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OTU1_CHICK
ID   OTU1_CHICK              Reviewed;         302 AA.
AC   Q5F3A6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Ubiquitin thioesterase OTU1;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6};
GN   Name=YOD1; ORFNames=RCJMB04_24h21;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC       and participates in endoplasmic reticulum-associated degradation (ERAD)
CC       for misfolded lumenal proteins. May act by triming the ubiquitin chain
CC       on the associated substrate to facilitate their threading through the
CC       VCP/p97 pore. Ubiquitin moieties on substrates may present a steric
CC       impediment to the threading process when the substrate is transferred
CC       to the VCP pore and threaded through VCP's axial channel. Mediates
CC       deubiquitination of 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked
CC       polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin
CC       chains. Cleaves both polyubiquitin and di-ubiquitin.
CC       {ECO:0000250|UniProtKB:Q5VVQ6}.
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:Q5VVQ6};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VVQ6}.
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DR   EMBL; AJ851744; CAH65378.1; -; mRNA.
DR   RefSeq; NP_001026670.1; NM_001031499.1.
DR   AlphaFoldDB; Q5F3A6; -.
DR   SMR; Q5F3A6; -.
DR   STRING; 9031.ENSGALP00000039556; -.
DR   MEROPS; C85.007; -.
DR   PaxDb; Q5F3A6; -.
DR   GeneID; 428266; -.
DR   KEGG; gga:428266; -.
DR   CTD; 55432; -.
DR   VEuPathDB; HostDB:geneid_428266; -.
DR   eggNOG; KOG3288; Eukaryota.
DR   InParanoid; Q5F3A6; -.
DR   OrthoDB; 1327072at2759; -.
DR   PhylomeDB; Q5F3A6; -.
DR   PRO; PR:Q5F3A6; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR   GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR   GO; GO:0035871; P:protein K11-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:1990167; P:protein K27-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0035523; P:protein K29-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:1990168; P:protein K33-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR   InterPro; IPR039138; OTU1_2_3.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR13312; PTHR13312; 1.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50802; OTU; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Metal-binding; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway; Unfolded protein response; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..302
FT                   /note="Ubiquitin thioesterase OTU1"
FT                   /id="PRO_0000282359"
FT   DOMAIN          103..228
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   ZN_FING         272..296
FT                   /note="C2H2-type"
FT   REGION          5..83
FT                   /note="UBX-like"
FT   REGION          108..114
FT                   /note="Cys-loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          167..177
FT                   /note="Variable-loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          217..221
FT                   /note="His-loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   REGION          245..250
FT                   /note="S2 site"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   ACT_SITE        114
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        221
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
SQ   SEQUENCE   302 AA;  33384 MW;  6ABA3C65C985248C CRC64;
     MLRLRCKARS GTQPLPGLTA HSRLRDMQAA LAALTGVPAP AQRLLLGFPP RSLDLSDGER
     RLGELGIHSG DTLIVEEDTS KPSAGSPVVA KRTMAVREAV PVLARRVVPA DNSCLFTSVY
     YVVEGGVYDP GCAPEMRSLI AQIVASDPEA YCEAVLGKTN REYCEWIRRE ETWGGAIEVS
     ILSKFYQCEI CVVDTQTVRI DRFGEDAGYT KRVLLIYDGI HYDPLERKIP DSDVPPQTIF
     STTDDVVLAQ ALELADEARR KRQFTDVNRF TLRCMVCQKG LTGQVEAREH AKETGHTNFG
     EV
 
 
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