ID A0A2Y9K964_ENHLU Unreviewed; 1036 AA.
AC A0A2Y9K964;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 48 {ECO:0000256|ARBA:ARBA00035173};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=LOC111154599 {ECO:0000313|RefSeq:XP_022369981.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022369981.1};
RN [1] {ECO:0000313|RefSeq:XP_022369981.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022369981.1};
RG RefSeq;
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_022369981.1; XM_022514273.1.
DR AlphaFoldDB; A0A2Y9K964; -.
DR STRING; 391180.A0A2Y9K964; -.
DR KEGG; elk:111154599; -.
DR OrthoDB; 307371at2759; -.
DR Proteomes; UP000248482; Unplaced.
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 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; PF00443; UCH; 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:0000313|RefSeq:XP_022369981.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 89..421
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 460..554
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 930..1003
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT REGION 613..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1036 AA; 119209 MW; 503EE6EE31EFDC0B CRC64;
MAPRLQLEKA AWRWAETVRP EEVSQEHIET AYRIWLEPCI RGVCRRNCKG NPNCLVGIGE
HIWLGEIDEN SFHNIDDPNC ERRKKNSFVG LTNLGATCYV NTFLQVWFLN LELRQALYLC
PSTCNDYMMG DGIQEEKDYE PQTICEHLQY LFALLQNSNR RYIDPSGFVK ALGLDTGQQQ
DAQEFSKLFM SLLEDTLSKQ KNPDVRNIVQ QQFCGEYAYV TVCNQCGRES KLLSKFYELE
LNIQGHKQLT DCISEFLKEE KLEGDNRYFC ENCQSKQNAT RKIRLLSLPC TLNLQLMRFV
FDRQTGHKKK LNTYIGFSEI LDMEPYVEHK GGSYVYELSA VLIHRGVSAY SGHYIAHVKD
PQSGEWYKFN DEDIEKMEGK KLQLGIEEDL AEPSKSQTRK PKCGKGTHCS RNAYMLVYRL
QTQEKPTTAV QVPAFLQELV DRDNSKFEEW CIEMAEMRKQ SVDKGKAKHE EVKELYQRLP
AGAEPYEFVS LEWLQKWLDE STPTKPIDNH ACLCSHDKLH PDKISIMKRI SEYAADIFYS
RYGGGPRLTV KALCKECVVE RCRVLRLKSQ LNEDYKTVNN LLKATVKGSD GFWVGKSSLR
SWRQLALEQL DEQDGDVDQS NGKMNGNTLN KDESKEERKE EEEELNFNED ILCPHGELCI
SENERRLVSK EAWSKLQQYF PKAPEFPSYR ECCSQCKILE REGEENEALH KMIANEQKTS
LPNLFQDKNR PCLSNWPEET DVLYIVSQFF VEEWRKFVRK PTRCSPVSSV GNSALLCPHG
GLMFTFASMT KEDSKLIALI WPSEWQMIQK LFVVDHVIKI TRTEVGDANP SETQYISEPK
LCPECREGLL CQQQRDLREY TQATIYVHKV VDNKKVMKDS APELNVSSSE TEEDKEEAKP
DGEKDPDFNQ SNGGTKRQKI THQNYIAYQK QVIRRSMRHR KVRGEKALLV SANQTLKELK
IQIMHAFSVA PFDQNLSIDG KILSDDCATL GTLGVIPESV ILLKADEPIA DYAAMDDVMQ
VCMPEEGFKG TGLLGH
//
