UBP14_RABIT
ID UBP14_RABIT Reviewed; 493 AA.
AC P40826;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 14;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 14;
DE AltName: Full=Ubiquitin thioesterase 14;
DE AltName: Full=Ubiquitin-specific-processing protease 14;
GN Name=USP14; Synonyms=TGT;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=8579355; DOI=10.1006/abbi.1996.0039;
RA Deshpande K.L., Seubert P.H., Tillman D.M., Farkas W.R., Katze J.R.;
RT "Cloning and characterization of cDNA encoding the rabbit tRNA-guanine
RT transglycosylase 60-kilodalton subunit.";
RL Arch. Biochem. Biophys. 326:1-7(1996).
CC -!- FUNCTION: Proteasome-associated deubiquitinase which releases ubiquitin
CC from the proteasome targeted ubiquitinated proteins. Ensures the
CC regeneration of ubiquitin at the proteasome. Is a reversibly associated
CC subunit of the proteasome and a large fraction of proteasome-free
CC protein exists within the cell. Required for the degradation of the
CC chemokine receptor CXCR4 which is critical for CXCL12-induced cell
CC chemotaxis. Serves also as a physiological inhibitor of endoplasmic
CC reticulum-associated degradation (ERAD) under the non-stressed
CC condition by inhibiting the degradation of unfolded endoplasmic
CC reticulum proteins via interaction with ERN1 (By similarity).
CC Indispensable for synaptic development and function at neuromuscular
CC junctions (NMJs) (By similarity). Plays a role in the innate immune
CC defense against viruses by stabilizing the viral DNA sensor CGAS and
CC thus inhibiting its autophagic degradation (By similarity).
CC {ECO:0000250|UniProtKB:P54578, ECO:0000250|UniProtKB:Q9JMA1}.
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;
CC -!- SUBUNIT: Homodimer (Potential). Associates with the 26S proteasome.
CC Interacts with FANCC, CXCR4 and ERN1. Interacts with TRIM14; this
CC interaction recruits USP14 to cleave ubiquitin chains of CGAS (By
CC similarity). {ECO:0000250|UniProtKB:P54578}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP14/UBP6 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a guanine tRNA-
CC ribosyltransferase. {ECO:0000305|PubMed:8579355}.
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DR EMBL; L37420; AAA96133.1; -; mRNA.
DR PIR; S68430; S68430.
DR RefSeq; NP_001075726.1; NM_001082257.1.
DR AlphaFoldDB; P40826; -.
DR SMR; P40826; -.
DR STRING; 9986.ENSOCUP00000015687; -.
DR MEROPS; C19.015; -.
DR Ensembl; ENSOCUT00000029186; ENSOCUP00000015687; ENSOCUG00000011595.
DR GeneID; 100009078; -.
DR KEGG; ocu:100009078; -.
DR CTD; 9097; -.
DR eggNOG; KOG1872; Eukaryota.
DR GeneTree; ENSGT00390000009615; -.
DR HOGENOM; CLU_017549_2_1_1; -.
DR InParanoid; P40826; -.
DR OMA; MCKGGIL; -.
DR OrthoDB; 600543at2759; -.
DR TreeFam; TF314494; -.
DR Proteomes; UP000001811; Chromosome 9.
DR Bgee; ENSOCUG00000011595; Expressed in blood and 16 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR044635; UBP14-like.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR43982; PTHR43982; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Immunity; Innate immunity; Membrane; Phosphoprotein; Protease;
KW Proteasome; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..493
FT /note="Ubiquitin carboxyl-terminal hydrolase 14"
FT /id="PRO_0000080639"
FT DOMAIN 4..80
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 105..482
FT /note="USP"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 434
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMA1"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 448
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
SQ SEQUENCE 493 AA; 55922 MW; 598553BF435E6495 CRC64;
MPLYSVTVKW GKEKFGGVEL NTDEPPMVFK AQLFALTGVQ PARQRVMVKG GTLKDDDWGN
IKIKNGMTIL MMGSADALPE EPSAKTVFVE DMTEEQLASA MELPCGLTNL GNTCYMNATV
QCIRSVPELK DALKRYAGAL RASGEMASAQ YITAALRDLF DSMDKTSSSI PPIILLQFLH
MAFPQFAEKG EQGQYLQQDA NECWIQMMRV LQQKLEAIED DSVKETDSSA AAVAPSKKKS
LIDQFFGVEF ETTMKCTESE EEEVTKGKEN QLQLSCFINQ EVKYLFTGLK LRLQEEITKQ
SPTLQRNALY IKSSKISRLP AYLTIQMVRF FYKEKESVNA KVLKDVKFPL MLDVYELCTP
ELQEKMVSFR SKFKDIEDKK VNQQPNASDK KSSPQKEVRY EPFSFADDIG SNNCGYYDLQ
AVLTHQGRSS SSGHYVSWVK RKHDEWIKFD DDKVSIVTPE DILRLSGGGD WHIAYVLLYG
PRRVEIMEEE NEQ
