ID H2NQ35_PONAB Unreviewed; 1086 AA.
AC H2NQ35; A0A2J8S085;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 72.
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 Name=USP7 {ECO:0000313|Ensembl:ENSPPYP00000008014.3};
GN ORFNames=CR201_G0047292 {ECO:0000313|EMBL:PNJ14179.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000008014.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000008014.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ14179.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ14179.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000008014.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; NDHI03003627; PNJ14179.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000008014; -.
DR Ensembl; ENSPPYT00000008346.3; ENSPPYP00000008014.3; ENSPPYG00000007087.3.
DR eggNOG; KOG1863; Eukaryota.
DR GeneTree; ENSGT00940000156053; -.
DR HOGENOM; CLU_003532_0_0_1; -.
DR TreeFam; TF105667; -.
DR Proteomes; UP000001595; Chromosome 16.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03772; MATH_HAUSP; 1.
DR CDD; cd02659; peptidase_C19C; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF644; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 7; 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 SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 52..179
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 198..505
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1086 AA; 126282 MW; 0D008246DCE4942B CRC64;
MAGNHRLGLE AGDTDDPPRI TQNPVINGNV ALSDGHNNAE EDMEDDTSWR SEATFQFTVE
RFSRLSESVL SPPCFVRNLP WKIMVMPRFY PDRPHQKSVG FFLQCNAESD STSWSCHAQA
VLKIINYRDD EKSFSRRISH LFFHKENDWG FSNFMAWSEV TDPEKGFIDD DKVTFEVFVQ
ADAPHGVAWD SKKHTGYVGL KNQGATCYMN SLLQTLFFTN QLRKAVYMMP TEGDDSSKSV
PLALQRVFYE LQHSDKPVGT KKLTKSFGWE TLDSFMQHDV QELCRVLLDN VENKMKGTCV
EGTIPKLFRG KMVSYIQCKE VDYRSDRRED YYDIQLSIKG KKNIFESFVD YVAVEQLDGD
NKYDAGEHGL QEAEKGVKFL TLPPVLHLQL MRFMYDPQTD QNIKINDRFE FPEQLPLDEF
LQKTDPKDPA NYILHAVLVH SGDNHGGHYV VYLNPKGDGK WCKFDDDVVS RCTKEEAIEH
NYGGHDDDLS VRHCTNAYML VYIRESKLSE VLQAVTDHDI PQQLVERLQE EKRIEAQKRK
ERQEAHLYMQ VQIVAEDQFC GHQGNDMYDE EKVKYTVFKV LKNSSLAEFV QSLSQTMGFP
QDQIRLWPMQ ARSNGTKRPA MLDNEADGNK TMIELSDNEN PWTIFLETVD PELAASGATL
PKFDKDHDVM LFLKMYDPKT RSLNYCGHIY TPISCKIRDL LPVMCDRAGF IQDTSLILYE
EVKPNLTERI QDYDVSLDKA LDELMDGDII VFQKDDPEND NSELPTAKEY FRDLYHRVDV
IFCDKTIPND PGFVVTLSNR MNYFQVAKTV AQRLNTDPML LQFFKSQGYR DGPGNPLRHN
YEGTLRDLLQ FFKPRQPKKL YYQQLKMKIT DFENRRSFKC IWLNSQFREE EITLYPDKHG
CVRDLLEECK KAVELGEKAS GKLRLLEIVS YKIIGVHQED ELLECLSPAT SRTFRIEEIP
LDQVDIDKEN EMLVTVAHFH KEVFGTFGIP FLLRIHQGEH FREVMKRIQS LLDIQEKEFE
KFKFAIVMMG RHQYINEDEY EVNLKDFEPQ PGNMSHPRPW LGLDHFNKAP KRSRYTYLEK
AIKIHN
//
