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
//