ID   A0A1D5P1U8_CHICK        Unreviewed;      1033 AA.
AC   A0A1D5P1U8;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 48 {ECO:0000256|ARBA:ARBA00035173};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   Name=USP48 {ECO:0000313|Ensembl:ENSGALP00010026204.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010026204.1, ECO:0000313|Proteomes:UP000000539};
RN   [1] {ECO:0000313|Ensembl:ENSGALP00010026204.1}
RP   IDENTIFICATION.
RC   STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010026204.1};
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_015152742.1; XM_015297256.1.
DR   AlphaFoldDB; A0A1D5P1U8; -.
DR   Ensembl; ENSGALT00010044085.1; ENSGALP00010026204.1; ENSGALG00010018251.1.
DR   VEuPathDB; HostDB:geneid_769457; -.
DR   GeneTree; ENSGT00940000156015; -.
DR   OrthoDB; 307371at2759; -.
DR   Proteomes; UP000000539; Chromosome 21.
DR   Bgee; ENSGALG00000030857; Expressed in lung and 12 other cell types or tissues.
DR   ExpressionAtlas; A0A1D5P1U8; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02668; Peptidase_C19L; 1.
DR   CDD; cd01795; Ubl_USP48; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.2230.10; DUSP-like; 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR044743; Ubl_USP48.
DR   InterPro; IPR033841; USP48.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF722; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 48; 1.
DR   Pfam; PF06337; DUSP; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
SQ   SEQUENCE   1033 AA;  118763 MW;  0D6A7F6AACD8E1C3 CRC64;
     MAPRLQLEKA AWRWTETVPP EAVTQEHIEA AYRVGLEPCQ RGTCRRNCRG NPNCLVGIGE
     HVWLGEIDEN SFHNIDDPNC ERRKKNAFVG LTNLGATCYV NTFLQMWFLN LELRQALYLC
     SSNEHAAGES IPKDKDYEPQ TICEHLQYLF ALLQNSKRRY IDPSGFVKAL GLDTGQQQDA
     QEFSKLFMSL LEDTLSKQKN PDVRNIVQKQ FCGEYAYVTV CNQCGRESKL VSKFYELELN
     IQGHKQLTDC ITEFLKEEKL EGDNRYFCET CQSKQNATRK IRLLSLPCTL NLQLMRFVFD
     RQTGHKKKLN TYIGFSELLD MEPFMEQKNG VYVYELSAVL IHRGVSAYSG HYIAHVKDPQ
     TGEWYKFNDE DIEKMEGKKL QLGIEEDLAE PSKSQTRKPK CGKGTHCSRN AYMLVYRLQT
     REKSLTVEVP AFLQELVERD NCKFEEWCNE MAEMRKQSVA RGKIKHEEVK ELYQRLPAEA
     GSPYDFISLE WLQKWLDEST PPKPIDNTAC LCSHGKLHPD KICIMKRISE YVADFFYRRY
     GGGPRLNVKA LCKDCVVERC RILRLKNQLN EDYKTVTNLL KITVKGSEGF WVGKASLRSW
     RQLALEQLNE QDEDAEHSNG KLNGNAPNKD EVNEEKREEE EELNFNEDIV CPHGDLCISE
     NERRVVSKEA WKKLKQYFPK APEFPSNKEC CSQCKILERE GEENEALHKM MASEQKTSLQ
     NLFHDKCRPC LGSWPQETDE LYIVSQFFVE EWRKFVRRPT RCSPVSSLGN SALLCPHGGL
     MFTYASMTKE DSKLIALIWP SEWERIQKLF VVDHVIKITR TRAAGEPESA LYSSEPQLCP
     ECREGLLCQQ QRDLREYTQA TIYIHKVVDN KKVMKDAAPE LNVSSSEAEE EREENKPEGE
     QDPDFNQSNG GAKRQKLSHQ SYISYQKQGI RRSTRHRKVR GEKALLVSAN QTLKELKIQI
     MHAFSVAPFD QNLLIDGKIL SDDTATLGSL GIIPESVILL KADEPIADYA AMDDVMQVCM
     PEEGFKGTGL LGH
//