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