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JOS1_PONAB
ID   JOS1_PONAB              Reviewed;         202 AA.
AC   Q5R739;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Josephin-1;
DE            EC=3.4.19.12;
DE   AltName: Full=Josephin domain-containing protein 1;
GN   Name=JOSD1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Deubiquitinates monoubiquitinated probes (in vitro). When
CC       ubiquitinated, cleaves 'Lys-63'-linked and 'Lys-48'-linked poly-
CC       ubiquitin chains (in vitro), hence may act as a deubiquitinating
CC       enzyme. May increase macropinocytosis and suppress clathrin- and
CC       caveolae-mediated endocytosis. May enhance membrane dynamics and cell
CC       motility independently of its catalytic activity (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   -!- SUBUNIT: Interacts with beta-actin/ACTB. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Note=Ubiquitination increases localization the plasma
CC       membrane. In the cytosol, the unubiquitinated form may be associated
CC       with the cytoskeleton via ACTB-binding. {ECO:0000250}.
CC   -!- PTM: Monoubiquitinated. Ubiquitination activates deubiquitination
CC       activity in vitro. {ECO:0000250}.
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DR   EMBL; CR860279; CAH92421.1; -; mRNA.
DR   RefSeq; NP_001126428.1; NM_001132956.1.
DR   AlphaFoldDB; Q5R739; -.
DR   SMR; Q5R739; -.
DR   STRING; 9601.ENSPPYP00000013191; -.
DR   MEROPS; C86.004; -.
DR   Ensembl; ENSPPYT00000013729; ENSPPYP00000013191; ENSPPYG00000011826.
DR   GeneID; 100173411; -.
DR   KEGG; pon:100173411; -.
DR   CTD; 9929; -.
DR   eggNOG; KOG2934; Eukaryota.
DR   GeneTree; ENSGT00390000009228; -.
DR   HOGENOM; CLU_103892_0_0_1; -.
DR   InParanoid; Q5R739; -.
DR   OrthoDB; 1482722at2759; -.
DR   Proteomes; UP000001595; Chromosome 22.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   InterPro; IPR040053; JOSD1/2.
DR   InterPro; IPR006155; Josephin.
DR   PANTHER; PTHR13291; PTHR13291; 1.
DR   Pfam; PF02099; Josephin; 1.
DR   SMART; SM01246; Josephin; 1.
DR   PROSITE; PS50957; JOSEPHIN; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Hydrolase; Membrane; Phosphoprotein; Protease;
KW   Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN           1..202
FT                   /note="Josephin-1"
FT                   /id="PRO_0000053841"
FT   DOMAIN          23..202
FT                   /note="Josephin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT   ACT_SITE        36
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15040"
SQ   SEQUENCE   202 AA;  23198 MW;  837268C393C0A5A9 CRC64;
     MSCVPWKGDK AKSESLELPQ AAPPQIYHEK QRRELCALHA LNNVFQDSNA FTRDTLQEIF
     QRLSPNTMVT PHKKSMLGNG NYDVNVIMAA LQTKGYEAVW WDKRRDVGVI ALTNVMGFIM
     NLPSSLCWGP LKLPLKRQHW ICVREVGGAY YNLDSKLKMP EWIGGESELR KFLKHHLRGK
     NCELLLVVPE EVEAHQSWRT DV
 
 
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