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Database: UniProt
Entry: A1IMF0_CHICK
LinkDB: A1IMF0_CHICK
Original site: A1IMF0_CHICK 
ID   A1IMF0_CHICK            Unreviewed;       224 AA.
AC   A1IMF0; A0A1L1RQZ0; F1NIT5;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 115.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU361215};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU361215};
GN   Name=UCH-L1 {ECO:0000313|EMBL:CAF21961.1};
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 {ECO:0000313|EMBL:CAF21961.1};
RN   [1] {ECO:0000313|EMBL:CAF21961.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=White leghorn {ECO:0000313|EMBL:CAF21961.1};
RC   TISSUE=Neural retina {ECO:0000313|EMBL:CAF21961.1};
RA   Muhleisen T.W.;
RT   "Expression of deubiquitinating enzymes in the embryonic chicken retina.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000707,
CC         ECO:0000256|RuleBase:RU361215};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004628}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004628}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004635}.
CC   -!- SIMILARITY: Belongs to the peptidase C12 family.
CC       {ECO:0000256|ARBA:ARBA00009326, ECO:0000256|RuleBase:RU361215}.
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DR   EMBL; AJ621938; CAF21961.1; -; mRNA.
DR   RefSeq; NP_001073681.1; NM_001080212.1.
DR   AlphaFoldDB; A1IMF0; -.
DR   SMR; A1IMF0; -.
DR   STRING; 9031.ENSGALP00000061212; -.
DR   MEROPS; C12.001; -.
DR   PaxDb; 9031-ENSGALP00000023022; -.
DR   GeneID; 770302; -.
DR   KEGG; gga:770302; -.
DR   CTD; 7345; -.
DR   VEuPathDB; HostDB:geneid_770302; -.
DR   eggNOG; KOG1415; Eukaryota.
DR   HOGENOM; CLU_054406_2_0_1; -.
DR   InParanoid; A1IMF0; -.
DR   OMA; TCFVQAP; -.
DR   Reactome; R-GGA-5689603; UCH proteinases.
DR   Bgee; ENSGALG00000014261; Expressed in spermatid and 12 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd09616; Peptidase_C12_UCH_L1_L3; 1.
DR   Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001578; Peptidase_C12_UCH.
DR   InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR   PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR10589:SF19; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L1; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00140; UCH_1; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361215};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Prenylation {ECO:0000256|ARBA:ARBA00023289};
KW   Protease {ECO:0000256|RuleBase:RU361215};
KW   Thiol protease {ECO:0000256|RuleBase:RU361215};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU361215}.
FT   DOMAIN          84..100
FT                   /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT                   cysteine active-site"
FT                   /evidence="ECO:0000259|PROSITE:PS00140"
SQ   SEQUENCE   224 AA;  25111 MW;  3856F6A4BB177F63 CRC64;
     MAWQPMEINP EMLNKVLSRL GVSPGWRFVD VLGFEEEALG AVPSPACALL LLFPLTEQHE
     NFRKQQTEKI KDQEISSKVY FLKQTVSNSC GTIGLIHAVA NNKDKVKLDE GSALKKFLDE
     TADLSPEERA KRFANNKAIQ EVHNSVAQEG QCRVEDNSVN FHFILFANVD GHLYELDGRL
     PFPVNHGTSS DDLLLKDSAK ICRQFTEREK GEVRFSAVAF CKSA
//
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