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Database: UniProt
Entry: W5Q6F3_SHEEP
LinkDB: W5Q6F3_SHEEP
Original site: W5Q6F3_SHEEP 
ID   W5Q6F3_SHEEP            Unreviewed;       517 AA.
AC   W5Q6F3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   Name=USP30 {ECO:0000313|Ensembl:ENSOARP00000018293.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000018293.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000018293.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000018293.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000018293.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC       from specific proteins to regulate different cellular processes.
CC       {ECO:0000256|RuleBase:RU366025}.
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         ECO:0000256|RuleBase:RU366025};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR   EMBL; AMGL01039637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01039638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01039639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004017487.1; XM_004017438.3.
DR   AlphaFoldDB; W5Q6F3; -.
DR   SMR; W5Q6F3; -.
DR   STRING; 9940.ENSOARP00000018293; -.
DR   PaxDb; 9940-ENSOARP00000018293; -.
DR   Ensembl; ENSOART00000018554.1; ENSOARP00000018293.1; ENSOARG00000017038.1.
DR   GeneID; 101123665; -.
DR   KEGG; oas:101123665; -.
DR   CTD; 84749; -.
DR   eggNOG; KOG1867; Eukaryota.
DR   HOGENOM; CLU_008279_14_2_1; -.
DR   OMA; CEREGND; -.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000002356; Chromosome 17.
DR   Bgee; ENSOARG00000017038; Expressed in pituitary gland and 52 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02662; Peptidase_C19F; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF650; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 30; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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|RuleBase:RU366025};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU366025}.
FT   TRANSMEM        35..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          68..502
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   517 AA;  58189 MW;  31DF50E1AFEFBF40 CRC64;
     MLSSRASAAM TAADRAIQRF LRTGAAVRYK VMKNWGVIGG IAAALAAGIY VIWGPITERK
     KRRKGLVPGL VNLGNTCFMN SLLQGLSACP TFIKWLEEFT TQYTGSHKEP PQHQYLSLTL
     LHLLKALSCQ EVTDEEVLDA SCLLDVLRMY RWQISSFEEQ DAHELFHVIT SSLEDERDRQ
     PRVTHLFDVH SLEQQTEITP RQITCRTRGS PHPASNHWKS QHPFHGRLTS NMVCKHCEHQ
     SPVRFDTFDS LSLSIPAATW GHPLTLDHCL HHFISSESVR DVVCDNCTKI EAKGTLNGEK
     VEHQRTTFVK QLKLGKLPQC LCIHLQRLSW SSQGTPLKRH EHVQFGEFLM MDIYKYHLLG
     HKPGHRGPER CEKAGPALEL QDGPAAPKSV RNHPGGPKTQ IFMNGACSPS LLPALPTPMP
     FPLPAVPDYS SSTYLFQLMA VVVHHGDMHS GHFVTYRRSP PSAKNPVSAS SQWLWVSDDT
     VRKASLQEVL SSSAYLLFYE RVLSKVQPQG REYKSEE
//
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