BRC3L_MOUSE
ID BRC3L_MOUSE Reviewed; 291 AA.
AC Q7M757; Q3UY45;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Lys-63-specific deubiquitinase BRCC36-like;
DE EC=3.4.19.-;
GN Name=C6.1al; Synonyms=Gm5136;
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 TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 135-291.
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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 [3]
RP IDENTIFICATION.
RX PubMed=12838346; DOI=10.1038/nrg1111;
RA Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.;
RT "Human and mouse proteases: a comparative genomic approach.";
RL Nat. Rev. Genet. 4:544-558(2003).
CC -!- FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked
CC polyubiquitin chains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. BRCC36 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC120506; AAI20507.1; -; mRNA.
DR EMBL; BC120508; AAI20509.1; -; mRNA.
DR EMBL; AK134982; BAE22368.1; -; mRNA.
DR EMBL; BN000130; CAD67592.1; -; mRNA.
DR CCDS; CCDS88084.1; -.
DR RefSeq; NP_988991.1; NM_203660.2.
DR AlphaFoldDB; Q7M757; -.
DR SMR; Q7M757; -.
DR MEROPS; M67.007; -.
DR iPTMnet; Q7M757; -.
DR PhosphoSitePlus; Q7M757; -.
DR MaxQB; Q7M757; -.
DR PRIDE; Q7M757; -.
DR ProteomicsDB; 273699; -.
DR DNASU; 368203; -.
DR Ensembl; ENSMUST00000218023; ENSMUSP00000151516; ENSMUSG00000112039.
DR GeneID; 368203; -.
DR KEGG; mmu:368203; -.
DR UCSC; uc007gzj.2; mouse.
DR MGI; MGI:3647286; Gm5136.
DR VEuPathDB; HostDB:ENSMUSG00000112039; -.
DR GeneTree; ENSGT00390000000360; -.
DR InParanoid; Q7M757; -.
DR OMA; FACFIED; -.
DR OrthoDB; 968461at2759; -.
DR PhylomeDB; Q7M757; -.
DR BioGRID-ORCS; 368203; 0 hits in 10 CRISPR screens.
DR PRO; PR:Q7M757; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q7M757; protein.
DR Bgee; ENSMUSG00000112039; Expressed in spermatocyte and 7 other tissues.
DR GO; GO:0070531; C:BRCA1-A complex; ISS:UniProtKB.
DR GO; GO:0070552; C:BRISC complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; ISS:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0070537; P:histone H2A K63-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR CDD; cd08068; MPN_BRCC36; 1.
DR InterPro; IPR040749; BRCC36_C.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR033860; MPN_BRCC36.
DR Pfam; PF18110; BRCC36_C; 1.
DR Pfam; PF01398; JAB; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..291
FT /note="Lys-63-specific deubiquitinase BRCC36-like"
FT /id="PRO_0000373951"
FT DOMAIN 12..179
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 122..135
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 291 AA; 33079 MW; F45CC0496EDC0130 CRC64;
MAVRMMQGVQ AVYLESDAFL VCLNHALSTE KEEVMGLCIG QLNDHGRSDS RLAYAGAEMC
TVAKKMEATR IVHIHSVIIL RRSDKTKDRV EISPEQLSAA SIEAERLAEQ TGRPMRVVGW
YHSHPHITVW PSHVDVRTQA MYQMMDQSFV GLIFACFIED KPTKIGRVLY TCFQSVQASK
SSEYERLEIP IHIVPRTTIG TVCLRSAIEL PGILCQEEQE AYRRIHGLTH LDSVTKIHNG
SVFTKHLCSQ MSAVCGPLLQ WLEDRLEQNQ QRLQELEQEK EDLMEELSSL E
