ID A0A2I0LW91_COLLI Unreviewed; 837 AA.
AC A0A2I0LW91;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP4 {ECO:0000313|EMBL:PKK21689.1};
GN ORFNames=A306_00010796 {ECO:0000313|EMBL:PKK21689.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK21689.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK21689.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK21689.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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:RU366025};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP4 subfamily.
CC {ECO:0000256|ARBA:ARBA00037971}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK21689.1}.
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DR EMBL; AKCR02000076; PKK21689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0LW91; -.
DR STRING; 8932.A0A2I0LW91; -.
DR InParanoid; A0A2I0LW91; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF45; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 4; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 1..67
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 200..816
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 837 AA; 95001 MW; 2F8D450CF0B9ABCB CRC64;
MAGADDPCLF PGPVDNSGLF SDPESQSLKE HLIEELDYVL VPTEAWNKLV TWYGCIEGQQ
PIVRKVVEYG LFVKHYKVEV YLLELKLCES SDPDNVISCH FSKADTVATI EKEMRKLFNI
PAEKETRLWN RYTSNTYEQL SKLDSTVQDA WLYHGQVVLI EVKNEDGTWP GQHFLAKGSG
FVSNSYNCRD GASLSQPGLC GLSNLGNTCF MNSALQCLSN TPPLTEYFLE DKYEAEINQN
NPLGMRGEIA EAYAELIKQI WSGRHSHVAP RMFKTQVGRF APQFSGYQQQ DSQELLAFLL
DGLHEDLNRV KKKPYLELKD ANGRPDSEVA KEAWENHRLR NDSIIVDIFH GLFKSTLVCP
KCSKVSVTFD PFCYLTLPLP LRRDRLMEVT LVYADPQHRP VQYRVVVPMM GAISDLCESL
SRLSGVPAEN MVVTDVYNHR FHKIFQMDEG LNHIMPKDDI FVYEVRKPSE DGTECVTLSV
YFREKTMRQS SSTSATMLFG QPLLISVPKH KLTVDHLYSV ILEQISRYVK LPLAEEYSTP
CPDKGTCNGS NGVVEGDVEE MEHQDGGQEG KEKMAEADSC HSEGCMQIES ARDLQPCKKQ
YFTFSLVNSS GTSEINSVVE GKILKLNAFS VLAVDWDSDT RRLLFDEQEA QAFEKHGSML
QPQKKKAVVA LRDCIELFTT METLGEHDPW YCPNCKKHQQ ATKKFDLWSL PRILVVHLKR
FSYSRYCRDK LDTVVLFPIR GLNMSEFVCD PRAGSYVYDL IAVSNHYGAM GVGHYTAYAK
NKVNGKWYYF DDSSVSVASE DQIVTKAAYV LFYQRRNSEE HTVPSPPQEE CDGMDTS
//
