ID K7FQP5_PELSI Unreviewed; 1106 AA.
AC K7FQP5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:ENSPSIP00000010355.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000010355.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000010355.1}
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; AGCU01096765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01096766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01096767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01096768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01096769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01096770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01096771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01096772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01096773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006124659.1; XM_006124597.1.
DR AlphaFoldDB; K7FQP5; -.
DR STRING; 13735.ENSPSIP00000010355; -.
DR MEROPS; C19.016; -.
DR Ensembl; ENSPSIT00000010407.1; ENSPSIP00000010355.1; ENSPSIG00000009176.1.
DR GeneID; 102452147; -.
DR KEGG; pss:102452147; -.
DR CTD; 7874; -.
DR eggNOG; KOG1863; Eukaryota.
DR GeneTree; ENSGT00940000156053; -.
DR HOGENOM; CLU_003532_0_0_1; -.
DR OMA; HTAHHRF; -.
DR OrthoDB; 51419at2759; -.
DR TreeFam; TF105667; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
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:UP000007267};
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..525
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1106 AA; 129093 MW; 482A8C04AD87188D CRC64;
MNHHQQQHQK PGEQQLSEPE DMEMEAGDTD DPPRITQNPV INGNVAMADG HNNTEEDMED
DTSWRSEATF QFTVERFNRL SESVLSPPCF VRNLPWKIMV MPRLYPDRPH QKSVGFFLQC
NAESDSTSWS CHAQAVLKII NYKDDEKSFS RRISHLFFHK ENDWGFSNFM AWSEVTDPEK
GFIEDDKVTF EVYVQADAPH GVAWDSKKHT GYVGLKNQGA TCYMNSLLQT LFFTNQLRKA
VYMMPTEGDD SSKSVPLALQ RVFYELQHSD KPANKKPVGT KKLTKSFGWE TLDSFMQHDV
QELCRVLLDN VENKMKGTCV EGTIPKLFRG KMVSYIQCKH VDYRSERIED YYDIQLSIKG
KKNIFESFID YVAVEQLDGD NKYDAGEHGL QEAEKGVKFL TLPPVLHLQL MRFMYDPQTD
QNIKINDRFE FPEQLPLDEF LQKTDPKDAA NYILHAVLVH SGDNHGGHYV VYLNPKGDGK
WCKFDDDVVS RCTKEEAIEH NYGGHDDDLS VRHCTNAYML VYIRESKLSE VLQPVTDHDI
PQQLVERLQE EKRIEAQKRK ERQEAHLYMQ VQIVTEDQFC GHQGNDMYDE EKVKYTVFKV
LKNSTLVEFV QNLSQTMGFP QDQIRLWPMQ ARSNGTKRPA MLDNEADGNK TMIELSDNEN
PWTIFLETVD PEMAATGATL PKFDKDHDVM LFLKMYDPKT RSLNYCGHIY TPISCKIRDL
LPVMCERAGF PQETNLILYE EVKPNLTERI QDYDVSLDKA LDELMDGDII VFQKDDPEND
NSELPTAKEY FRDLYHRVDV IFCDKTIPND PGFVVTLSNR MNYFQVAKTV AQRLNTDPML
LQFFKSQGYR DGPGNPLRHN YEGTLRDLLQ FFKPRQPKKL YYQQLKMKIT DFENRRSFKC
IWLNNQFREE EITLYPDKHG CVRDLLEECK KAVELCERGS GKLRLLEIVS YKIIGVHQED
ELLECLSPAT SRTFRIEEIP LDQVDIDKEN EMLITVAHFH KEVFGTFGIP FLLRIHQGEH
FREVMKRIQT MLDIQEKEFE KFKFAIVMMG RHQYLNEDEY EVNLKDFEPQ PGNMSHPRPW
LGLDHFNKAP KRSRYTYLEK AIKIHN
//
