ID H0VFU2_CAVPO Unreviewed; 1355 AA.
AC H0VFU2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=USP19 {ECO:0000313|Ensembl:ENSCPOP00000008953.3};
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:ENSCPOP00000008953.3, 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:ENSCPOP00000008953.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000008953.3};
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};
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DR EMBL; AAKN02012891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 10141.ENSCPOP00000008953; -.
DR Ensembl; ENSCPOT00000010065.3; ENSCPOP00000008953.3; ENSCPOG00000009975.4.
DR VEuPathDB; HostDB:ENSCPOG00000009975; -.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000159085; -.
DR HOGENOM; CLU_001060_8_1_1; -.
DR InParanoid; H0VFU2; -.
DR OMA; RIWPQRV; -.
DR TreeFam; TF106276; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000009975; Expressed in cerebellum and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:Ensembl.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:1900037; P:regulation of cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:1904292; P:regulation of ERAD pathway; IEA:Ensembl.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:Ensembl.
DR CDD; cd06466; p23_CS_SGT1_like; 1.
DR CDD; cd06463; p23_like; 1.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 2.60.40.790; -; 2.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF74; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 19; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16602; USP19_linker; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 2.
DR PROSITE; PS51203; CS; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT TRANSMEM 1328..1349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..140
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 320..422
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 537..1251
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 831..873
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1255..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1355 AA; 150119 MW; 517868A9785E5879 CRC64;
MSGGASATGS RRGTPGLEEA TSKKKQKDRA NQESKDGDPR RVSTPREEQI KEELLLDWRQ
SADEVIIKLR VGTGPLRLEE VDAAFTDTDC VVRFPGGQQW GGVFYAEIES SCTKVQARKG
GLLQLALPKK VPLLTWPSLL KPLETQELAT GLWSQENGQE LSPVALEPGP EPRRAKQEAR
NQKRAQGRGE VGSGAGPGVQ AGPSAKRAVH LRRGPEGERS RDGPGPQGDA PSFLADPDTQ
VEAKEHLHVP PLNPKTCLLG SETNLALLSG EKAVFPRNDT VSSAISQVRD PGKDGCVKED
MAGAANVTDL ADEPESMVNL AFVKNDSYEK GPDSVVVHVY VKEIQRDTSR VLFREQDFTL
IFQTRDGNFL RLHPGCGPHT IFRWQVKLRN LIEPEQCTFC FTTSRIDICL HKRQSQRWGG
LEAPAARGAV GGAKVAVPTG PTPLESAPPG GPPHPLTGQE EARTVEKDKA KARSEDVGLD
SMAVRTPLEH VSTKPEPHLA SPKPTCMVPP MPHSPVSGDS VEEEEEEEKK VCLPGFTGLV
NLGNTCFMNS VIQSLSNTRE LRDFFHDRSF EAEINYNNPL GTGGRLAIGF AVLLRALWKG
THHAFQPSKL KAIVASKASQ FTGYAQHDAQ EFMAFLLDGL HEDLNRIQNK PYTETVDSDG
RPDEVVAAEA WQRHKMRNDS FIVDLFQGQY KSKLVCPVCA KVSITFDPFL YLPVPLPQKQ
KVLPIFYFAR EPHCKPIKFL VSVSKENSSA SEVLDSLSQS VHVKPENLRL AEVIKNRFHR
VFLPSQSLDT VSPSDTLLCF ELLSPELAKE RVVVLEVQQR PQVPSIPISK CAACQRKQQS
EDEKLKRCTR CYRVGYCNQL CQKSHWPDHK GLCRPENIGY PFLVSVPASR LTYARLTQLL
EGYARYSVSV FQPPFQPGRM ALESQSPGCT TLLSTSSLEA GDSEREPSQS PELQLVAEGD
TGVPRLWAAP DRGPVTSTSG ISSEMLTSGP TESSSLPVGE RVSRPEAAVH GYQHPSEAIN
AHTPQFFIYK IDASNREQRL EDKGETPLEL GEDCSLALVW RNNERLQEFV LVASKELECA
EDPGSAGEAA RAGHFTLDQC LNLFTRPEVL APEEAWYCPQ CKLHREASKQ LLLWRLPNVL
IVQLKRFSFR SFIWRDKIND LVEFPVRNLD LSKFCIGQKE EQLPSYDLYA VINHYGGMIG
GHYTACARLP NDRSSQRSDV GWRLFDDSTV TTVDESQVVT RYAYVLFYRR RNSPVERPPR
AGHSEHHPDL DPAAEAAASQ ASRIWQELEA EEELVPEGPG PMGPWGPQDW VGPPPRGPTT
PDEGCLRYFV LGTVAALVAL VLNVFYPLVS QSRWR
//
