UBP14_BOVIN
ID UBP14_BOVIN Reviewed; 494 AA.
AC Q0IIF7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 95.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP ASSOCIATION WITH THE 26S PROTEASOME.
RX PubMed=18162577; DOI=10.1091/mbc.e07-10-1040;
RA Koulich E., Li X., DeMartino G.N.;
RT "Relative structural and functional roles of multiple deubiquitylating
RT proteins associated with mammalian 26S proteasome.";
RL Mol. Biol. Cell 19:1072-1082(2008).
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}.
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DR EMBL; BC122666; AAI22667.1; -; mRNA.
DR RefSeq; NP_001068657.1; NM_001075189.1.
DR RefSeq; XP_015315570.1; XM_015460084.1.
DR AlphaFoldDB; Q0IIF7; -.
DR BMRB; Q0IIF7; -.
DR SMR; Q0IIF7; -.
DR STRING; 9913.ENSBTAP00000025580; -.
DR MEROPS; C19.015; -.
DR PaxDb; Q0IIF7; -.
DR PRIDE; Q0IIF7; -.
DR Ensembl; ENSBTAT00000025580; ENSBTAP00000025580; ENSBTAG00000019214.
DR GeneID; 505106; -.
DR KEGG; bta:505106; -.
DR CTD; 9097; -.
DR VEuPathDB; HostDB:ENSBTAG00000019214; -.
DR VGNC; VGNC:36712; USP14.
DR eggNOG; KOG1872; Eukaryota.
DR GeneTree; ENSGT00390000009615; -.
DR InParanoid; Q0IIF7; -.
DR OMA; MCKGGIL; -.
DR OrthoDB; 600543at2759; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000019214; Expressed in omental fat pad and 105 other tissues.
DR ExpressionAtlas; Q0IIF7; baseline and differential.
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; IDA:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cytoplasm; Hydrolase; Immunity;
KW Innate immunity; Membrane; Phosphoprotein; Protease; Proteasome;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..494
FT /note="Ubiquitin carboxyl-terminal hydrolase 14"
FT /id="PRO_0000268845"
FT DOMAIN 4..80
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 105..483
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 435
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 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 449
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
SQ SEQUENCE 494 AA; 56013 MW; 089AE0AC7790CCC5 CRC64;
MPLYSVTVKW GKEKFEGVEL NTDEPPMVFK AQLFALTGVQ PARQKVMVKG GTLKDDDWGN
IKMKNGMTVL MMGSADALPE EPSAKTVFVE DMTEEQLASA MELPCGLTNL GNTCYMNATV
QCIRSVPELK DALKRYAGAL RASGEMASAQ YITAALRDLF DSMDKTSSSI PPIILLQFLH
MAFPQFAEKG EQGQYLQQDA NECWVQMMRV LQQKLEAIED DTVKETDSSS ASAVTPSKKK
SLIDQFFGVE FETTMKCTES EEEEVTKGKE SQLQLSCFIN QEVKYLFTGL KLRLQEEITK
QSPTLQRNAL YIKSSKISRL PAYLTIQMVR FFYKEKESVN AKVLKDVKFP LMLDVYELCT
PELQEKMVSF RSKFKDLEDK KVNQQPKTGD KDSSPQKEVK YEPFSFADDI GSNNCGYYDL
QAVLTHQGRS SSSGHYVSWV KRKQDEWIKF DDDKVSIVTP EDILRLSGGG DWHIAYVLLY
GPRRVEIMEE ESEQ
