ID F6YGJ7_CIOIN Unreviewed; 1099 AA.
AC F6YGJ7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 71.
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};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000008727.3, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000008727.3}
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; EAAA01001766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6YGJ7; -.
DR STRING; 7719.ENSCINP00000008727; -.
DR Ensembl; ENSCINT00000008727.3; ENSCINP00000008727.3; ENSCING00000004226.3.
DR GeneTree; ENSGT00940000156053; -.
DR HOGENOM; CLU_003532_0_0_1; -.
DR InParanoid; F6YGJ7; -.
DR OMA; HTAHHRF; -.
DR TreeFam; TF105667; -.
DR Proteomes; UP000008144; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
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:UP000008144};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 65..193
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 212..520
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 126331 MW; E53D184ED36118F1 CRC64;
LSVPQIEETY KPMEHQGGNP DAMETEDSPA INDASMVNGD ASENDDAKSD EIAEEDDEFG
FYRSQATFSF TVDNINKLVE STTSPPTYVR GLPWRILVMP RTIHDRSAGK SLGYFLQCNA
ENESTLWSCH GSAALRILPA KDGVEMLDKK IEHMFYCKEN DWGFSTFLPW ADLVNPEKGY
ITPDKKVTFQ VHVYADAPHG LAWDSRKLTG YIGLKNQGAT CYMNSLLQTL FFTNKLRKAV
YMMPTESDDS MKSVSLALQR VFYELQSSDK PVATKKLTKS FGWETFDSFM QHDVQELCRV
LLDNVELKMK GTCVEGTIPD ILEGKFKSYV KCKHVDYVSS REESFFDIQL IVKGNKNVME
SFRNYVKPDT LDGDNKFDAG DFGMQEAEKG IIFKHFPAVL HLQLLRFQYD AATDMYVKTN
DRYEFPEVLH LDEFLEKPDR NDSAVYILHA ILVHSGDNHG GHYVAYLNPK GDGKWCKFDD
DVVSRCTKKE AFLGSYGGVG EESYVARNST NAYMLVYIRK SKLNDVLCPV TDADIPEQLM
ERLNEERQLE AFRRKEKAEM HLYLSVNLVT EDMFCGHQAE DLFDFERSHF TRHIKILRQA
SFDDLLNLIS QGIGYSKNQF RLWLFSQRPN NSWRPTLLET GETVGKHLIE VAENENPWHL
WLETIQPDST EDTLPAFDKQ GDILVFLKMY TPSTRTISYC GHVSVPIEGT SVVAMEKTLR
KRGGLPPNTP LLLFEEISAS ELRPIHDRNL QFGEVMDKLM DGNIIVFQPV EPSCPDAARY
FLDVFFRVDV ILCDKNDPLD PGFTVSLNRN WTYGQFAEKV AERLDTDPMM LQFFRVQNVR
DQPGNVIRSS FDGQLKDLLQ IYGTRKPSKR LYYQQLTMKV NEFENKRQFR CMFVWPNLKE
EEIVLYPNKT SCVAGLLEEC RKKFAIDSSK ELRVLEVVGN KICGILRPEK ALEDLTPYGQ
VARLYRIEIV PDDQKEISDE EVLICASHFH KEIYNTFGVP LLIKVRTGER FSEIRERIQK
AMEIPDNVFE KYKIAVVVAG QVKYMSEDMH MMMNLKDVMP TMSSKLCAKA WIGLDHLNKN
SKRHQSRFGY TEKAIKIHN
//
