ID L5KFN9_PTEAL Unreviewed; 706 AA.
AC L5KFN9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-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 ORFNames=PAL_GLEAN10015526 {ECO:0000313|EMBL:ELK10365.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK10365.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 -!- SIMILARITY: Belongs to the peptidase C19 family. USP44 subfamily.
CC {ECO:0000256|ARBA:ARBA00038113}.
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DR EMBL; KB030754; ELK10365.1; -; Genomic_DNA.
DR AlphaFoldDB; L5KFN9; -.
DR STRING; 9402.L5KFN9; -.
DR MEROPS; C19.057; -.
DR eggNOG; KOG1867; Eukaryota.
DR InParanoid; L5KFN9; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF15; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 44; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 2..99
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 269..674
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 686..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..203
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 706 AA; 80942 MW; F384C52BA71BD54D CRC64;
MDKCKHIEQL RLAQDHSILN PQKWHCVDCN TTESIWACLS CSHVACGRYI EEHALKHFQE
SSHPVALEVN EMYVFCYLCD DYVLNDNATG DLKLLRSTLS AIKSQSYYCT TRSGRVLRSI
GISDDSYFLN DGAQSLLQNE DQMYTALWHR RRILMGKIFR IWFEQSPIGR KRQEEQFQEK
TEKREVKKRR QELEHQVKAE LESMPPRKSL RLQGQVQSTT VEIVPVQEPL QTSASPAKDD
VVSTSEDVKF KKASDSSVKQ RPIVTPGVTG LRNLGNTCYM NSVLQVLSHL LIFRQCFLKL
DLNRWLAVTA SDKTRSSYKH PPVTDTLYRM NECQEKDTGS VFSRHPSLSS RLTGGVSKSR
KMELIQLRES SSQYISLCHE LHTLFQVMWS GKWALVSPFA MLHSVWRLIP AFRGYAQQDA
QEFLCELLDK IQHELETTGT RLPALIPISQ RKLIKQVLNV VNNIFHGQLL SQVTCLACDN
KSNTIEPFWD LSLEFPERYQ CSGKDTASQP CLVTEMLAKF TETEALEGKI YVCDQCNSKR
RRFSTKPVVL TEAQKQLMIC HLPQVLRLHL KRFRWSGRNN REKIGVHVGF EEILNMEPYC
CMESLKALRP ECFIYDLSAV VMHHGKGFGS GHYTAYCFNS EGGFWVHCND SKLSMCTMDE
VCKAQAYILF YTQRVTENGH SKLLPPELLS GSLPPNEEAD TSEILS
//
