CE295_RAT
ID CE295_RAT Reviewed; 2395 AA.
AC A4L9P8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Centrosomal protein of 295 kDa {ECO:0000305};
GN Name=Cep295 {ECO:0000250|UniProtKB:Q9C0D2};
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 158-2395.
RA Hagemann C., Stojic J., Weigelin B., Gerngras S., Roosen K., Vince G.H.;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Centriole-enriched microtubule-binding protein involved in
CC centriole biogenesis. Essential for the generation of the distal
CC portion of new-born centrioles in a CENPJ- and CEP120-mediated
CC elongation dependent manner during the cell cycle S/G2 phase after
CC formation of the initiating cartwheel structure. Required for the
CC recruitment of centriolar proteins, such as POC1B, POC5 and CEP135,
CC into the distal portion of centrioles. Also required for centriole-to-
CC centrosome conversion during mitotic progression, but is dispensable
CC for cartwheel removal or centriole disengagement. Binds to and
CC stabilizes centriolar microtubule. {ECO:0000250|UniProtKB:Q9C0D2}.
CC -!- SUBUNIT: Interacts (via ALMS motif) with microtubules; this interaction
CC is direct. {ECO:0000250|UniProtKB:Q9C0D2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q9C0D2}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9C0D2}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9C0D2}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9C0D2}. Note=Associates with both of the
CC converted centrioles during G1 but becomes more enriched at the newly
CC formed daughter (or unconverted) centrioles during S, G2, and early M
CC phases. In early S phase, localized at the procentriolar microtubule
CC wall and enriched at the proximal ends of the centrioles in CENPJ- and
CC CEP135-dependent manner. Colocalizes with SASS6 and CEP250 proteins.
CC Colocalizes with CEP135 and CEP192 at the centrosomes. Associates with
CC interphase microtubules and mitotic spindles. Colocalizes with
CC centriolar acetylated tubulin. {ECO:0000250|UniProtKB:Q9C0D2}.
CC -!- DOMAIN: The N-terminal and the ALMS motif-containing C-terminal regions
CC are essential for CEP295-mediated centriole elongation.
CC {ECO:0000250|UniProtKB:Q9C0D2}.
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; AABR03062369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EF460314; ABO47656.1; -; mRNA.
DR AlphaFoldDB; A4L9P8; -.
DR SMR; A4L9P8; -.
DR STRING; 10116.ENSRNOP00000029431; -.
DR iPTMnet; A4L9P8; -.
DR PhosphoSitePlus; A4L9P8; -.
DR PaxDb; A4L9P8; -.
DR PRIDE; A4L9P8; -.
DR UCSC; RGD:1311723; rat.
DR RGD; 1311723; Cep295.
DR VEuPathDB; HostDB:ENSRNOG00000010999; -.
DR eggNOG; ENOG502QSZR; Eukaryota.
DR InParanoid; A4L9P8; -.
DR PhylomeDB; A4L9P8; -.
DR TreeFam; TF331536; -.
DR PRO; PR:A4L9P8; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000010999; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; A4L9P8; baseline and differential.
DR Genevisible; A4L9P8; RN.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990498; C:mitotic spindle microtubule; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
DR GO; GO:1903724; P:positive regulation of centriole elongation; ISS:UniProtKB.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; ISS:UniProtKB.
DR GO; GO:1904951; P:positive regulation of establishment of protein localization; ISS:UniProtKB.
DR GO; GO:1901985; P:positive regulation of protein acetylation; ISS:UniProtKB.
DR GO; GO:0046599; P:regulation of centriole replication; IBA:GO_Central.
DR InterPro; IPR029560; CEP295.
DR PANTHER; PTHR21553:SF25; PTHR21553:SF25; 2.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..2395
FT /note="Centrosomal protein of 295 kDa"
FT /id="PRO_0000324597"
FT REGION 1..540
FT /note="Necessary for centriole targeting and microtubule
FT association"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D2"
