ID H0UZS5_CAVPO Unreviewed; 1101 AA.
AC H0UZS5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 76.
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:ENSCPOP00000002694.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000002694.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000002694.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000002694.3};
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; AAKN02007474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003477794.1; XM_003477746.3.
DR AlphaFoldDB; H0UZS5; -.
DR STRING; 10141.ENSCPOP00000002694; -.
DR Ensembl; ENSCPOT00000003006.3; ENSCPOP00000002694.3; ENSCPOG00000002969.4.
DR GeneID; 100726431; -.
DR KEGG; cpoc:100726431; -.
DR CTD; 7874; -.
DR VEuPathDB; HostDB:ENSCPOG00000002969; -.
DR eggNOG; KOG1863; Eukaryota.
DR GeneTree; ENSGT00940000156053; -.
DR HOGENOM; CLU_003532_0_0_1; -.
DR InParanoid; H0UZS5; -.
DR OMA; HTAHHRF; -.
DR OrthoDB; 51419at2759; -.
DR TreeFam; TF105667; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000002969; Expressed in testis and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:1990380; F:K48-linked deubiquitinase activity; IEA:Ensembl.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; IEA:Ensembl.
DR GO; GO:0044027; P:negative regulation of gene expression via CpG island methylation; IEA:Ensembl.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:Ensembl.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:Ensembl.
DR GO; GO:1901537; P:positive regulation of DNA demethylation; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0042752; P:regulation of circadian rhythm; IEA:Ensembl.
DR GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; IEA:Ensembl.
DR GO; GO:0075342; P:symbiont-mediated disruption of host cell PML body; IEA:Ensembl.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IEA:Ensembl.
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:UP000005447};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 67..194
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 213..520
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 128067 MW; 62E62C4F54313C97 CRC64;
MNHQQQPPPK AGEQQLSEPE DMEMEAGDTD DPPRITQNPV INGNVALSDG HSNAEEDMED
DTSWRSEATF QFTVERFSRL SESVLSPPCF VRNLPWKIMV MPRFYPDRPH QKSVGFFLQC
NAESDSTSWS CHAQAVLKII NYRDDDKSFS RRISHLFFHK ENDWGFSNFM AWSEVTDPEK
GFIDDDKVTF EVFVQADAPH GVAWDSKKHT GYVGLKNQGA TCYMNSLLQT LFFTNQLRKA
VYMMPTEGDD SSKSVPLALQ RVFYELQHSD KPVGTKKLTK SFGWETLDSF MQHDVQELCR
VLLDNVENKM KGTCVEGTIP KLFRGKMVSY IQCKEVDYRS DRREDYYDIQ LSIKGKKNIF
ESFVDYVAVE QLDGDNKYDA GEHGLQEAEK GVKFLTLPPV LHLQLMRFMY DPQTDQNIKI
NDRFEFPEQL PLDEFLQKTD PKDPANYILH AVLVHSGDNH GGHYVVYLNP KGDGKWCKFD
DDVVSRCTKE EAIEHNYGGH DDDLSVRHCT NAYMLVYIRE SKLSEVLQAV TDHDIPQQLV
ERLQEEKRIE AQKRKERQEA HLYMQVQIVA EDQFCGHQGN DMYDEEKVKY TVFKVLKNSS
LAEFVQSLSQ TMGFPQDQIR LWPMQARSNG TKRPAMLDNE ADGNKTMIEL SDNENPWTIF
LETVDPELAA SGATLPKFDK DHDVMLFLKM YDPKTRSLNY CGHIYTPISC KIRDLLPVMC
DRAGFIQDTS LILYEEVKPN LTERIQDYDV SLDKALDELM DGDIIVFQKD DPENDNSELP
TAKEYFRDLY HRVDVIFCDK TIPNDPGFVV TLSNRMNYFQ VAKTVAQRLN TDPMLLQFFK
SQGYRDGPGN PLRHNYEGTL RDLLQFFKPR QPKKLYYQQL KMKITDFENR RSFKCIWLNS
QFREEEITLY PDKHGCVRDL LEECKKAVEL GEKASGKLRL LEIVSYKIIG VHQEDELLEC
LSPATSRTFR IEEIPLDQVD IDKENEMLIT VAHFHKEVFG TFGIPFLLRI HQGEHFREVM
KRIQSLLDIQ EKEFEKFKFA IVMMGRHQYI NEDEYEVNLK DFEPQPGNMS HPRPWLGLDH
FNKAPKRSRY TYLEKAIKIH N
//
