ID   JOS1_RAT                Reviewed;         202 AA.
AC   Q5BJY4;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Josephin-1;
DE            EC=3.4.19.12;
DE   AltName: Full=Josephin domain-containing protein 1;
GN   Name=Josd1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; BC091280; AAH91280.1; -; mRNA.
DR   RefSeq; NP_001020180.1; NM_001025009.1.
DR   AlphaFoldDB; Q5BJY4; -.
DR   SMR; Q5BJY4; -.
DR   STRING; 10116.ENSRNOP00000019612; -.
DR   MEROPS; C86.004; -.
DR   iPTMnet; Q5BJY4; -.
DR   PhosphoSitePlus; Q5BJY4; -.
DR   PaxDb; Q5BJY4; -.
DR   Ensembl; ENSRNOT00000019612; ENSRNOP00000019612; ENSRNOG00000014440.
DR   GeneID; 315134; -.
DR   KEGG; rno:315134; -.
DR   UCSC; RGD:1305388; rat.
DR   CTD; 9929; -.
DR   RGD; 1305388; Josd1.
DR   eggNOG; KOG2934; Eukaryota.
DR   GeneTree; ENSGT00390000009228; -.
DR   HOGENOM; CLU_103892_0_0_1; -.
DR   InParanoid; Q5BJY4; -.
DR   OMA; MSCMPWK; -.
DR   OrthoDB; 1482722at2759; -.
DR   PhylomeDB; Q5BJY4; -.
DR   TreeFam; TF313660; -.
DR   Reactome; R-RNO-5689877; Josephin domain DUBs.
DR   PRO; PR:Q5BJY4; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000014440; Expressed in colon and 20 other tissues.
DR   Genevisible; Q5BJY4; RN.
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; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
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_0000053842"
FT   DOMAIN          23..202
FT                   /note="Josephin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  23178 MW;  A4762D1C78E56623 CRC64;
     MSCMPWKGDK AKSESLELPQ AAPPQIYHEK QRRELCALHA LNNVFQDSNA FTRETLQEIF
     QRLSPNTVVT PHKKSMLGNG NYDVNVIMAA LQTKGYEAVW WDKRRDVGVI ALANVMGFIM
     NLPSSLCWGP LKLPLKRQHW ICVREVGGAY YNLDSKLKMP EWIGGESELR KFLKYHLRGK
     NCELLLVVPE EVEAHQSWRA DV