CE57L_MOUSE
ID CE57L_MOUSE Reviewed; 400 AA.
AC Q8VDS7; Q9CZE0; Q9D5A1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Centrosomal protein CEP57L1;
DE AltName: Full=Centrosomal protein 57kDa-like protein 1;
DE AltName: Full=Centrosomal protein of 57 kDa-related protein;
DE Short=Cep57R;
DE AltName: Full=Cep57-related protein;
GN Name=Cep57l1; Synonyms=Cep57r;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: Centrosomal protein which may be required for microtubule
CC attachment to centrosomes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VDS7-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VDS7-1; Sequence=VSP_013897, VSP_013898;
CC Name=3;
CC IsoId=Q8VDS7-2; Sequence=VSP_013899, VSP_013900;
CC -!- SIMILARITY: Belongs to the translokin family. {ECO:0000305}.
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DR EMBL; AK012710; BAB28426.1; -; mRNA.
DR EMBL; AK015619; BAB29907.1; -; mRNA.
DR EMBL; BC021375; AAH21375.1; -; mRNA.
DR CCDS; CCDS23808.1; -. [Q8VDS7-3]
DR RefSeq; NP_001230003.1; NM_001243074.1.
DR RefSeq; NP_001230004.1; NM_001243075.1.
DR AlphaFoldDB; Q8VDS7; -.
DR SMR; Q8VDS7; -.
DR BioGRID; 222050; 4.
DR PhosphoSitePlus; Q8VDS7; -.
DR EPD; Q8VDS7; -.
DR MaxQB; Q8VDS7; -.
DR PRIDE; Q8VDS7; -.
DR ProteomicsDB; 281450; -. [Q8VDS7-3]
DR ProteomicsDB; 281451; -. [Q8VDS7-1]
DR ProteomicsDB; 281452; -. [Q8VDS7-2]
DR GeneID; 103268; -.
DR KEGG; mmu:103268; -.
DR UCSC; uc007eya.2; mouse. [Q8VDS7-1]
DR CTD; 285753; -.
DR MGI; MGI:1915511; Cep57l1.
DR eggNOG; ENOG502QTVF; Eukaryota.
DR InParanoid; Q8VDS7; -.
DR PhylomeDB; Q8VDS7; -.
DR BioGRID-ORCS; 103268; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Cep57l1; mouse.
DR PRO; PR:Q8VDS7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VDS7; protein.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..400
FT /note="Centrosomal protein CEP57L1"
FT /id="PRO_0000189535"
FT REGION 222..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..111
FT /evidence="ECO:0000255"
FT COILED 138..213
FT /evidence="ECO:0000255"
FT COILED 261..345
FT /evidence="ECO:0000255"
FT COMPBIAS 222..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYX8"
FT VAR_SEQ 50..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013897"
FT VAR_SEQ 215
FT /note="E -> ELQTGFEISKILMSTVSNSKHCKEKKKQPK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013898"
FT VAR_SEQ 216..256
FT /note="KTNCLKREPPQQRDHKFRTPTFERKKPFRTTSQARANPQSS -> LQTGFEI
FT SKILMSTVSNSKHCKEKKKQPKVYYIQLIPDITS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013899"
FT VAR_SEQ 257..400
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013900"
FT CONFLICT 291
FT /note="T -> M (in Ref. 1; BAB28426)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 46790 MW; E0EE017BE1310C66 CRC64;
MDSELSQSMV GSYLNPPERM HLPSFTQNEA FQNCHPGTPP KMFNSPNNQA LVSALKTLQE
KIRRLELERT QAEDNLNLLS REAAQYKKAL EEETNERNLA HQELIKQKKD ISIQLSSAQS
RCILLEKQLE YTKRMVLNVE REKTMILEQQ AQLQREKEQD QMKLHAKLEK LHVLEKECLR
LTATRQTAED KIKCLEEKLK EEEHQRRLFQ DRACEKTNCL KREPPQQRDH KFRTPTFERK
KPFRTTSQAR ANPQSSGEPV SICDSLSELL MTMEEELDQM NMEHRELLRQ TMQPGNHSVS
EDIEQELEQL AKKMESKGDQ ISKLKKHQDS VRKLQEKIEN SRINESSGIH GNPKGSKNLK
TSPRKCVSET SSFQRDRGFQ PVQVHSLQSK LRRDDIKWEQ
