ID V9LBH0_CALMI Unreviewed; 270 AA.
AC V9LBH0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE AltName: Full=Deubiquitinating enzyme A {ECO:0000256|ARBA:ARBA00033460};
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:AFP09602.1};
RN [1] {ECO:0000313|EMBL:AFP09602.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Kidney {ECO:0000313|EMBL:AFP09602.1};
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 -!- SIMILARITY: Belongs to the peptidase C85 family.
CC {ECO:0000256|ARBA:ARBA00010407}.
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DR EMBL; JW877085; AFP09602.1; -; mRNA.
DR AlphaFoldDB; V9LBH0; -.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR CDD; cd22752; OTU_OTUD5-like; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12419:SF4; OTU DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50802; OTU; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 44..173
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFP09602.1"
FT NON_TER 270
FT /evidence="ECO:0000313|EMBL:AFP09602.1"
SQ SEQUENCE 270 AA; 31017 MW; 735B72935B113EEB CRC64;
RRSSDLNSED EYETPGREQQ HQDPAQLQQQ EHWFEKALSE KKGFVIKRMK EDGACLFRAV
ADQVYGDQDM HDVVRKHCMD YLVKNADYFS NYVTEDFTTY INRKRMSSCH GNHIEMQAMA
EMYNRPVEVY QYSPGREDSL EPINTFHGIH QTEDEPIRVS YHRNVHYNSV VNPNKATIGV
GLGLPAFKPG AADQSLMKSA IKTSEESWIE QQMLEDKKRA TDWEATNEAI EEQVARESYL
QWLRDQEKQA KQPRKATATC SSATAAAASG
//
