GenomeNet

Database: UniProt
Entry: H2XX74_CIOIN
LinkDB: H2XX74_CIOIN
Original site: H2XX74_CIOIN 
ID   H2XX74_CIOIN            Unreviewed;       367 AA.
AC   H2XX74;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
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:ENSCINP00000034258.1, 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:ENSCINP00000034258.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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};
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DR   EMBL; EAAA01002494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H2XX74; -.
DR   STRING; 7719.ENSCINP00000034258; -.
DR   Ensembl; ENSCINT00000031318.1; ENSCINP00000034258.1; ENSCING00000018394.1.
DR   GeneTree; ENSGT00390000016392; -.
DR   HOGENOM; CLU_056188_0_0_1; -.
DR   InParanoid; H2XX74; -.
DR   OMA; TDFQILH; -.
DR   TreeFam; TF329594; -.
DR   Proteomes; UP000008144; Unassembled WGS sequence.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   CDD; cd22770; OTU_OTUD3; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR12419:SF7; OTU DOMAIN-CONTAINING PROTEIN 3; 1.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW   Protease {ECO:0000256|ARBA:ARBA00022807};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008144};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   DOMAIN          47..170
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..347
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   367 AA;  42115 MW;  544DB0463ABA234B CRC64;
     MSNRSRKNEE RSIRKAHQNN RKHKELSYFV DDENYAGFSN QLATLGLTLK DIPGDGNCLF
     RALADQLEGN SRRHLHHREE TVRYMVEHRA DFEPFVEDDC SFNDHVYKLR KDGTYAGNDA
     IVAFARNNGV NVVIHQLNAP MWTINGNERS RRQLHIAYHN GDHYSSVRKL TDDTDGPTNI
     KLTIQSKHEN KSTSGRRESK KKATASKRRT PTTQCMQCNV LTYYDIMLLF KCLCDNNQPL
     LQDPNISQWD SNVSPVDDDE SYQAQWNDHI WDHNGTGTRI FGNAGTNVQA TTNKTNISHP
     QKKQVTSIQT NPNTIPPQVS NKHRKEQARK ERKKRSDERK KNSSNRASPS DSDDSSILVK
     NIDILKI
//
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