellite proteins to centrosomes. Also
CC required for centriole-centriole cohesion during interphase by acting
CC as a platform protein for cep250 at the centriole (By similarity).
CC {ECO:0000250|UniProtKB:Q66GS9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q66GS9,
CC ECO:0000250|UniProtKB:Q6P5D4}. Note=During centriole biogenesis, it is
CC concentrated within the proximal lumen of both parental centrioles and
CC procentrioles. {ECO:0000250|UniProtKB:Q66GS9}.
CC -!- SIMILARITY: Belongs to the CEP135/TSGA10 family. {ECO:0000305}.
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DR EMBL; CR352243; CAI21313.2; -; Genomic_DNA.
DR EMBL; BX294157; CAI21313.2; JOINED; Genomic_DNA.
DR EMBL; BX294157; CAM56389.1; -; Genomic_DNA.
DR EMBL; CR352243; CAM56389.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001186919.1; NM_001199990.1.
DR RefSeq; XP_009298989.1; XM_009300714.2.
DR PDB; 7BJI; X-ray; 2.58 A; A/B/C/D=64-190.
DR PDBsum; 7BJI; -.
DR AlphaFoldDB; Q5RG45; -.
DR SMR; Q5RG45; -.
DR STRING; 7955.ENSDARP00000107420; -.
DR PaxDb; Q5RG45; -.
DR Ensembl; ENSDART00000033436; ENSDARP00000035272; ENSDARG00000002991.
DR GeneID; 553303; -.
DR KEGG; dre:553303; -.
DR CTD; 9662; -.
DR ZFIN; ZDB-GENE-041210-325; cep135.
DR eggNOG; ENOG502QT27; Eukaryota.
DR GeneTree; ENSGT00940000165649; -.
DR InParanoid; Q5RG45; -.
DR OMA; QGRENTM; -.
DR PhylomeDB; Q5RG45; -.
DR TreeFam; TF326518; -.
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:Q5RG45; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000002991; Expressed in mature ovarian follicle and 27 other tissues.
DR ExpressionAtlas; Q5RG45; baseline and differential.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0007099; P:centriole replication; IBA:GO_Central.
DR GO; GO:0010457; P:centriole-centriole cohesion; IEA:InterPro.
DR InterPro; IPR026732; Cep135.
DR PANTHER; PTHR23159:SF18; PTHR23159:SF18; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..1164
FT /note="Centrosomal protein of 135 kDa"
FT /id="PRO_0000307124"
FT REGION 475..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 91..153
FT /evidence="ECO:0000255"
FT COILED 198..475
FT /evidence="ECO:0000255"
FT COILED 524..887
FT /evidence="ECO:0000255"
FT COILED 922..1121
FT /evidence="ECO:0000255"
FT COMPBIAS 1121..1144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 65..144
FT /evidence="ECO:0007829|PDB:7BJI"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:7BJI"
SQ SEQUENCE 1164 AA; 134956 MW; B1FCEE379964CFE2 CRC64;
MTMTTNAERK FINLRKRLDQ LGYRQPLAIE SLPLVEKLFS DLIHTTESLR NAKLAAGKTE
KESRNVDAIL EPYKTENARL VKENNEMHLG LLKLREEKDR ISRELKAYIR KLDHETSDLK
FLNNQYVQKV RSLEKDSNGK TERILQLQEK NMQAVVQTPG GKKRSIPFRR QRMQTDELLP
SSGGYVPPAV AQPDDPYIAD LLQVADDRIQ ELQKEVAQLK LDLERAQGGI KHLNKQVEER
DKEIERLNRA LDGGRPHDVI SLEAQNISNE KLIAHLNLQI EYLQETNRSL EQRVDSLQQK
KKTVSSEVAD LSARNQELCQ ELTQIDQLAQ QLEKDKEMVL ETADMELQEA KKAIQRQQRE
LEGQEEVIST LRRDMADGDH VKDQLRNQLL DLQDQNNKME GLIHFLEEDK KRLQDKIEAM
MQEDKEMVLE LERMRARHGM CGKDHSPSRL DAFVKSLEEE RNYYREEVER YRLVRGRTDR
SPTPVGRGRS PRGRGSWHGK RDGDAELSRV VKERDELQSV LLGFEKHMED IQTRVKLLTA
ERDQLSSQCQ QAQEELRRVQ RELESSELQR RIRDDREQTE AELQRVTAER DALRDRLKVA
HSTALTDREQ EEFRFLDLEN TIEKLEREKA DLRAQVTVLK ESRVVVEKEL KAQSAVLLQN
VEEATQQRVE SSALRLLQEQ MEQSLSDVQH RLSVKTNELQ AAHQQIDKLE EKIADLSRHG
SSQKDEVVIL QNTIASLDRE KDTLQDAVDQ KTESVVLLQQ EVHRKEETLL EVRLTVTDLE
NSLNQLQAVL SSREREIASL RRQLDQSQEE LFSVSRDREV ALRENRRLQD DLATMTRENQ
AVHAEMQEAL NERDELKLRV HSYISEVARI ESLMAAKEQE NRDMLERFRS IHTESEDKEL
KLQQSEGLNN SIRLELLSSD TERRHLRERV SLQDREIQEH LNALQAYEAQ VSSLARAMSR
LEEEVQAARA EKASVLADLA SVRELCVKLD SSKELTVRQL TSKSMELERV TGELEDVRSE
MELLKKQLGS ERLTVRNLET LLSTNRQKEF QTHISASEKE SELKVLKDRL ALADSKTAGH
AREVSQLRGK VSQLQTEMDV LKRQLTTERF ERERAVQEMR RQGLSFSSLR SSSPLSTSLS
PRPASPERSI LRTPERSTDK TQDK
