CEP57_RAT
ID CEP57_RAT Reviewed; 499 AA.
AC B4F7A7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Centrosomal protein of 57 kDa;
DE Short=Cep57;
DE AltName: Full=Translokin;
GN Name=Cep57;
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;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=18294141; DOI=10.1042/bj20071501;
RA Momotani K., Khromov A.S., Miyake T., Stukenberg P.T., Somlyo A.V.;
RT "Cep57, a multidomain protein with unique microtubule and centrosomal
RT localization domains.";
RL Biochem. J. 412:265-273(2008).
CC -!- FUNCTION: Centrosomal protein which may be required for microtubule
CC attachment to centrosomes. May act by forming ring-like structures
CC around microtubules. Mediates nuclear translocation and mitogenic
CC activity of the internalized growth factor FGF2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and homooligomer. Interacts with FGF2 and RAP80.
CC Does not interact with FGF1 or FGF2 isoform 24 kDa. Interacts with
CC microtubules (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous (at protein level).
CC {ECO:0000269|PubMed:18294141}.
CC -!- DOMAIN: The C-terminal region mediates the interaction with
CC microtubules and is able to nucleate and bundles microtubules in vitro.
CC {ECO:0000250}.
CC -!- DOMAIN: The centrosome localization domain (CLD) region mediates the
CC localization to centrosomes and homooligomerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the translokin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI68198.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EDL78488.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; BC168198; AAI68198.1; ALT_INIT; mRNA.
DR EMBL; CH473993; EDL78488.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001101594.2; NM_001108124.3.
DR RefSeq; XP_006242585.1; XM_006242523.3.
DR RefSeq; XP_006242586.1; XM_006242524.3.
DR AlphaFoldDB; B4F7A7; -.
DR SMR; B4F7A7; -.
DR STRING; 10116.ENSRNOP00000009318; -.
DR PaxDb; B4F7A7; -.
DR PRIDE; B4F7A7; -.
DR Ensembl; ENSRNOT00000009318; ENSRNOP00000009318; ENSRNOG00000006792.
DR GeneID; 315423; -.
DR KEGG; rno:315423; -.
DR UCSC; RGD:1309884; rat.
DR CTD; 9702; -.
DR RGD; 1309884; Cep57.
DR eggNOG; ENOG502QTZR; Eukaryota.
DR GeneTree; ENSGT00530000063695; -.
DR HOGENOM; CLU_034321_2_0_1; -.
DR InParanoid; B4F7A7; -.
DR OMA; ASSRCCK; -.
DR OrthoDB; 1255254at2759; -.
DR PhylomeDB; B4F7A7; -.
DR TreeFam; TF329178; -.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR PRO; PR:B4F7A7; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000006792; Expressed in testis and 19 other tissues.
DR Genevisible; B4F7A7; RN.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISO:RGD.
DR GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0034453; P:microtubule anchoring; IEA:InterPro.
DR GO; GO:0051260; P:protein homooligomerization; ISO:RGD.
DR GO; GO:0007286; P:spermatid development; ISO:RGD.
DR InterPro; IPR010597; Centrosomal_protein_57kDa.
DR InterPro; IPR025913; Cep57_CLD.
DR InterPro; IPR024957; Cep57_MT-bd_dom.
DR PANTHER; PTHR19336:SF11; PTHR19336:SF11; 1.
DR Pfam; PF14073; Cep57_CLD; 1.
DR Pfam; PF06657; Cep57_MT_bd; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..499
FT /note="Centrosomal protein of 57 kDa"
FT /id="PRO_0000381817"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..239
FT /note="centrosome localization domain (CLD)"
FT /evidence="ECO:0000250"
FT REGION 255..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..490
FT /note="Mediates interaction with microtubules"
FT /evidence="ECO:0000250"
FT REGION 424..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 63..242
FT /evidence="ECO:0000255"
FT COILED 388..491
FT /evidence="ECO:0000255"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XR8"
SQ SEQUENCE 499 AA; 57040 MW; 077C86BFE2B3C2C7 CRC64;
MAAASVSAAS DSQFSSVLAE PSRSNGNMVH HSSSPYVLYP PDKPFLNSDL RRSPNKPTFA
YPESNSRAIF SALKNLQDKI RRLELERIRA EESVKTLSRE TIEYKKVLDE QIQERENSKN
EESKHNQELA SQLVAAENKC NLLEKQLEYM RNMIKHAEME RTSVLEKQVS LERERQHDQS
HVQSQLEKLD LLEQEYNRLT AMQALAEKKM QELESKLHEE EQERKRMQAR AAELQSGIEA
NRLIFEDRNT SCVSTSTRKI KKKKSKPPEK KGFRNNFGAQ PHYRLCLGDM PFVAGTSTSP
SHAVVANVQH VLHLMKHHSR ALCNDRVVNS VPLAKQACSR GSKSKKSVAP PSSSVNEELS
DVLQTLQDEF GQMSFDHQQL TKLIQESPSE ELKDNLECEL EALVRRMEAK ANQITKVRKY
QAQLEKQSTD KQKELKGNKK TLDEEGNSSS RSSVITRTTS KKDFTKQRPG EKSRKNLQLL
KDMQTLQNSL QSSNVCWDY
