位置:首页 > 蛋白库 > UCHL1_MACFA
UCHL1_MACFA
ID   UCHL1_MACFA             Reviewed;         223 AA.
AC   Q60HC8;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L1;
DE            Short=UCH-L1;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:P09936};
DE   AltName: Full=Ubiquitin thioesterase L1;
DE   Flags: Precursor;
GN   Name=UCHL1; ORFNames=QccE-15749;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological disease
RT   genes.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=15664418; DOI=10.1016/j.placenta.2004.05.007;
RA   Sekiguchi S., Takatori A., Negishi T., Kwon J., Kokubo T., Ishii Y.,
RA   Kyuwa S., Yoshikawa Y.;
RT   "Localization of ubiquitin carboxyl-terminal hydrolase-L1 in cynomolgus
RT   monkey placentas.";
RL   Placenta 26:99-103(2005).
CC   -!- FUNCTION: Ubiquitin-protein hydrolase involved both in the processing
CC       of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a
CC       thiol protease that recognizes and hydrolyzes a peptide bond at the C-
CC       terminal glycine of ubiquitin (By similarity). Also binds to free
CC       monoubiquitin and may prevent its degradation in lysosomes (By
CC       similarity). The homodimer may have ATP-independent ubiquitin ligase
CC       activity (By similarity). {ECO:0000250|UniProtKB:P09936,
CC       ECO:0000250|UniProtKB:Q9R0P9}.
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:P09936};
CC   -!- SUBUNIT: Monomer. Homodimer. Interacts with COPS5 and SNCA (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum
CC       membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=Found both cytoplasmic and nuclear in
CC       cytotrophoblasts and decidual cells. {ECO:0000269|PubMed:15664418}.
CC   -!- TISSUE SPECIFICITY: Expressed in the placenta at all stages of
CC       pregnancy. Expression increases as pregnancy progresses.
CC       {ECO:0000269|PubMed:15664418}.
CC   -!- PTM: O-glycosylated. {ECO:0000250}.
CC   -!- MISCELLANEOUS: In contrast to UCHL3, does not hydrolyze a peptide bond
CC       at the C-terminal glycine of NEDD8. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
CC   -!- CAUTION: The homodimer may have ATP-independent ubiquitin ligase
CC       activity. However, in another study, UCHL1 was shown to lack ubiquitin
CC       ligase activity. {ECO:0000250|UniProtKB:P09936}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB125199; BAD51987.1; -; mRNA.
DR   AlphaFoldDB; Q60HC8; -.
DR   BMRB; Q60HC8; -.
DR   SMR; Q60HC8; -.
DR   STRING; 9541.XP_005554811.1; -.
DR   MEROPS; C12.001; -.
DR   eggNOG; KOG1415; Eukaryota.
DR   BRENDA; 3.4.19.12; 1793.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.532.10; -; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001578; Peptidase_C12_UCH.
DR   InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR   InterPro; IPR030297; UCHL1.
DR   PANTHER; PTHR10589; PTHR10589; 1.
DR   PANTHER; PTHR10589:SF19; PTHR10589:SF19; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00140; UCH_1; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipoprotein;
KW   Membrane; Nucleus; Phosphoprotein; Prenylation; Protease;
KW   Reference proteome; Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..220
FT                   /note="Ubiquitin carboxyl-terminal hydrolase isozyme L1"
FT                   /id="PRO_0000211056"
FT   PROPEP          221..223
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000414312"
FT   REGION          5..10
FT                   /note="Interaction with ubiquitin"
FT                   /evidence="ECO:0000250|UniProtKB:P09936"
FT   REGION          211..216
FT                   /note="Interaction with ubiquitin"
FT                   /evidence="ECO:0000250|UniProtKB:P09936"
FT   ACT_SITE        90
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10091"
FT   ACT_SITE        161
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10091"
FT   SITE            176
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00981"
FT   LIPID           220
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P09936"
SQ   SEQUENCE   223 AA;  24752 MW;  CB15EDCD56B5D03B CRC64;
     MQLKPMEINP EMLNKVLSRL GVAGQWRFVD VLGLEEDSLG SVPAPACALL LLFPLTAQHE
     NFRKKQIEEL KGQEVSPKVY FMKQTIGNSC GTIGLIHAVA NNQDKLGFED GSVLKQFLSE
     TEKMSPEDRA KCFEKNEAIQ AAHDAVAQEG QCRVDDKVNF HFILFNNVDG HLYELDGRMP
     FPVNHGASSE GTLLQDAAKV CREFTEREQG EVRFSAVALC KAA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024