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   24-JAN-2024, entry version 103.
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; 10090-ENSMUSP00000061221; -.
DR   ProteomicsDB; 252565; -. [Q3UQI9-1]
DR   ProteomicsDB; 252566; -. [Q3UQI9-2]
DR   Pumba; Q3UQI9; -.
DR   Antibodypedia; 3440; 53 antibodies from 14 providers.
DR   Ensembl; ENSMUST00000053094.8; ENSMUSP00000061221.8; ENSMUSG00000038022.12. [Q3UQI9-1]
DR   GeneID; 330323; -.
DR   KEGG; mmu:330323; -.
DR   UCSC; uc009cao.1; mouse. [Q3UQI9-1]
DR   AGR; MGI:3583959; -.
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; 72090at2759; -.
DR   PhylomeDB; Q3UQI9; -.
DR   TreeFam; TF323996; -.
DR   BioGRID-ORCS; 330323; 5 hits in 77 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 118 other cell types or tissues.
DR   ExpressionAtlas; Q3UQI9; baseline and differential.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:1990380; F:K48-linked deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR025257; MINDY-3/4_CD.
DR   InterPro; IPR039785; MINY3/4.
DR   PANTHER; PTHR12473:SF13; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE MINDY-4-RELATED; 1.
DR   PANTHER; PTHR12473; UNCHARACTERIZED; 1.
DR   Pfam; PF13898; MINDY-3_4_CD; 1.
DR   SMART; SM01174; DUF4205; 1.
DR   Genevisible; Q3UQI9; MM.
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
//