ID G1NTZ2_MYOLU Unreviewed; 537 AA.
AC G1NTZ2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU367139};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU367139};
GN Name=MINDY2 {ECO:0000313|Ensembl:ENSMLUP00000000667.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000000667.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000000667.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000000667.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Hydrolase that can specifically remove 'Lys-48'-linked
CC conjugated ubiquitin from proteins. Has exodeubiquitinase activity and
CC has a preference for long polyubiquitin chains. May play a regulatory
CC role at the level of protein turnover. {ECO:0000256|RuleBase:RU367139}.
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:0000256|RuleBase:RU367139};
CC -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM63
CC subfamily. {ECO:0000256|ARBA:ARBA00006616,
CC ECO:0000256|RuleBase:RU367139}.
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DR EMBL; AAPE02011458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02011459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02011460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1NTZ2; -.
DR STRING; 59463.ENSMLUP00000000667; -.
DR Ensembl; ENSMLUT00000000732.2; ENSMLUP00000000667.2; ENSMLUG00000000733.2.
DR eggNOG; KOG2427; Eukaryota.
DR GeneTree; ENSGT00390000016607; -.
DR HOGENOM; CLU_022566_3_0_1; -.
DR InParanoid; G1NTZ2; -.
DR OMA; THLCPDN; -.
DR TreeFam; TF314589; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0016807; F:cysteine-type carboxypeptidase activity; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0140934; F:histone deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071795; F:K11-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:1990380; F:K48-linked deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071796; F:K6-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR007518; MINDY.
DR InterPro; IPR033979; MINDY_domain.
DR PANTHER; PTHR18063; NF-E2 INDUCIBLE PROTEIN; 1.
DR PANTHER; PTHR18063:SF8; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE MINDY-2; 1.
DR Pfam; PF04424; MINDY_DUB; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU367139};
KW Protease {ECO:0000256|RuleBase:RU367139};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Thiol protease {ECO:0000256|RuleBase:RU367139};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU367139}.
FT DOMAIN 187..309
FT /note="MINDY deubiquitinase"
FT /evidence="ECO:0000259|Pfam:PF04424"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 59908 MW; 05011D1FED828A70 CRC64;
KDLANSSTSA QKVPLRGQPK VTASPETAEG GAGQGLGAAG DAGAGPDPRA PREPSSAGRP
QQQLQRPEPL PGNRRAWTSE SFFYLHSFPV TSDLIMEKEL RSRVPEEEEE GEGEGKRGAA
AVLPGAVPLC RGEEEEEGEA AQVLAASKER FPGQSVYHIK WIQWKEEHTP IITQNENGPC
PLLAILNVLL LAWKVKLPPM MEIITAEQLM EYLGDYMLDA KPKEISEIQR LNYEQNMSDA
MAILHKLQTG LDVNVKFTGV RVFEYTPECI VFDLLDIPLY HGWLVDPQVD DIVKAVGNCS
YNQLVEKIIS CKQSDNSELV SEGFVAEQFL NNTATQLTYH GLCELTSTVQ EGELCVFFRN
NHFSTMTKYK GLLYLLVTDQ GFLTEEKIVW ESLHNVDGDG NFCDSDFHLR PPSDPETVYR
GQQDQIDQDY LMALSLQQEQ QSQEINWEQA PEGISDLELA KKLQEEEDRR ASQYYQEQEQ
AAVAAASTSA STQAQQSQPA QASPSSGRQS GNSERKRKEP REKDKEKEKE KNSCVIL
//
