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MINY3_DANRE
ID   MINY3_DANRE             Reviewed;         446 AA.
AC   A0AUR5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase MINDY-3;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme MINDY-3;
DE   AltName: Full=Protein CARP;
GN   Name=mindy3; Synonyms=carp, fam188a; ORFNames=zgc:153892;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H8M7}.
CC   -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM188
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC124766; AAI24767.1; -; mRNA.
DR   RefSeq; NP_001071224.1; NM_001077756.1.
DR   AlphaFoldDB; A0AUR5; -.
DR   STRING; 7955.ENSDARP00000059034; -.
DR   PaxDb; A0AUR5; -.
DR   PeptideAtlas; A0AUR5; -.
DR   Ensembl; ENSDART00000059035; ENSDARP00000059034; ENSDARG00000028715.
DR   GeneID; 777708; -.
DR   KEGG; dre:777708; -.
DR   CTD; 80013; -.
DR   ZFIN; ZDB-GENE-061110-13; mindy3.
DR   eggNOG; KOG2871; Eukaryota.
DR   GeneTree; ENSGT00940000155958; -.
DR   HOGENOM; CLU_033478_0_0_1; -.
DR   InParanoid; A0AUR5; -.
DR   OMA; HVWDHDQ; -.
DR   OrthoDB; 1276386at2759; -.
DR   PhylomeDB; A0AUR5; -.
DR   TreeFam; TF323996; -.
DR   PRO; PR:A0AUR5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 16.
DR   Bgee; ENSDARG00000028715; Expressed in testis and 27 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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   2: Evidence at transcript level;
KW   Apoptosis; Hydrolase; Nucleus; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..446
FT                   /note="Ubiquitin carboxyl-terminal hydrolase MINDY-3"
FT                   /id="PRO_0000317563"
FT   REGION          117..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        51
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT   ACT_SITE        288
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5J2"
SQ   SEQUENCE   446 AA;  50111 MW;  379F0E55AF0D8B29 CRC64;
     MSDTNKEVVD LVWGRPSGGG VPASLFRRWS QGFVFSETER SALEQFEGGP CAVIAPVQAF
     LLKNILFNTE GLNWKDISEE EQRTVLCSTL SEILELACLN KSQAFHLVTW PHAKTTDNSD
     ITDSHPEPES SQPTDTPTAL ATEELGFERF HSVIQKRTLR TVAELKEAVL SLYDTWKNKF
     GVLLFLYSVI LTKGIENIKN EIEDTTEPLI DPVYGHGSQS LINLLVTGHA VSNVWDGDRE
     CSGMKLHGIY QQASVGFLTL MESLRYCKVG AFLKSPKFPI WILGSETHLS VFFTKEMALV
     APESASEQAR RVFQTFDPED NGFIPDTLLE DVMKALDLVS EPDYVNLMKS KLDPEGLGII
     LLGQFLLEFF PDQDSVIPDS FPVYHYNGLK QSNHNEKVSY VEGTALVMGF EDPMVRTDDT
     PVKRCLQTKW PYIELLWTTE RSPSLN
 
 
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