GenomeNet

Database: UniProt
Entry: A0A452ERW3_CAPHI
LinkDB: A0A452ERW3_CAPHI
Original site: A0A452ERW3_CAPHI 
ID   A0A452ERW3_CAPHI        Unreviewed;      1152 AA.
AC   A0A452ERW3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Ubiquitin specific peptidase 25 {ECO:0000313|Ensembl:ENSCHIP00000014840.1};
GN   Name=USP25 {ECO:0000313|Ensembl:ENSCHIP00000014840.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000014840.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000014840.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000014840.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   EMBL; LWLT01000001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_017907986.1; XM_018052497.1.
DR   AlphaFoldDB; A0A452ERW3; -.
DR   STRING; 9925.ENSCHIP00000014840; -.
DR   Ensembl; ENSCHIT00000022639.1; ENSCHIP00000014840.1; ENSCHIG00000015678.1.
DR   GeneID; 102177278; -.
DR   CTD; 29761; -.
DR   GeneTree; ENSGT00940000157962; -.
DR   OrthoDB; 1423057at2759; -.
DR   Proteomes; UP000291000; Chromosome 1.
DR   Bgee; ENSCHIG00000015678; Expressed in longissimus thoracis muscle and 16 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:Ensembl.
DR   GO; GO:0032183; F:SUMO binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:1904293; P:negative regulation of ERAD pathway; IEA:Ensembl.
DR   CDD; cd02665; Peptidase_C19I; 1.
DR   CDD; cd14354; UBA_UBP25; 1.
DR   CDD; cd20486; USP25_C; 1.
DR   Gene3D; 6.10.250.1720; -; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF666; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 25; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02809; UIM; 2.
DR   SMART; SM00726; UIM; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50330; UIM; 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:UP000291000};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          197..685
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          492..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          714..741
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        500..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..765
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..819
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1152 AA;  133252 MW;  CC82809C23D9B884 CRC64;
     MTVEQNVLQQ SAAQKHQQTF LNQLREITGI NDAQILQQAL KDSNGNLELA VAFLTAKNAK
     TPQQEETTYY QTALPGNDRY ISVGSQADTR KKQYMPTRTR CATIEQSKYG SKDKRDLDVI
     DLTGDDKDDL QRAIALSLAE SNRAFRETGI TDEEQAISRV LEASIAENKE CLKRTPTEVW
     RDSRNPYDRK RQDKAPVGLK NVGNTCWFSA VIQSLFNLLE FRRLVLNYKP PSNVQDLPRN
     QKEHRNLPFM RELRYLFALL VGTKRKYVDP SRAVEILKDA FKSNDSQQQD VSEFTHKLLD
     WLEDAFQMKA EEETDEDKPK NPMVELFYGR FLAVGVLEGK KFENTEMFGQ YPLQVNGFKD
     LHECLEAAMI EGEIESLHSE NSGKSGQEHW FTELPPVLTF ELSRFEFNQA LGRPEKIHNK
     LEFPQVLYLD RYMHRNREIT RIKREEIKRL KDYLTVLQQR LERYLSYGSG PKRFPLVDVL
     QYALEFASSK PVCTSPVDDI DASSPPSGSV PSQTLPSTTD QQGAPSSELP STSPASIAAI
     SSRSVIHKPF TQSRIPPDLP MHPAPRHITE EELSVLESCL HRWRTEIEND TRDLQESISR
     IHRTIDLMYS DKSMIQVPYR LHAVLVHEGQ ANAGHYWAYI FDHRENRWMK YNDIAVTKSS
     WEELVRDSFG GYRNASAYCL MYINDKPQFL IQEEFNKETG QALAGIETLP PDLRDFVEED
     NQRFEKELEE WDAQLAQKAL QEKLLASQKL RESESSVTTA QAGEPEYLEQ PSRSDFSKHL
     KEETIRIITK ASHEHEDKSP ETVLQSKPEN TTSQPPSKQQ VVEVEIPHVG TFMIESKEGG
     YDDEIMMTPN MQGIIMAIGK SRSVYDRCGP EAGFFKAIKL EYSRLVKLAQ EDTPPETDYR
     LHHVIVYFIQ NQAPKKIIEK TLLEQFADRN LSFDERCHNI MKVAQAKIEM IKPEEVNMEE
     YEEWHQDYRK FRETTMYLII GLENFQRESY IDSLLFLICA YQNNKELLSK GPYRGHDEEL
     ISHYRRECLL KLNEQAAELF ESGEDREVNN GLIIMNEFIV PFLPLLLVDE MEEKDILAVE
     DMRNRWCSYL GQEMESNLQE KLTDFLPKLL DCSTEVKGFH EPPKLPPYST HELCERFTRI
     MLSLSRTPAD GR
//
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