FT REGION 602..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1677..1715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1819..1845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1875..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1989..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2329..2395
FT /note="ALMS motif"
FT REGION 2354..2395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..84
FT /evidence="ECO:0000255"
FT COILED 114..148
FT /evidence="ECO:0000255"
FT COILED 209..277
FT /evidence="ECO:0000255"
FT COILED 488..538
FT /evidence="ECO:0000255"
FT COILED 567..592
FT /evidence="ECO:0000255"
FT COILED 817..848
FT /evidence="ECO:0000255"
FT COILED 1444..1488
FT /evidence="ECO:0000255"
FT COMPBIAS 1218..1272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1878..1892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1990..2013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2363..2379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D2"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D2"
FT MOD_RES 1565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D2"
SQ SEQUENCE 2395 AA; 269982 MW; 4393391A96C9837B CRC64;
MKRKVMNGKL RLSPNEEAFI LKEDYERRRK LRLLQVREQE RGIAFQIRED IKQRRNQQVS
HLAEELRAEW EEAQSQKIQN LEKLYLASLR HMGDGHQQAK ENEPDLDALS RRAAERKTKA
EARHKEALKA QKKQKEMLMK QKTRHIKARK EAVLVEKERS AKMARLPPPV PSPFENIDIN
RIPSLKTNRS TYHHISAFVS RQMGTKQPDA HLAAEEEARR VERLRKQAAQ ERMEQSERAH
ARGSQAMKKI HLAQNQERLM EELKQLQRED LACKRQTAAQ MPSQLLELPY RRSEMKEDWQ
RELEFAFEDV YSADRKVKGN LILHLKPEPL PTMSDQLQDE ELDLSMEQEN EVPLATKTQQ
IPSRILLKRL LNKIRNQKSL WTIKSFSEDD NQVTASIISE IERKVPSTDS GTITTGETAV
SFEQEQVMGS DRLMIESGPP SSEDKPLCYK SVTGKEQAMG VSPPATTVAQ SSVLLHPQEE
AARLRMSARH KQIMEIEEQK QKQLELLEQI EQQKLRLETD CFQAQLEETR KQADHLEVRP
APVSHAMISD EERHRQMIRN YQYQLLQQNR LHKQTVETAR KRLLEYQTVL KERCPSMSAR
SLIPDSVVSE PPQQAQKPAV ASDYWDPSQR PKLSPSKYQP VQPSQIPALD QNHIQVPRQG
HIPQRQGETA RAKQSVESQE RQWQFSQVET QQRDYEFIFK DSHSLSRTSS YVRPQTLQAA
GEVSKPLRAI ICQTSDSQQI SSEDSENISS KPTEPSSSLP LMPECSSSSL SVKLESETIQ
KAFTTVNRSV ISQMHGQPLS SSETGTTQQG DIRFLQGQLE LQKKVLQERQ EAQEKLLSCT
QKELEEQTGI PVFFPSPVGN MFSSLPSASA ESGNIQTSST KSDATVSSDS MDNPYSQPIS
LRQTNLEFLQ EQFSVEKDNL QARREAQEVS FTHTQSKLDK IVRSEQTGSS WPQLVALESF
SSLTSADTQS RKIQKPPLPT NKKGLLPSQS EILSSQDGSS GFLQQTLPLQ NTLKLLQEQL
TIQRGMIQPR LNAQETLLLH KERCSVDSKA GPVNSLSSAV AQHSEAGPQS LQELYSSKKE
NTVLSSHLIT PEVQEESHGS PQHSLPRQEH FASLQEQAHI QRVILGARKQ IQEFAHKQNE
FKKGLYSQQT GALSSPSQGT GWEISQESLS VRSDSTDPLS HFKIPGFQER LVRALQPTFP
LRDNLQEHQE WVDPEKESFQ FSPQTQENRS SQQTGFSSFT PSLRQPSCVS LPSVDSGITQ
HPLSTERDSK VTSSHLQIPE LQHRLLKISQ LIQPQQDSLK ALQEQLATSR TIIHSRQEAL
EETLREWKEK IFPEQVGPFS PLMTQHSFAS FPVSDIERAQ ELCSTNSEGA ISSGYSEMLE
LPDRALGLSC TALPQQGNLT VHPGHLHAQT NSFHSTEKAQ EKLVFPRPCK LEEISAEHSI
QPPHDDLQAL QQQLDVHREA IRSCQDIQEE LLLQRLNKLE QRVSSKQISS SPLLSQVALP
IANSEGTLQS SPAKNDDTEM LRSHSEYLNF SQPLQDNVTE QLDLEVVFHK ELLLHKQKSQ
TKSESPEHAA PFNDAVIPRL QDRLLSYFQP ALTQQDSMSP QKQLNLQREA LYSRQKAQEE
LLVQRQTALQ QQVQKHRETL KGFSNVSQTR AASGENDLEM QKTEQLTGWF PHIQGWPWGD
SSQGSSSGDQ PGAAAVHAEH SGESLGKELS GRASKPPVSK VKCVFDLNQH ELSTIQEVES
PTSGRTSMPG KAEFYRDRDP LRVSVSREQS YLGSPVAHDP FGCHQPSVQE NSKSHDTAKA
VKVKKSDIED HALLSHAISE EEEEEEACTN LSPLMKPDDE VETQEISQEL LSSMTVSTGS
FLSYEITDLS LTDPESFSEQ TEHQEQESSS KEEETGSLSC AVPSTQVTYQ QQHSLGAHNS
LLPTEEENAS DQTHVHQIID KDINEANLIP DKRDFQVPAV DLDFPELEHL FPHLHRQLFK
PLEPHLDLDL SSPGTSQEDR DFYQQNSESS SEKHVKALST STLCFTALTA GSHSPNSRLN
QQLDVNLAHA TTEGSEQSFQ QLLPEFSSQE SQHTDLPSIY SIEARGTSQS MENQNYSEIL
QNKKKSIYFQ PSTENLSPAC SSSDTTLFDQ LHPQHSTPCG SVSSEGSVKQ LEGREEMLGF
EELSRRAVPM SQRLTEDENV VLPINPYVGT VEMETSIQGS NSLSIQNEKP IQNVIKTETT
KAVRNVCQLA QEEHMLKSES CPFRRPIPVW ETETGYGIME EPDLTLLSTS DISITDTDLA
NLTIEDNEAQ CSQAGAVQPS SSVETTFCGA ASEPWADQPT VASSAIPGSL GEAFMKRKKT
FMERSYQRQR EIWNKTPLPQ AKVSKEKLST SSSLSHLKEA VSGDETAKRN RSQCI
