ID A0A158REG0_HYDTA Unreviewed; 1763 AA.
AC A0A158REG0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7 {ECO:0000256|ARBA:ARBA00021393};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Ubiquitin thioesterase 7 {ECO:0000256|ARBA:ARBA00031508};
DE AltName: Full=Ubiquitin-specific-processing protease 7 {ECO:0000256|ARBA:ARBA00031500};
GN ORFNames=TTAC_LOCUS7227 {ECO:0000313|EMBL:VDM31573.1};
OS Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Hydatigera.
OX NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000724201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TTAC_0000724201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM31573.1, ECO:0000313|Proteomes:UP000274429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the calreticulin family.
CC {ECO:0000256|ARBA:ARBA00010983}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; UYWX01020354; VDM31573.1; -; Genomic_DNA.
DR STRING; 6205.A0A158REG0; -.
DR WBParaSite; TTAC_0000724201-mRNA-1; TTAC_0000724201-mRNA-1; TTAC_0000724201.
DR Proteomes; UP000046396; Unplaced.
DR Proteomes; UP000274429; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.10.250.10; Calreticulin/calnexin, P domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR001580; Calret/calnex.
DR InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR11073:SF1; CALNEXIN 14D-RELATED; 1.
DR PANTHER; PTHR11073; CALRETICULIN AND CALNEXIN; 1.
DR Pfam; PF00262; Calreticulin; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR PRINTS; PR00626; CALRETICULIN.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF63887; P-domain of calnexin/calreticulin; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 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 Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000274429};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT TRANSMEM 1661..1681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..227
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 246..557
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 51..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1444..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1728..1748
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1763 AA; 198650 MW; B2C035738DEE8516 CRC64;
MLVFICAIIE VNTTSDLVQE LEVIAIKMPV KDLVGQGDYR TEDAMDVDSN TNVNKAADPA
HPPLQSTLNH GHLKQSNVSD PQIEELSIDE DDPARPSGKI DYTFDGIEDP RSFDIKKELR
LLSDPVTIRC LPWRILLVFV PVCQRSTMGM FLQCNDNSTT TNWTCGARAK LELLSQTRSL
SKTHTIMHSF AAKENDWGYQ AFISYEELFN PENGYVVNKK LRARIQVEAD APHGTEWDSK
KFTGFVGLKN QGATCYLNSV LQALYCTNAL RKAVFQMPTE SDEISTSVPL ALQRTFFDLQ
CSDKAVGTEK LTRSFGWTTW DSFMQHDAQE LCRVLLDNME CKMKGTDVEA IIPKLFCGKM
ISYIRCKDVA YESKREEQFY DIQLKVKGNC DVHDAFKEYV QVETLDSDNK YDAGTFGLQD
AEKGIKFLRF PPVLYLQLMR FQYDFVSNSN VKINDRFEFP YDLDLSDYLV QDVENMEEEP
RYTKYFLQAV LVHSGDHHGG HYVVYINPRG DNKWYQFDDD VVSSCRPKDA IEMNYGNSDD
PLCRASSNAY MLVYIACDAR EEVLCPVTDD MIPFSLSNRF HEEHSVEEKE RRVKDHAHEF
ATINILLDED FYGFEGPELL RINEIPIRSL RIHRQELSES KLIDAIGDFL QWSTQKFHLW
RAICQKSTCC VEFSRKITTE LSSDGVLTLW ARRREQAIWV GGPASDCNLC FFKYFDPNIC
TLCYCGHADL PTSASVEALP ALLNKRVGLP PTTPLIFYRQ DNAQLPKPVE LAVLSRKLKH
GEIIYFHVCL CHFIYASSLQ PSRRHQWRHE LPNVSLHLRK VAINGHSPSE PQKSLPLSEA
FVHYFVSSSL MVDILLVDKL RKSDPGILIR VSPELSYWEF AKLAAGYLSG RLDHLQFFAS
HPPPTSGTGV NAAANKTSNV SAQDLHVTAT NPSPLSGDPG NGNSFSPSGG ASLVSEQSLA
AKASGFAGAS ANLISALASA AHQGLVREPP GPPVPSGTKA NLRDFLSLPS TVSAITVQCT
TPASVASQDR PSLCVSRYSS IPRAIPSPFS NHTLHVPAPR RVYYAHTALP VSQLECLKQI
QVAFFGPKLT DRLDLGLSVP SSGTVTDILA EVRSHITLSG SGKLRLMEIR LNRIFQIYEE
NYPLERIDDA MMVLQSDINE NLRTGLRVEE VPQDEENLQQ DDLVINAAHY NKALNDTFGV
PFTVRLRNGE SYSDVKKRIR ERLDVVNDKE FDAWNFALVF RNKFIAIPDE NSVYVDTVAL
TRDTCLGPKP WLVLFSLHVP RMVLSTATKE GVDASISKYE GKWSIEVPLT SAVENDYCLV
LKSEGKHHAI SVDLGRDFAF DKDEFVVQYE VKFMNKLTCG GAYIKLLSAS PNLNLLHFIF
RHENPKTGVI QEKHMDKPTT TLESLFTDGK THLFTCVTRF DNSFEVYVDQ SLIKSGNLLS
DFTPPVNPPA EINDPNDKKP ETWDERERIP DPDAKRPDDW DESAPQFIID EDATMPEGWL
ADTPKLIPDP KAERPSDWNT ETDGEWEAPM IDNPDCQSAP GCGPWEKPKK LNPNYRGKWS
PPMIANPKFD GIWKPKRIPN PDYFEDKHPY RMAPIRALGL ELWSMTAEIA FDNFYIGTSK
KGADKFAAET WVLKQKAEEQ SRADGRSVFN AAVEMISEKP WHAAACIAIG LLSLGLFFCW
CCRSPVAKDD ADYKKTDEPV PDSSPEEFDL NVSTEVDAER SGSDVDKGEE EQEDEDGGDA
DEEQEVEEEL TKPLTTRQRT RKE
//