ID   JOS1_BOVIN              Reviewed;         202 AA.
AC   Q5EAE5; A5D797;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Josephin-1;
DE            EC=3.4.19.12;
DE   AltName: Full=Josephin domain-containing protein 1;
GN   Name=JOSD1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2007) 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; BT020624; AAX08641.1; -; mRNA.
DR   EMBL; BC140477; AAI40478.1; -; mRNA.
DR   RefSeq; NP_001014898.1; NM_001014898.2.
DR   RefSeq; XP_005207376.1; XM_005207319.2.
DR   RefSeq; XP_005207377.1; XM_005207320.3.
DR   AlphaFoldDB; Q5EAE5; -.
DR   SMR; Q5EAE5; -.
DR   STRING; 9913.ENSBTAP00000013418; -.
DR   MEROPS; C86.004; -.
DR   PaxDb; Q5EAE5; -.
DR   GeneID; 510781; -.
DR   KEGG; bta:510781; -.
DR   CTD; 9929; -.
DR   eggNOG; KOG2934; Eukaryota.
DR   HOGENOM; CLU_103892_0_0_1; -.
DR   InParanoid; Q5EAE5; -.
DR   OrthoDB; 1482722at2759; -.
DR   TreeFam; TF313660; -.
DR   Proteomes; UP000009136; Unplaced.
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_0000053838"
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;  23181 MW;  8681F2DB1EAF375C CRC64;
     MSCVPWKGDK VKSESLELPQ AAPPQIYHEK QRRELCALHA LNNVFQDSNA FTRETLQEIF
     QRLSPNTMVT PHKKSMLGNG NYDVNVIMAA LQTKGYEAVW WDKRRDVGAI ALTNVMGFIM
     NLPSSLCWGP LKLPLKRQHW ICVREVGGAY YNLDSKLKMP EWIGGKSELR KFLKHHLRGK
     NCELLLVVPE EVEAHQSWRA DV