ID K7FQZ0_PELSI Unreviewed; 448 AA.
AC K7FQZ0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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:ENSPSIP00000010450.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000010450.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000010450.1}
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; AGCU01015063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01015064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01015065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01015066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01015067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01015068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01015069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01015070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01015071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7FQZ0; -.
DR STRING; 13735.ENSPSIP00000010450; -.
DR Ensembl; ENSPSIT00000010503.1; ENSPSIP00000010450.1; ENSPSIG00000009432.1.
DR eggNOG; KOG2427; Eukaryota.
DR GeneTree; ENSGT00390000016607; -.
DR HOGENOM; CLU_022566_5_0_1; -.
DR OMA; THLCPDN; -.
DR TreeFam; TF314589; -.
DR Proteomes; UP000007267; 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:UP000007267};
KW Thiol protease {ECO:0000256|RuleBase:RU367139};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU367139}.
FT DOMAIN 100..223
FT /note="MINDY deubiquitinase"
FT /evidence="ECO:0000259|Pfam:PF04424"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 50506 MW; 8D11F76DC7CB2571 CRC64;
SSGDPSPPEE ESRSLDSLES FSNLHSCCPS SSELNSDAEE AAAPAAEDKA LAPGAQLLSA
GKERFPGQSV YHIKWVRWKE ENTPIITQNE NGPCPLLAIM NVLLLAWKVK LPPMMEIITA
EQLMEYLGDY ILDAKPKEIS EIQRLNYEQN MSDAMAILHK LQTGLDVNVK FTGVRVFEYT
PECIVFDLLD IPLYHGWLVD PQIADIVKAV GNCSYNQLVE KIICCKQSDN SELVSEGFVA
EQFLNNTATQ LTYHGLCELT SAVQEGELCV FFRNNHFSTM TKYKGQLYLL VTDQGFLTEE
KVVWESLHNV DGDGNFCDSE FHLRPPSDPE TVYRGQQDQI DQDYLMALSL QQEQQSQDIN
WEQIPEGISD LELAKKLQEE EDRRASQYYQ EQEQAVAAAA QVQSFFQQVQ GAASPASGKQ
SGSSERKRKE PREKEREKEK EKNSCIIL
//
