CD37L_MOUSE
ID CD37L_MOUSE Reviewed; 335 AA.
AC Q9CZP7; Q3TNC7; Q8BP15; Q8C892; Q8C8X2; Q9CU15;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Hsp90 co-chaperone Cdc37-like 1;
GN Name=Cdc37l1;
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 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Embryo, Head, Hypothalamus, Kidney, Muellerian duct, and
RC Retina;
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=FVB/N; TISSUE=Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Co-chaperone that binds to numerous proteins and promotes
CC their interaction with Hsp70 and Hsp90. {ECO:0000250}.
CC -!- SUBUNIT: Self-associates. Forms complexes with Hsp70 and Hsp90.
CC Interacts with CDC37, FKBP4, PPID and STIP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9CZP7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CZP7-2; Sequence=VSP_031215, VSP_031216;
CC Name=3;
CC IsoId=Q9CZP7-3; Sequence=VSP_031214, VSP_031217;
CC Name=4;
CC IsoId=Q9CZP7-4; Sequence=VSP_031213, VSP_031218;
CC -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
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DR EMBL; AK012312; BAB28158.1; -; mRNA.
DR EMBL; AK018787; BAB31410.1; -; mRNA.
DR EMBL; AK044291; BAC31858.1; -; mRNA.
DR EMBL; AK048044; BAC33220.1; -; mRNA.
DR EMBL; AK078468; BAC37289.1; -; mRNA.
DR EMBL; AK079556; BAE43368.1; -; mRNA.
DR EMBL; AK165398; BAE38162.1; -; mRNA.
DR EMBL; BC031761; AAH31761.1; -; mRNA.
DR CCDS; CCDS29729.1; -. [Q9CZP7-1]
DR CCDS; CCDS89371.1; -. [Q9CZP7-2]
DR CCDS; CCDS89372.1; -. [Q9CZP7-4]
DR RefSeq; NP_001289309.1; NM_001302380.1. [Q9CZP7-4]
DR RefSeq; NP_001289311.1; NM_001302382.1. [Q9CZP7-2]
DR RefSeq; NP_001289372.1; NM_001302443.1.
DR RefSeq; NP_080226.1; NM_025950.3. [Q9CZP7-1]
DR AlphaFoldDB; Q9CZP7; -.
DR SMR; Q9CZP7; -.
DR BioGRID; 211919; 8.
DR STRING; 10090.ENSMUSP00000060421; -.
DR iPTMnet; Q9CZP7; -.
DR PhosphoSitePlus; Q9CZP7; -.
DR EPD; Q9CZP7; -.
DR MaxQB; Q9CZP7; -.
DR PaxDb; Q9CZP7; -.
DR PeptideAtlas; Q9CZP7; -.
DR PRIDE; Q9CZP7; -.
DR ProteomicsDB; 280019; -. [Q9CZP7-1]
DR ProteomicsDB; 280020; -. [Q9CZP7-2]
DR ProteomicsDB; 280021; -. [Q9CZP7-3]
DR ProteomicsDB; 280022; -. [Q9CZP7-4]
DR Antibodypedia; 24046; 206 antibodies from 29 providers.
DR DNASU; 67072; -.
DR Ensembl; ENSMUST00000050148; ENSMUSP00000060421; ENSMUSG00000024780. [Q9CZP7-1]
DR Ensembl; ENSMUST00000224511; ENSMUSP00000152985; ENSMUSG00000024780. [Q9CZP7-4]
DR Ensembl; ENSMUST00000225210; ENSMUSP00000153424; ENSMUSG00000024780. [Q9CZP7-3]
DR Ensembl; ENSMUST00000225310; ENSMUSP00000153192; ENSMUSG00000024780. [Q9CZP7-2]
DR GeneID; 67072; -.
DR KEGG; mmu:67072; -.
DR UCSC; uc008hcs.2; mouse. [Q9CZP7-1]
DR UCSC; uc008hct.2; mouse. [Q9CZP7-3]
DR UCSC; uc008hcu.2; mouse. [Q9CZP7-2]
DR UCSC; uc008hcw.2; mouse. [Q9CZP7-4]
DR CTD; 55664; -.
DR MGI; MGI:1914322; Cdc37l1.
DR VEuPathDB; HostDB:ENSMUSG00000024780; -.
DR eggNOG; KOG2260; Eukaryota.
DR GeneTree; ENSGT00390000013443; -.
DR HOGENOM; CLU_046495_1_0_1; -.
DR InParanoid; Q9CZP7; -.
DR OMA; GKWTKDD; -.
DR OrthoDB; 786744at2759; -.
DR PhylomeDB; Q9CZP7; -.
DR TreeFam; TF101059; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 67072; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Cdc37l1; mouse.
DR PRO; PR:Q9CZP7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9CZP7; protein.
DR Bgee; ENSMUSG00000024780; Expressed in interventricular septum and 248 other tissues.
DR ExpressionAtlas; Q9CZP7; baseline and differential.
DR Genevisible; Q9CZP7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR Gene3D; 1.20.58.610; -; 1.
DR InterPro; IPR004918; Cdc37.
DR InterPro; IPR013874; Cdc37_Hsp90-bd.
DR InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
DR PANTHER; PTHR12800; PTHR12800; 1.
DR Pfam; PF08565; CDC37_M; 1.
DR SMART; SM01070; CDC37_M; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..335
FT /note="Hsp90 co-chaperone Cdc37-like 1"
FT /id="PRO_0000318522"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..170
FT /note="Self-association"
FT /evidence="ECO:0000250"
FT REGION 147..276
FT /note="Self-association and interaction with Hsp90"
FT /evidence="ECO:0000250"
FT REGION 266..335
FT /note="Interaction with Hsp70"
FT /evidence="ECO:0000250"
FT REGION 277..335
FT /note="Required for interaction with STIP1"
FT /evidence="ECO:0000250"
FT COILED 84..120
FT /evidence="ECO:0000255"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L3B6"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L3B6"
FT VAR_SEQ 304..312
FT /note="NPDSLQCCT -> FSFLEAHRN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031213"
FT VAR_SEQ 304..310
FT /note="NPDSLQC -> VSWKRGY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031214"
FT VAR_SEQ 304..307
FT /note="NPDS -> APRF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031215"
FT VAR_SEQ 308..335
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031216"
FT VAR_SEQ 311..335
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031217"
FT VAR_SEQ 313..335
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031218"
FT CONFLICT 144
FT /note="D -> G (in Ref. 1; BAB31410)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 38439 MW; B487C836C22569E7 CRC64;
MEQPWPPPGP WSFPRTGGET EEESDLDVSP SSSHYSPVPD GGAQMYSHGI ELACQKQKEF
VKSSVACKWN LAEAQQKLGS LALHNSESLD QEHAKAQTAV SELRQREEEW RQKEEALVQR
ERMCLWNMDA ISKDVFNKSF INQDKRKTEE EDKSQSFMQK YEQKIRHFGM LSRWDDSQRF
LSDHPHLVCE ETAKYLILWC FHLEAEQKGA LMEQIAHQAV VMQFIMEMAK NCNVDPRGCF
RLFFQKAKAE EEGYFEAFKN ELEAFKSRVR LYAQSQSLQP VTVQNHVPHS GVGCIGSLES
LPQNPDSLQC CTPAPLCSVD SVVHKEDDDR MMDTV
