CE104_RAT
ID CE104_RAT Reviewed; 922 AA.
AC D3Z8X7; A0A0G2JUH6; Q62965;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 3.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Centrosomal protein of 104 kDa;
DE Short=Cep104;
DE AltName: Full=Glycine-, glutamate- and thienylcyclohexylpiperidine-binding protein;
DE Short=Gly-, L-Glu and TCP-binding protein;
DE Short=GlyBP;
GN Name=Cep104;
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 392-922 (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Hippocampus;
RX PubMed=7488117; DOI=10.1006/bbrc.1995.2636;
RA Kumar K.N., Babcock K.K., Johnson P.S., Chen X., Ahmad M., Michaelis E.K.;
RT "Cloning of the cDNA for a brain glycine-, glutamate- and
RT thienylcyclohexylpiperidine-binding protein.";
RL Biochem. Biophys. Res. Commun. 216:390-398(1995).
CC -!- FUNCTION: Required for ciliogenesis and for structural integrity at the
CC ciliary tip. {ECO:0000250|UniProtKB:O60308}.
CC -!- SUBUNIT: Interacts with CCP110 and CEP97. Interacts with ARMC9,
CC TOGARAM1, CCDC66 and CSPP1. {ECO:0000250|UniProtKB:O60308}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000250|UniProtKB:O60308}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:O60308}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:O60308}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O60308}.
CC Note=In interphase non-ciliated cells, localizes to the distal ends of
CC both the mother and daughter centrioles. In ciliated cells, present at
CC the distal end of the daughter centriole, but not on the mother
CC centriole, and at the tip of primary cilium. Localization at the
CC ciliary tip is also observed in motile cilia. Throughout S phase,
CC associated with both mother and daughter centrioles in each centrosome.
CC During metaphase and telophase, present at both spindle poles.
CC {ECO:0000250|UniProtKB:O60308}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=D3Z8X7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=D3Z8X7-2; Sequence=VSP_058205;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the brain. Also
CC detected, although at much lower levels, in the heart and the liver.
CC Within the brain, expressed in the cerebral cortex, hippocampus,
CC cerebellum and brainstem. {ECO:0000269|PubMed:7488117}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA99783.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AABR07050617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U53513; AAA99783.1; ALT_INIT; mRNA.
DR RefSeq; NP_659550.2; NM_145082.2.
DR AlphaFoldDB; D3Z8X7; -.
DR SMR; D3Z8X7; -.
DR STRING; 10116.ENSRNOP00000034972; -.
DR iPTMnet; D3Z8X7; -.
DR PhosphoSitePlus; D3Z8X7; -.
DR PaxDb; D3Z8X7; -.
DR PRIDE; D3Z8X7; -.
DR GeneID; 246295; -.
DR KEGG; rno:246295; -.
DR UCSC; RGD:708505; rat.
DR CTD; 9731; -.
DR RGD; 708505; Cep104.
DR VEuPathDB; HostDB:ENSRNOG00000025000; -.
DR eggNOG; KOG4825; Eukaryota.
DR HOGENOM; CLU_003200_0_0_1; -.
DR InParanoid; D3Z8X7; -.
DR OMA; VQGNDYN; -.
DR OrthoDB; 242784at2759; -.
DR TreeFam; TF323766; -.
DR PRO; PR:D3Z8X7; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000025000; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; D3Z8X7; baseline and differential.
DR Genevisible; Q62965; RN.
DR GO; GO:0005814; C:centriole; ISO:RGD.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0016595; F:glutamate binding; IMP:RGD.
DR GO; GO:0016594; F:glycine binding; IMP:RGD.
DR GO; GO:0016596; F:thienylcyclohexylpiperidine binding; IMP:RGD.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Reference proteome; Repeat.
FT CHAIN 1..922
FT /note="Centrosomal protein of 104 kDa"
FT /id="PRO_0000435986"
FT REPEAT 526..564
FT /note="HEAT 1"
FT REPEAT 601..637
FT /note="HEAT 2"
FT REGION 307..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 210..277
FT /evidence="ECO:0000255"
FT COILED 678..705
FT /evidence="ECO:0000255"
FT COMPBIAS 383..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 912..922
FT /note="SKSSSRTHTRR -> KS (in isoform 2)"
FT /id="VSP_058205"
FT CONFLICT 393
FT /note="S -> T (in Ref. 2; AAA99783)"
FT /evidence="ECO:0000305"
FT CONFLICT 469..471
FT /note="EDL -> GFV (in Ref. 2; AAA99783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 922 AA; 103790 MW; 1B08DE78210283C9 CRC64;
MPHKIGFVVV SSSGHEDGFS ARELMIHAPT VSGWRSPKFC QFPQEIVLQM VERCRIRKLQ
LLAHQYMISS KVEFYISESL PEYLVPYQAE RFRRLGYVSL CDNEKTGCKA RELKSVYVDA
VGQFLKLIFH QTTNKYNVNQ VALVAINIIG DPADLGDESN TTCREKLIDH YLGHSPHNPE
DPALDGTFAG RSDYISPLDD LAFDMYQDPE VAQIIRRLDE RKREAAKKER YDHAKKLKQA
IADLQKVGER LGRYEVEKRR AVEKEDYDLA KEKKQQMARY RAQVYEQLEL HGLLQGEPEM
QRPFALPLQP LASPSSPQHW KAVSSLPRTE ELAAEDTCAG PILQEKPLAS SPRHSAVDRS
PPAAGPAPRS HVEALPYDER PLPVTRKQLE EPSAEPEVRE ADSDVRRRGV SAEPEPLTEK
ALREASSAID TLGEALVAGA YSKMWSCRED ALLALYKRLM EMPVGTQKED LKNMLRASVF
LIRRAIKDIV TSVFQASLKL LKMIITQYIP KHKLGKLDTT YCVERAIPLL LARTGDSSAR
LRVMALNFIQ EMALFKEVRS LQLIPSYLVQ PLKTNASVHL AMSQVDLLAR LLRDLGTEGS
GFTVDNVMKF AVSALEHRVY EVRETAVRII LDMYRQHPAL TLEHLPPDDS TTRRNLLYKA
IFEGFAKIDG RPTEAEGKTQ KRVVTKEAEK QKKEETKALQ GLSAAPRETQ AGVQEKENEA
VKLKNQDPQG RKAAPPDTPE IPDNHYLDNL CIFCGERNES FTEEGLDLHY WKHCLMLTRC
DHCRQVVEIS SLTEHLLTEC DKRDGFGKCP RCSEAVPKEE LPRHIKTKEC NPAKSEKVAN
RCPLCHENFA PGEEAWKVHL MGSAGCTMNL RKTHILCKAP APQQGKGPMA SKSGTSAPKV
GSKIPTPKGG LSKSSSRTHT RR
