ID A0A2I0MJ58_COLLI Unreviewed; 860 AA.
AC A0A2I0MJ58;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP15 {ECO:0000313|EMBL:PKK29716.1};
GN ORFNames=A306_00005005 {ECO:0000313|EMBL:PKK29716.1};
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:PKK29716.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK29716.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK29716.1};
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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:PKK29716.1}.
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DR EMBL; AKCR02000009; PKK29716.1; -; Genomic_DNA.
DR RefSeq; XP_005498071.1; XM_005498014.1.
DR AlphaFoldDB; A0A2I0MJ58; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
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 InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF28; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 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|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 167..811
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 95..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..547
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 98239 MW; DCCA889CA33CF6E9 CRC64;
MFVKHCKVEV YLTELKLCEN GNMNNVVTRR FSKADTIDTI EKEIRKIFNI PGEKETRLWN
KYMSNTFEPL NKPDSTIQDA GLYQGQVLVI EQKNEDGTWP RGPSTPKSPG ASNFSTLPKI
SSSLSNNYNN MNNRNVKNSN YCPPSYTAYK NYDYSEPGRH NEQPGLCGLS NLGNTCFMNS
AIQCLSNTPP LTEYFLTDKY QEELNFDNPL GMRGEIAKSY AELIKQMWSG KYSYVTPRAF
KTQVGRFAPQ FSGYQQQDCQ ELLAFLLDGL HEDLNRIRKK PYIQLKDADG RPDKVVAEEA
WENHLKRNDS IIVDIFHGLF KSTLVCPECA KISVTFDPFC YLTLPLPMKK ERTLEVYLVR
MDPLAKPMQY KVVVPKIGNI LDLCTALSAL SGVPADKMIV TDIYNHRFHR IFGMDENLSN
IMERDDIYVF EIPINRTEDT EQVIIPVCLR EKCRHTSYSH SGSSLFGQPF LIAVPRNNTE
DKLYNLLLLR MCRYVKTCTE SEDTEGSLHC CKDHGINGNG PNGIHEEGSP SEMETDEQDD
ESSQDQELPS ENENSQSEDS VGGDNDSENG LCTEDTCKGQ PLTGHKKRLF TFQFNNLGNT
DINYIKDDTR HIRFDDRQPR LDERSFLALD WDPELKKRYF DDSAAEDFEK HESVEYKPPK
KPFVKLKDCI ELFTTKEKLG AEDPWYCPNC KEHQQATKKL DLWSLPPVLV VHLKRFSYSR
YMRDKLDTLV GFPINDLDMS EFLINPNAGP CRYNLIAVSN HYGGMGGGHY TAFAKNKDDG
KWYYFDDSSV STACEDQIVS KAAYVLFYQR QDTISGTGFF PLDRETKQGA SAATGIPLES
DEDSNENDND IENENCMHTN
//
