CMBL_MOUSE
ID CMBL_MOUSE Reviewed; 245 AA.
AC Q8R1G2; Q8C1N1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Carboxymethylenebutenolidase homolog;
DE EC=3.1.-.-;
GN Name=Cmbl;
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].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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].
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, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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: Cysteine hydrolase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dienelactone hydrolase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25255.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK009374; BAC25255.1; ALT_FRAME; mRNA.
DR EMBL; BC024580; AAH24580.1; -; mRNA.
DR CCDS; CCDS27410.1; -.
DR RefSeq; NP_853619.1; NM_181588.3.
DR RefSeq; XP_006520239.1; XM_006520176.2.
DR RefSeq; XP_006520240.1; XM_006520177.3.
DR AlphaFoldDB; Q8R1G2; -.
DR SMR; Q8R1G2; -.
DR BioGRID; 213542; 6.
DR STRING; 10090.ENSMUSP00000070314; -.
DR ESTHER; mouse-CMBL; CMBL.
DR iPTMnet; Q8R1G2; -.
DR PhosphoSitePlus; Q8R1G2; -.
DR SwissPalm; Q8R1G2; -.
DR jPOST; Q8R1G2; -.
DR MaxQB; Q8R1G2; -.
DR PaxDb; Q8R1G2; -.
DR PeptideAtlas; Q8R1G2; -.
DR PRIDE; Q8R1G2; -.
DR ProteomicsDB; 283388; -.
DR Antibodypedia; 22459; 130 antibodies from 20 providers.
DR DNASU; 69574; -.
DR Ensembl; ENSMUST00000070918; ENSMUSP00000070314; ENSMUSG00000022235.
DR GeneID; 69574; -.
DR KEGG; mmu:69574; -.
DR UCSC; uc007vki.1; mouse.
DR CTD; 134147; -.
DR MGI; MGI:1916824; Cmbl.
DR VEuPathDB; HostDB:ENSMUSG00000022235; -.
DR eggNOG; KOG3043; Eukaryota.
DR GeneTree; ENSGT00390000000183; -.
DR HOGENOM; CLU_054590_8_2_1; -.
DR InParanoid; Q8R1G2; -.
DR OMA; HIKAYVV; -.
DR OrthoDB; 1275897at2759; -.
DR PhylomeDB; Q8R1G2; -.
DR TreeFam; TF331795; -.
DR BRENDA; 3.1.1.45; 3474.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR BioGRID-ORCS; 69574; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q8R1G2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8R1G2; protein.
DR Bgee; ENSMUSG00000022235; Expressed in right kidney and 214 other tissues.
DR ExpressionAtlas; Q8R1G2; baseline and differential.
DR Genevisible; Q8R1G2; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR042946; CMBL.
DR InterPro; IPR002925; Dienelactn_hydro.
DR PANTHER; PTHR46812; PTHR46812; 1.
DR Pfam; PF01738; DLH; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96DG6"
FT CHAIN 2..245
FT /note="Carboxymethylenebutenolidase homolog"
FT /id="PRO_0000308189"
FT ACT_SITE 132
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /evidence="ECO:0000250"
FT ACT_SITE 212
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96DG6"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96DG6"
FT CONFLICT 40
FT /note="D -> V (in Ref. 1; BAC25255)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="D -> V (in Ref. 1; BAC25255)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="K -> I (in Ref. 1; BAC25255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 27902 MW; 188DF4689A08F543 CRC64;
MANEANPCPC DIGHKLEYGG MGHEVQVEHI KAYVTRSPVD AGKAVIVVQD IFGWQLPNTR
YMADMIARNG YTTIVPDFFV GQEPWDPAGD WSTFPAWLKS RNARKVNREV DAVLRYLRQQ
CHAQKIGIVG FCWGGVVVHQ VMTAYPDIRA GVSVYGIIRD SEDVYNLKNP TLFIFAENDT
VIPLEQVSTL TQKLKEHCIV NYQVKTFSGQ THGFVHRKRE DCSPADKPYI EEARRNLIEW
LNKYV
