MINY4_MOUSE
ID MINY4_MOUSE Reviewed; 744 AA.
AC Q3UQI9; Q8C472;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase MINDY-4;
DE EC=3.4.19.12;
DE AltName: Full=Probable deubiquitinating enzyme MINDY-4;
GN Name=Mindy4; Synonyms=Fam188b;
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=Lung;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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: Probable hydrolase that can remove 'Lys-48'-linked conjugated
CC ubiquitin from proteins. {ECO:0000250|UniProtKB:Q8NBR6}.
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:Q8NBR6};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UQI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UQI9-2; Sequence=VSP_031672;
CC -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM188
CC subfamily. {ECO:0000305}.
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DR EMBL; AK082855; BAC38655.1; -; mRNA.
DR EMBL; AK142385; BAE25052.1; -; mRNA.
DR CCDS; CCDS51782.1; -. [Q3UQI9-1]
DR RefSeq; NP_001136253.1; NM_001142781.1. [Q3UQI9-1]
DR RefSeq; NP_808551.2; NM_177883.4.
DR AlphaFoldDB; Q3UQI9; -.
DR BioGRID; 236942; 1.
DR STRING; 10090.ENSMUSP00000061221; -.
DR iPTMnet; Q3UQI9; -.
DR PhosphoSitePlus; Q3UQI9; -.
DR jPOST; Q3UQI9; -.
DR MaxQB; Q3UQI9; -.
DR PaxDb; Q3UQI9; -.
DR PRIDE; Q3UQI9; -.
DR ProteomicsDB; 252565; -. [Q3UQI9-1]
DR ProteomicsDB; 252566; -. [Q3UQI9-2]
DR Antibodypedia; 3440; 42 antibodies from 13 providers.
DR Ensembl; ENSMUST00000053094; ENSMUSP00000061221; ENSMUSG00000038022. [Q3UQI9-1]
DR GeneID; 330323; -.
DR KEGG; mmu:330323; -.
DR UCSC; uc009cao.1; mouse. [Q3UQI9-1]
DR CTD; 84182; -.
DR MGI; MGI:3583959; Mindy4.
DR VEuPathDB; HostDB:ENSMUSG00000038022; -.
DR eggNOG; KOG2871; Eukaryota.
DR GeneTree; ENSGT00940000159600; -.
DR HOGENOM; CLU_011769_1_0_1; -.
DR InParanoid; Q3UQI9; -.
DR OrthoDB; 1276386at2759; -.
DR PhylomeDB; Q3UQI9; -.
DR TreeFam; TF323996; -.
DR BioGRID-ORCS; 330323; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Fam188b; mouse.
DR PRO; PR:Q3UQI9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3UQI9; protein.
DR Bgee; ENSMUSG00000038022; Expressed in molar tooth and 115 other tissues.
DR ExpressionAtlas; Q3UQI9; baseline and differential.
DR Genevisible; Q3UQI9; MM.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IBA:GO_Central.
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.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..744
FT /note="Probable ubiquitin carboxyl-terminal hydrolase
FT MINDY-4"
FT /id="PRO_0000320591"
FT REGION 211..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 443
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT ACT_SITE 664
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0A6"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0A6"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0A6"
FT VAR_SEQ 506..744
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031672"
SQ SEQUENCE 744 AA; 82937 MW; 5AF10D14154B3241 CRC64;
MDSLYVEEVA ASLVREFLSR KGLNKTFVTM DQERPRCELS INSRNDLRKV LHLEFLYKEN
KAKEKPLRTN LELITRYFLD NVGNTDNSES QEVPIPAIPV PKKNNKLPLR HSETTLVNIY
DLSDEDTGRR TSWSEAGKAR HDSLDGDILG NFVSSKKPSH KSKAAHVDLG DSLPLVPAWE
KVDQLHSSEP GIDVKKTMER TRPKSGLIVR GMMAGPVASS PQDSFRKRSL RRSSALSRKL
QTPEEIQQQS EPFVHTPAYL GPQEVPDSSS DSVSRSPLGQ LNELSIEKPN VTSSSQGLSQ
RDRPRLRSVS EDSPLGYSHT EGNSRMAQDQ LERAFKRQGV QPPSLRKNQL VSDRTDDKPD
ALQLEDVEDE LIKEDIVLFP PPSMLKLQTV SKPIDLSLAK EIKTLLFGST FCCFSEEWKL
QNFSFNDIAS LKYGIVQNKG GPCGVLAAVQ GCVLQKLLFE GDNRTNSNLR LQPSDAQRTR
CLALAIADIL WRAGGKEQAV VALASGTPHF SPTGKYKADG VLETLTLYSL TSSEDLVTFI
QQSVHQFEAG PYGCILLTLS AILSRSLELV RQDFDVPTSH LIGAHGYCTQ ELVNLLLTGR
AVSNVFNDVV ELDSGDGNIT LLRGIEARSD IGFLSLFEHY NVCQVGCFLK TPRFPIWVVC
SESHFSILFS LQPELLCDWR SERLFDLYYY DGLANQQEEI RLTVDTTKTA PADSCSDLVP
PLELCIRTKW KGASVNWNGS DPIL
