CEP57_BOVIN
ID CEP57_BOVIN Reviewed; 499 AA.
AC Q865V0; Q32L39;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Centrosomal protein of 57 kDa;
DE Short=Cep57;
DE AltName: Full=Testis-specific protein 57;
DE AltName: Full=Translokin;
GN Name=CEP57; Synonyms=TSP57;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12717444; DOI=10.1038/ncb979;
RA Bossard C., Laurell H., Van den Berghe L., Meunier S., Zanibellato C.,
RA Prats H.;
RT "Translokin is an intracellular mediator of FGF-2 trafficking.";
RL Nat. Cell Biol. 5:433-439(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-492.
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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=AAI09783.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AY225094; AAO73940.1; -; mRNA.
DR EMBL; BC109782; AAI09783.1; ALT_SEQ; mRNA.
DR RefSeq; NP_852115.1; NM_181450.1.
DR AlphaFoldDB; Q865V0; -.
DR SMR; Q865V0; -.
DR IntAct; Q865V0; 2.
DR STRING; 9913.ENSBTAP00000046049; -.
DR PaxDb; Q865V0; -.
DR PRIDE; Q865V0; -.
DR GeneID; 353245; -.
DR KEGG; bta:353245; -.
DR CTD; 9702; -.
DR eggNOG; ENOG502QTZR; Eukaryota.
DR InParanoid; Q865V0; -.
DR OrthoDB; 1255254at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISS:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0034453; P:microtubule anchoring; IEA:InterPro.
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 2: Evidence at transcript 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_0000189531"
FT REGION 1..58
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 277..490
FT /note="Mediates interaction with microtubules"
FT /evidence="ECO:0000250"
FT REGION 334..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 63..241
FT /evidence="ECO:0000255"
FT COILED 389..450
FT /evidence="ECO:0000255"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XR8"
FT CONFLICT 113
FT /note="P -> Q (in Ref. 2; AAI09783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 56986 MW; 685DE587F7D8ED40 CRC64;
MAAASVSETS ASQFSNILAE PSKSNGSMVR HSSSPYVVYP PDKPFLNSDL RRSPNKPTFA
YPESNSRAIF SALKNLQDKI RRLELERIQA EESVKTLSKE TIEYKKVLDE QIPERENSKN
EESKHNQELT SQLLAAENKC NLLEKQLEYM RNMIKHAEME RTSVLEKQVS LERERQHDQT
HVQNQLEKLD LLEQEYNKLT TMQALAEKKM QELEAKLRQE EQERKRMQAK AAQLQTGLEV
NRLIYEDKAT SCVPNTKRIK KKKSKPPEKK GSRNYFAVQP HYRLCLGDMP FVAGKSTSPS
HAVVANVQHV LHLMKQHSKV LCNDRVVSSI PLAKQVSSRT GKSKKSATPP SSSSVNEELS
EVLQTLQDEF GQMSFDHQQL AKLIQESPTV ELKDNLECEL EALVGRMEAK ANQITKVRKY
QAQLEKQKLE KQKKELKATR KTLDEEGNSS SRSTTTGTTN KKDFAKPRPG EKSRKNLQLL
KDMQSIQNSL QSNSLCWDY
