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Database: UniProt
Entry: A0A2U3VRA0_ODORO
LinkDB: A0A2U3VRA0_ODORO
Original site: A0A2U3VRA0_ODORO 
ID   A0A2U3VRA0_ODORO        Unreviewed;      1605 AA.
AC   A0A2U3VRA0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   Name=USP32 {ECO:0000313|RefSeq:XP_004397745.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004397745.1};
RN   [1] {ECO:0000313|RefSeq:XP_004397745.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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};
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DR   RefSeq; XP_004397745.1; XM_004397688.1.
DR   STRING; 9708.A0A2U3VRA0; -.
DR   GeneID; 101370396; -.
DR   KEGG; oro:101370396; -.
DR   CTD; 84669; -.
DR   InParanoid; A0A2U3VRA0; -.
DR   OrthoDB; 5474185at2759; -.
DR   Proteomes; UP000245340; Unplaced.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 3.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
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:SF76; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 32; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF13202; EF-hand_5; 2.
DR   Pfam; PF14836; Ubiquitin_3; 1.
DR   Pfam; PF00443; UCH; 1.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00695; DUSP; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000313|RefSeq:XP_004397745.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245340}.
FT   DOMAIN          228..263
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          264..299
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          369..586
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          735..1568
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1323..1435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1355..1404
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1416..1431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1605 AA;  181474 MW;  6AB713E66A5E5D95 CRC64;
     MGAKESRIGF LSYEEALRRV TDVELKRLKD AFKRTCGLSY YMGQHCFIRE VLGDGVPPKV
     AEVIYCSFGG TSKGLHFNNL IVGLVLLTRG RDEEKAKYIF SLFASESGSY VVREEMERML
     HVVDGKVPDT LRKCFSEGEK VNYEKFRNWL LLNKDAFTFS RWLLSGGVYV TLTDDSDTPT
     FYQTLAGVTH LEESDIIDLE KRYWLLKAQS RTGRFDLETF GPLVSPPIRP SLSEGLFNAF
     DENRDNHIDF KEISCGLSAC CRGPLAERQK FCFKVFDVDR DGVLSRVELR DMVVALLEVW
     KDNRTDDIPE LHTDLSDIVE GILNAHDTTK MGHLTLEDYQ IWSVKNVLAN EFLNLLFQVC
     HIVLGLRPAT PEEEGQIIRG WLERESRYGL QPGHNWFIIS MQWWQQWKEY VKYDASPVVI
     EPSSVLNGGK YSFGTAVHCI EQSEDRIGGG SLTYVNTTEE KFSDNISSAS EASETAGSGF
     LYSATPGADM CFARQHNTSD NNNQCLLGAN GNILLHLNPQ KPGAIDNQPL VTQEPVKATS
     LTLEGGRLKR TPQLIHGRDY EMVPEPVWRA LYHWYGANLA LPRPVIKNSK TEIPELELFP
     RYLLFLRQQP ATRTQQSNVW VNMGNVPSPN APLKRVLAYT GCFSRMQTIK EIHEYLSQRL
     RIKEEDMRLW LYNSENYLTL LDDEDHRLEY LKIQDEQHLV IEVRNKDMSW PEEMSFIANS
     SKIDRHKVPT EKGATGLSNL GNTCFMNSSI QCVSNTQPLT QYFISGRHLY ELNRTNPIGM
     KGHMAKCYGD LVQELWSGTQ KNVAPLKLRW TIAKYAPRFN GFQQQDSQEL LAFLLDGLHE
     DLNRVHEKPY VELKDSDGRP DWEVAAEAWD NHLRRNRSIV VDLFHGQLRS QVRCKTCGHI
     SVRFDPFNFL SLPLPMDSYM HLEITVIKLD GTTPVRYGLR LNMDEKYTGL KKQLSDLCGL
     KSEQILLAEV HGSNIKNFPQ DNQKVRLSVS GFLCAFEIPI PGSPISASSP VQTDFSSSPS
     TNGMFTLTTN GDLPRPIFIP NGMPNTVVPC GTEKNFTNGM VNGHMPSLPD NSFTGYIIAV
     HRKMMRTELY FLSSQKNRPS LFGMPLIVPC TVHTRKKDLY DAVWIQVSRL ASPLPPQEAS
     NHAQDCDDSM GYQYPFTLRV VQKDGNSCAW CPWYRFCRGC KIDCGEDRAF IGNAYIAVDW
     DPTALHLRYQ TSQERVVDEH ESVEQSRQAQ AEPINLDSCL RAFTSEEELG ENEMYYCSKC
     KTHCLATKKL DLWRLPPILI IHLKRFQFVN GRWIKSQKIV KFPRESFDPS AFLVPRAPAL
     CQRKPLTPQG DDLSEPRVPG GDVKKVDAQN SAGEEEVLLS KSPSSLSANI ISSPKGSPSS
     TRKSGTSCPS SKNSSPNSSP RTLGRSKGRL RLPQIGSKNK LSSSKENLDA SRENGAGQVC
     ELADASSRGH MLGGSQTELV TPQDHEGALA NGFLYEHEAC GNGYSNGQLE NHSEEDSTDD
     QREDVRVKPI YNLYAISCHS GILGGGHYVT YAKNPNSKWY CYNDSSCKEL HPDEIDTDSA
     YILFYEQQGI DYAQFLPKID GKKMADTSSM DEDFESDYKK YCVLQ
//
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