ID   V9KA95_CALMI            Unreviewed;      1052 AA.
AC   V9KA95;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 48 {ECO:0000256|ARBA:ARBA00035173};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE   Flags: Fragment;
OS   Callorhinchus milii (Ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO95065.1};
RN   [1] {ECO:0000313|EMBL:AFO95065.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Ovary {ECO:0000313|EMBL:AFO95065.1};
RX   PubMed=24402279; DOI=10.1038/nature12826;
RG   International Elephant Shark Genome Sequencing Consortium;
RA   Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA   Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA   Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA   Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA   Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA   Wilson R.K., Brenner S., Warren W.C.;
RT   "Elephant shark genome provides unique insights into gnathostome
RT   evolution.";
RL   Nature 505:174-179(2014).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JW862548; AFO95065.1; -; mRNA.
DR   AlphaFoldDB; V9KA95; -.
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; 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; 2.
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   Hydrolase {ECO:0000313|EMBL:AFO95065.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          94..426
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          467..562
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          724..837
FT                   /note="DUSP"
FT                   /evidence="ECO:0000259|PROSITE:PS51283"
FT   DOMAIN          963..1019
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   REGION          621..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFO95065.1"
SQ   SEQUENCE   1052 AA;  120872 MW;  54DDC0ADAFB0C90A CRC64;
     RRSSDLAPKQ QLEKAAWQWA ESVRPEEVRR EHIELAYRVL LGSCRRDARR RNCRGNPNCL
     VGLGEHVWLG EIDENSFHNI DDPNSERRCK NTFVGLTNLG ATCYVNTLLQ VWFHNLELRQ
     ALYLCHSPRK EMGTGERIED DADFEPQSVC EHLQYLFALL QSSNRRYIDP SGFVKALGLD
     TGQQQDAQEF SKLFMSLLED TLSKQNNPDV QNIIQQQFCG QYAYVTVCNQ CGWESKLLSR
     FYELELNIQG HKQLTDCIEE FLKEEKLEGD NRYFCDKCQD KQNATRKIKL LNLPRTLNLQ
     LLRFVFDRQT GHKKKLNSYI SFPEVLDLSP YLERKDVSTV YELSAVLIHR GVSAYSGHYI
     AHVRDDRTGD WYKFNDEEIE KMEGKKLQLG IEEDLAEPSK SQTRKPKCVK GVHCSRNAYM
     LVYRRKGEMS KEKDISVQLP AHLQKMVERD NKKFEEWCME MAEMRKQSVD KGKAKHEEVQ
     ELFNMLPAKE DELYEFVPVD WLRKWLDDSA VTKPIDNSCN LCAHGGLNPD KICDVKRISQ
     KAADIFYARY GGGPRLDASA LCADCVMEKC RILRLKNQLN EDYKIISNLT RTTLQSLEGY
     WVGKTSLRSW RQLALDQLDG KDDDSDLADG KSNGEGLNNL HAKGDDEMTG EKDNEDMNFN
     EDLVCPHGDL CTSETERRLV SEETWKRLKA YFPKSPEFAH YHSPCVQCQV LEKEGEENET
     LSKMMANEQK SALLCLFQEK NRPILIKWPE ETDVLYIVSQ FFVEEWKKFI RKPTKCSPVS
     SVGNNALLCP HGGLMFTAES MTKEDSKHVA LIWPNEWEIL HKLFVVDNTI KVMRKTSIAE
     TGSVQVEYST SPGLCVECRE GLLCQQQRDL REYTQATIYI RKVVDNIKVM KEGAPELNMS
     GSEAEEEREE FKIEGEKDPD FNQSNGAKRR KLAHLCIGNT HSSVHYKPGI RRSTRHRVRG
     EKELLVSANQ TLKELKIQIM HAFSVAPFDQ NLSLEGRMLT DDTATLGNLG IIPESVILLK
     ADEPIADYTA MDDIMQVCMP EEGFKGTGLL GH
//