MINY3_MOUSE
ID MINY3_MOUSE Reviewed; 444 AA.
AC Q9CV28; Q3UPS0; Q9DCC9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase MINDY-3 {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q9H8M7};
DE AltName: Full=Deubiquitinating enzyme MINDY-3 {ECO:0000250|UniProtKB:Q9H8M7};
DE AltName: Full=MINDY lysine 48 deubiquitinase 3 {ECO:0000312|MGI:MGI:1914210};
DE AltName: Full=Protein CARP {ECO:0000250|UniProtKB:Q9H8M7};
GN Name=Mindy3 {ECO:0000312|MGI:MGI:1914210};
GN Synonyms=Carp {ECO:0000250|UniProtKB:Q9H8M7},
GN Fam188a {ECO:0000312|MGI:MGI:1914210};
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 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and 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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, Spleen, 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: Hydrolase that can remove 'Lys-48'-linked conjugated
CC ubiquitin from proteins. {ECO:0000250|UniProtKB:Q9H8M7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q9H8M7};
CC -!- SUBUNIT: Interacts with COPS5. {ECO:0000250|UniProtKB:Q9H8M7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H8M7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CV28-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CV28-2; Sequence=VSP_031041;
CC -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM188
CC subfamily. {ECO:0000305}.
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DR EMBL; AK002900; BAB22443.1; -; mRNA.
DR EMBL; AK009891; BAB26566.2; -; mRNA.
DR EMBL; AK143250; BAE25325.1; -; mRNA.
DR EMBL; AL772342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027202; AAH27202.1; -; mRNA.
DR CCDS; CCDS15690.1; -. [Q9CV28-1]
DR RefSeq; NP_077147.2; NM_024185.4. [Q9CV28-1]
DR AlphaFoldDB; Q9CV28; -.
DR STRING; 10090.ENSMUSP00000028105; -.
DR iPTMnet; Q9CV28; -.
DR PhosphoSitePlus; Q9CV28; -.
DR EPD; Q9CV28; -.
DR jPOST; Q9CV28; -.
DR MaxQB; Q9CV28; -.
DR PaxDb; Q9CV28; -.
DR PeptideAtlas; Q9CV28; -.
DR PRIDE; Q9CV28; -.
DR ProteomicsDB; 295610; -. [Q9CV28-1]
DR ProteomicsDB; 295611; -. [Q9CV28-2]
DR Antibodypedia; 25119; 44 antibodies from 16 providers.
DR Ensembl; ENSMUST00000028105; ENSMUSP00000028105; ENSMUSG00000026767. [Q9CV28-1]
DR GeneID; 66960; -.
DR KEGG; mmu:66960; -.
DR UCSC; uc008ijn.1; mouse. [Q9CV28-1]
DR UCSC; uc008ijs.1; mouse. [Q9CV28-2]
DR CTD; 80013; -.
DR MGI; MGI:1914210; Mindy3.
DR VEuPathDB; HostDB:ENSMUSG00000026767; -.
DR eggNOG; KOG2871; Eukaryota.
DR GeneTree; ENSGT00940000155958; -.
DR HOGENOM; CLU_033478_0_0_1; -.
DR InParanoid; Q9CV28; -.
DR OMA; HVWDHDQ; -.
DR OrthoDB; 1276386at2759; -.
DR PhylomeDB; Q9CV28; -.
DR TreeFam; TF323996; -.
DR BioGRID-ORCS; 66960; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Car8; mouse.
DR PRO; PR:Q9CV28; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CV28; protein.
DR Bgee; ENSMUSG00000026767; Expressed in dorsal pancreas and 256 other tissues.
DR ExpressionAtlas; Q9CV28; baseline and differential.
DR Genevisible; Q9CV28; MM.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISO:MGI.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR025257; MINDY-3/4_CD.
DR InterPro; IPR039785; MINY3/4.
DR PANTHER; PTHR12473; PTHR12473; 1.
DR Pfam; PF13898; DUF4205; 1.
DR SMART; SM01174; DUF4205; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Hydrolase; Nucleus; Phosphoprotein;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..444
FT /note="Ubiquitin carboxyl-terminal hydrolase MINDY-3"
FT /id="PRO_0000317562"
FT ACT_SITE 51
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 342..444
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031041"
SQ SEQUENCE 444 AA; 49612 MW; 02D382FAEB3D6167 CRC64;
MSEVTKELLE LVWGTKSSPG LSDTIFCRWT QGFVFSESEG SALEQFEGGP CAVIAPVQAF
LLKKLLFSSE KSSWRDCSEE EQKELLCHTL CDIVESAYDS SGSYCLVSWL RGRTPEEAAR
ISGSPAQSSC QVEHSSALAV EELGFERFHA LIQKRSFRTV SELKDAVLDQ YSMWGNKFGV
LLFLYSVLLT KGIENIKNSI EDANEPLIDP VYGHGSQSLI NLLLTGHAVS NVWDGDRECS
GMQLLGIHEQ AAVGFLTLME ALRYCKVGSY LKSPKFPIWI VGSETHLTVF FAKDMALVAP
EAPSEQARRV FQTYDPEDNG FIADSLLEDV MKALDLVSDP EYINLMKNKL DPEGLGIILL
GPFLQEFFPD QGSSGPESFT VYHYNGLKQS NYNEKVMYVE GTAVVMGFED PMLQTDDTPI
KRCLQTKWPY IELLWTTDRC PSLN
