ID A0A3Q3B0N2_KRYMA Unreviewed; 522 AA.
AC A0A3Q3B0N2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000022440.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000022440.1}
RP IDENTIFICATION.
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,
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 AlphaFoldDB; A0A3Q3B0N2; -.
DR STRING; 37003.ENSKMAP00000022440; -.
DR Ensembl; ENSKMAT00000022725.1; ENSKMAP00000022440.1; ENSKMAG00000016617.1.
DR GeneTree; ENSGT00550000075075; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
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|ARBA:ARBA00022801, 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:UP000264800};
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..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..511
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 522 AA; 58859 MW; A7A8475F81C22D2E CRC64;
RANRMLWCRP ESSDKLVGEF LGTGPAIRNK MIKNWGVIGG IAAAIAAGVY VMWGPITERK
KRKRGMVPGL LNLGNTCFLN SLLQGLAACP SFIRWLEKFS GLPSIQSCKD NQLSTTLLQL
LKALSSDEPG DEDVLDAGCL LDVLRLYRWH ISSFEEQDAH ELFHVLTSSL EEERNRQPKV
THLFDVQSLE ASYPRTSSSP LHPIPDPWKF QHPFHGRLTS NMSCKHCEIQ SPVRYDSFES
LSLSILLPQW GRPISLDQCL QHFISSETIK EVECENCTKL QQSTTLNGQV FESQRTTFVK
QLKLGKLPQC LCIHLQRLTW SGEGTPIKRQ EHVEFAEFLS MDRYKHNSST QILRLKRAAK
APQAESLNDS TEKPKANGTG EFTKTAVCVP HIYFAFCRLA LTGPSFPDRD NNNKTFSNGT
CSSVFLRSPG FNPHVFPSSS TEYLFQLTAV LVHHGDMHSG HFVTYRRSPS SPRGSSAFSS
QWLWVSDDSV RKSSLHEVLS SNAYMLFYER VRRPSLSPCS DE
//
