ID   V9LBB0_CALMI            Unreviewed;       235 AA.
AC   V9LBB0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Ataxin-3 {ECO:0000313|EMBL:AFP09102.1};
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:AFP09102.1};
RN   [1] {ECO:0000313|EMBL:AFP09102.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Gills {ECO:0000313|EMBL:AFP09102.1};
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};
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DR   EMBL; JW876585; AFP09102.1; -; mRNA.
DR   AlphaFoldDB; V9LBB0; -.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   InterPro; IPR033865; Ataxin-3.
DR   InterPro; IPR003903; UIM_dom.
DR   PANTHER; PTHR14159; ATAXIN-3-RELATED; 1.
DR   PANTHER; PTHR14159:SF0; ATAXIN-3-RELATED; 1.
DR   Pfam; PF16619; SUIM_assoc; 1.
DR   Pfam; PF02809; UIM; 2.
DR   PRINTS; PR01233; JOSEPHIN.
DR   SMART; SM00726; UIM; 2.
DR   PROSITE; PS50330; UIM; 1.
PE   2: Evidence at transcript level;
FT   REGION          68..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFP09102.1"
SQ   SEQUENCE   235 AA;  25967 MW;  903AD08A368B8446 CRC64;
     SGKAVIANIC RVTFVCAVDK VVKRGALCEV CFVSAGYSIF VLRGDLPECE ADELLKIMRV
     VQQERPKLIG EEGTQRTQTE SSPSVQNSDW EQTIDASKSV TSVVDEDDEN LQRALSLSRQ
     HMETEDEEAD LRRAIHLSMQ GFGQGTEITE VTSNDVAQSS GINQISPEEL RRRRQDYFEK
     KQPCAQPSNS NQPEKPGCTA LRVNSASVTE RETPQADVNK SLDTDANDNS KEKGS
//