ID A0A2K5W1Q2_MACFA Unreviewed; 1635 AA.
AC A0A2K5W1Q2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000031018.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000031018.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000031018.2}
RP IDENTIFICATION.
RG Ensembl;
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 Ensembl; ENSMFAT00000005228.2; ENSMFAP00000031018.2; ENSMFAG00000042248.2.
DR VEuPathDB; HostDB:ENSMFAG00000042248; -.
DR GeneTree; ENSGT00940000155797; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000233100; Chromosome 16.
DR Bgee; ENSMFAG00000042248; Expressed in bone marrow and 13 other cell types or tissues.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT DOMAIN 245..280
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 281..316
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 386..602
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 765..1598
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1398..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1635 AA; 185333 MW; 8C64C59432353C17 CRC64;
MCGVERGLWQ SAQLARRGWR PFSQGYCQML LILTPPVTDV ELKRLKDAFK RTCGLSYYMG
QHCFIREVLG DGVPPKVAEV IYCSFGGTSK GLHFNNLIVG LVLLTRGKDE EKAKYIFSLF
SSESGNYVIR EEMERMLHVV DGKVPDTLRK CFSEGEKVNY EKFRNWLFLN KDAFTFSRWL
LSGGVYVTLT DDSDTPTFYQ TLAGVTHLEE SDIIDLEKRY WLLKAQSRTG RFDLETFGPL
VSPPIRPSLS EGLFNAFDEN RDNHIDFKEI SCGLSACCRG PLAERQKFCF KVFDVDRDGV
LSRVELRDMV VALLEVWKDN RTDDIPELHM DLSDIVEGIL NAHDTTKMGH LTLEDYQIWS
VKNVLANEFL NLLFQVCHIV LGLRPATPEE EGQIIRGWLE RESRYGLQPG HNWFIISMQW
WQQWKEYVKY DTNPVVIEPS SVLNGGKYSF GTAVHPMEQV EDRIGSSLSY VNTTEEKFSD
NISTASEASE TAGSGFLYSA TPGADVCFAR QHNTSDNNNQ CLLGANGNIL LHLNPQKPGA
IDNQPLVTQE PVKATSLTLE GGRLKQTPQL IHGRDYEMVP EPVWRALYHW YGANLALPRP
VIKNSKTDIP ELELFPRYLL FLRQQPATRT QQSNIWVNMG MMSLRMFPQH FPRGNVPSPN
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 QVKCKTCGHI SVRFDPFNFL SLPLPMDSYM HLEITVIKLD
GTTPVRYGLR LNMDEKYTGL KKQLSDLCGL NSEQILLAEV HGSNIKNFPQ DNQKVRLSVS
GFLCAFEIPV PASPISASSP TQTDFSSSPS TNGMFTLTTN GDLPRPIFIP NGMPNTVVPC
GTEKNFTNGM VNGHMSSLPD SPFTGYIIAV HRKMMRTELY FLSSQKNRPS LFGMPLIVPC
TVHTRKKDLY DAVWIQVSRL ASPLPPQEAS NHAQDCDDSM GYQYPFTLRV VQKDGNTCAW
CPWYRFCRGC KIDCGEDRAF IGNAYIAVDW DPTALHLRYQ TSQERVVDEH ESVEQSRRAQ
AEPINLDSCL RAFTSEEELG ENEMYYCSKC KTHCLATKKL DLWRLPPILI IHLKRFQFVN
GRWIKSQKIV KFPRESFDPS AFLVPRDPAL CRRKPLTPEG DELSEPRVLA REVKKVDAQS
SAGEEDVLLS KSPSSLSANI ISSPKGSPSS SRKSGASCPS SKNSSPSSSP RTLGRSKGRL
RLPQIGSKNK LSSSKENLDA SRDNGAGQIC ELADALSRGH MLGGSQPELV TPQDHEVALA
NGFLYEHEAC GNGYSNGQLG NHSEEDSTDD QREDTRIKPI YNLYAISCHS GILGGGHYVT
YAKNPNCKWY CYNDSSCKEL HPDEIDTDSA YILFYEQQGI DYAQFLPKID GKKMADTSSM
DEDFESDYKK YCVLQ
//
