CE57L_XENLA
ID CE57L_XENLA Reviewed; 488 AA.
AC Q5FWP9;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Centrosomal protein cep57l1;
DE AltName: Full=Centrosomal protein 57kDa-like protein 1;
DE AltName: Full=Centrosomal protein of 57 kDa;
DE Short=Cep57;
DE Short=XCep57;
DE AltName: Full=Cep57-related protein;
DE Short=Cep57R;
GN Name=cep57l1; Synonyms=cep57, cep57r;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CLIP1; GAMMA-TUBULIN;
RP MIS12; NDC80 AND ZWINT.
RX PubMed=17803911; DOI=10.1016/j.cell.2007.07.023;
RA Emanuele M.J., Stukenberg P.T.;
RT "Xenopus Cep57 is a novel kinetochore component involved in microtubule
RT attachment.";
RL Cell 130:893-905(2007).
CC -!- FUNCTION: Required for spindle microtubule attachment to both
CC kinetochores and centrosomes. Also functions to tether minus-ends of
CC spindle microtubules to centrosomes. May act by forming ring-like
CC structures around microtubules, or by serving as a cross-linker or
CC scaffold at the attachment site. {ECO:0000269|PubMed:17803911}.
CC -!- SUBUNIT: Interacts with clip1, mis12, ndc80 and zwint. Interacts with
CC gamma-tubulin. {ECO:0000269|PubMed:17803911}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:17803911}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:17803911}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:17803911}. Note=Localizes to
CC spindle microtubules.
CC -!- SIMILARITY: Belongs to the translokin family. {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; BC089255; AAH89255.1; -; mRNA.
DR RefSeq; NP_001089236.1; NM_001095767.1.
DR AlphaFoldDB; Q5FWP9; -.
DR SMR; Q5FWP9; -.
DR PRIDE; Q5FWP9; -.
DR DNASU; 734283; -.
DR GeneID; 734283; -.
DR KEGG; xla:734283; -.
DR CTD; 734283; -.
DR Xenbase; XB-GENE-5897421; cep57l1.L.
DR OrthoDB; 1255254at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 734283; Expressed in egg cell and 18 other tissues.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
DR InterPro; IPR025913; Cep57_CLD.
DR InterPro; IPR024957; Cep57_MT-bd_dom.
DR Pfam; PF14073; Cep57_CLD; 1.
DR Pfam; PF06657; Cep57_MT_bd; 1.
PE 1: Evidence at protein level;
KW Centromere; Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore;
KW Microtubule; Reference proteome.
FT CHAIN 1..488
FT /note="Centrosomal protein cep57l1"
FT /id="PRO_0000381818"
FT REGION 232..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 71..226
FT /evidence="ECO:0000255"
FT COILED 377..403
FT /evidence="ECO:0000255"
FT COMPBIAS 425..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 55108 MW; 351075E06862955B CRC64;
MESVSKESYL PSFHQFPLCA SLSEFESASS KETQSSALKN ISPHPYDILQ APNSRALISA
LKTLQNKICR LESEKTHARD RLTNLSRAAG EHKKVLESEK RSAEWAAQEA TSQKNDVAMQ
LNNAEQRCSL LEKQLDYMRK MMENADIQNN PIHQIPAQKE QKDMLEMQSK LQKLEVLENE
CLRLKATHKS SENKIQFLEE KLSVEEQERK ALQDKAAQVQ TSLEVNRILL SSASSQNSTQ
RKVKKKKQSK QKNAISKEPS SKEPLSKEPP SKCFFPKAGE LPFVAGKSTT SSHSLSANVQ
NMLHMMKHQS PRVSQKDPKT VEHKPSILPG GSRSIPTRLM SSSTGDTLSD ILLALQDELG
QMSFEHQELL KHIDETKNTD MREDLERELD YLVKQMEIKS DQIIKLKRHQ LNVAKLKKTA
KKQPRPPSTT KPAEDEQNIG ATDPCTPRNK GNLANGTGTP NSKASLELLK SVRKIQMTLK
KDDIMWEK