ID F7A912_CIOIN Unreviewed; 1072 AA.
AC F7A912;
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=Ubiquitinyl hydrolase 1 {ECO:0008006|Google:ProtNLM};
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:ENSCINP00000023650.2, 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:ENSCINP00000023650.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; EAAA01000275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F7A912; -.
DR STRING; 7719.ENSCINP00000023650; -.
DR Ensembl; ENSCINT00000023896.2; ENSCINP00000023650.2; ENSCING00000000779.3.
DR GeneTree; ENSGT00940000160441; -.
DR HOGENOM; CLU_009980_0_0_1; -.
DR InParanoid; F7A912; -.
DR OMA; TCNKESA; -.
DR TreeFam; TF106277; -.
DR Proteomes; UP000008144; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR015063; USP8_dimer.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF104; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000008144}.
FT DOMAIN 177..298
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 746..1072
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 372..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 100..127
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 526..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 120767 MW; 9705491CA915FF03 CRC64;
RNFTMAKPKD LYIAKSLKDL NKHTDSKCEK GRSIKIYLNF ANKAFAEAEK AFKSRDEERA
YILYMKYLDM VGIVRKCPEF KKDTQHYSLL LGKMNTITAL ENAEATSNSL KKRYDALAKK
AAEAEMKQVE GKIKQNGAVE EFSHPVPDEE KVTETPEKET FGNEVNSAKL YELIYKKSKD
VLILDIRSSE DFQMSHVQHS ICANVPKAAI QPGTVVSKIE EGIAPSDMEM WNKRDSVDLV
VLLDWTSSVK RLQDKGDPLR SLKDAIWKWN QDKILQHEPV VLEGGFSDWL EFYPQFTTNP
KAKVPKANVK TLNVNSLLEF SYSDLNTNFV KPKPPPENVN VPNSIPITIA QTNPPKQVSV
SNTILKLVTP ASEPVETPLP QKKKPQPMFD RSKKPSPAPA VHPSVPKPES QFKKNGESPK
NEMEVVKPSP PSKVKSKDVD NDAIFSEYEQ RIALMVKQKE EKENAIVEIE KKKKVAELQA
LEKKLKEEAE ETEKRKMEAE RQLAMTMRDL SKPKPITNNM EKPLVIEPPN KKDDAPINKD
MSPEPIYAEV KKTKIPKETP GNNKAKQKAP KPERPTAEKP DVSIPSKSVA SPVDQSKSTT
VSSQHETQVK PKLSQSAPAI SKPVDPIKPT TNQSTTKDVA IKQNKDQEKT VPPKPQEVKP
ISRKPTLSTG LNPNSDKGGF ALKRSSSSPN INKLVEEESK VVSTSTMPSI PDRERKPSIR
PGPSELVTAL THSLRGVYGG KGRGLCGLRN LGNSCYMNSV LQCMFNMTQL AEYILTDSYT
KDLNRANKIG HGGRVAESFS VLLRAVWSSK YEYIVPSDFK SIIGTINSSF AGYTQEDSQE
FLMLLLDGLH EDLNKAPQSE YKEEPDNDAL DDEEAAQMAW KYHKKRNESI IVELLKGQFK
ATVKCLHCGK ASRKFDPFMY LSLPLPNKSA SIYDILKSFQ RVEQMTGSDR WHCPNCKTLR
DAVRSIEIWK LPPVLIIHFK RFVHTGRWRD KIHTNISYPM TQLDLTPFIS GKQRRPKYNL
FAVSHHQGAG LDSGHYTASC KSVLDNNWYK FDDTEVMRTS APQGPTASIL FY
//
