UBP48_CHICK
ID UBP48_CHICK Reviewed; 1033 AA.
AC Q5ZM45;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 48;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 48;
DE AltName: Full=Ubiquitin thioesterase 48;
DE AltName: Full=Ubiquitin-specific-processing protease 48;
GN Name=USP48; ORFNames=RCJMB04_3d5;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC precursors as well as that of ubiquitinated proteins (By similarity).
CC {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AJ719539; CAG31198.1; -; mRNA.
DR RefSeq; NP_001073211.1; NM_001079743.1.
DR AlphaFoldDB; Q5ZM45; -.
DR SMR; Q5ZM45; -.
DR STRING; 9031.ENSGALP00000022836; -.
DR MEROPS; C19.068; -.
DR PaxDb; Q5ZM45; -.
DR GeneID; 769457; -.
DR KEGG; gga:769457; -.
DR CTD; 84196; -.
DR VEuPathDB; HostDB:geneid_769457; -.
DR eggNOG; KOG1863; Eukaryota.
DR InParanoid; Q5ZM45; -.
DR OrthoDB; 113272at2759; -.
DR PhylomeDB; Q5ZM45; -.
DR PRO; PR:Q5ZM45; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02668; Peptidase_C19L; 1.
DR CDD; cd01795; Ubl_USP48; 1.
DR Gene3D; 3.30.2230.10; -; 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 Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF143791; SSF143791; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS51283; DUSP; 3.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Nucleus; Protease; Reference proteome; Repeat;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1033
FT /note="Ubiquitin carboxyl-terminal hydrolase 48"
FT /id="PRO_0000249526"
FT DOMAIN 89..419
FT /note="USP"
FT DOMAIN 457..552
FT /note="DUSP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 567..690
FT /note="DUSP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 710..823
FT /note="DUSP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 931..1007
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 610..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 1033 AA; 118691 MW; 55E1960AAFB983C2 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
ECRGGLLCQQ QRDLREYTQA TIYIHKVVDN KKVMKDAAPE LNVSSSEAEE EREENKPEGE
QDPDFNQSNG GAKRQKLSHQ SYISYQKQGI RRSTRHRKVR GEKALLVSAN QTLKELKIQI
MHAFSVAPFD QNLLIDGKIL SDDTATLGSL GIIPESVILL KADEPIADYA AMDDVMQVCM
PEEGFKGTGL LGH
