JOS1_MOUSE
ID JOS1_MOUSE Reviewed; 202 AA.
AC Q9DBJ6; Q3U3E9;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Josephin-1;
DE EC=3.4.19.12;
DE AltName: Full=Josephin domain-containing protein 1;
GN Name=Josd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
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).
RN [3]
RP TISSUE SPECIFICITY, AND UBIQUITINATION.
RX PubMed=23625928; DOI=10.1074/jbc.m113.463406;
RA Seki T., Gong L., Williams A.J., Sakai N., Todi S.V., Paulson H.L.;
RT "JosD1, a membrane-targeted deubiquitinating enzyme, is activated by
RT ubiquitination and regulates membrane dynamics, cell motility, and
RT endocytosis.";
RL J. Biol. Chem. 288:17145-17155(2013).
RN [4]
RP 3D-STRUCTURE MODELING.
RX PubMed=12486728; DOI=10.1002/prot.10280;
RA Albrecht M., Hoffmann D., Evert B.O., Schmitt I., Wuellner U., Lengauer T.;
RT "Structural modeling of ataxin-3 reveals distant homology to adaptins.";
RL Proteins 50:355-370(2003).
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 -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC {ECO:0000269|PubMed:23625928}.
CC -!- PTM: Monoubiquitinated. Ubiquitination activates deubiquitination
CC activity in vitro. {ECO:0000269|PubMed:23625928}.
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DR EMBL; AK004913; BAB23664.1; -; mRNA.
DR EMBL; AK154799; BAE32837.1; -; mRNA.
DR EMBL; BC006928; AAH06928.1; -; mRNA.
DR EMBL; BC086769; AAH86769.1; -; mRNA.
DR CCDS; CCDS27647.1; -.
DR RefSeq; NP_083068.1; NM_028792.3.
DR RefSeq; XP_001481034.3; XM_001480984.6.
DR AlphaFoldDB; Q9DBJ6; -.
DR SMR; Q9DBJ6; -.
DR STRING; 10090.ENSMUSP00000023061; -.
DR MEROPS; C86.004; -.
DR iPTMnet; Q9DBJ6; -.
DR PhosphoSitePlus; Q9DBJ6; -.
DR EPD; Q9DBJ6; -.
DR MaxQB; Q9DBJ6; -.
DR PaxDb; Q9DBJ6; -.
DR PRIDE; Q9DBJ6; -.
DR ProteomicsDB; 269372; -.
DR Antibodypedia; 202; 95 antibodies from 16 providers.
DR Ensembl; ENSMUST00000023061; ENSMUSP00000023061; ENSMUSG00000022426.
DR GeneID; 74158; -.
DR KEGG; mmu:74158; -.
DR UCSC; uc007wue.2; mouse.
DR CTD; 9929; -.
DR MGI; MGI:1921408; Josd1.
DR VEuPathDB; HostDB:ENSMUSG00000022426; -.
DR eggNOG; KOG2934; Eukaryota.
DR GeneTree; ENSGT00390000009228; -.
DR HOGENOM; CLU_103892_0_0_1; -.
DR InParanoid; Q9DBJ6; -.
DR OMA; MSCMPWK; -.
DR OrthoDB; 1482722at2759; -.
DR PhylomeDB; Q9DBJ6; -.
DR TreeFam; TF313660; -.
DR Reactome; R-MMU-5689877; Josephin domain DUBs.
DR BioGRID-ORCS; 100043771; 0 hits in 1 CRISPR screen.
DR BioGRID-ORCS; 74158; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Josd1; mouse.
DR PRO; PR:Q9DBJ6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9DBJ6; protein.
DR Bgee; ENSMUSG00000022426; Expressed in lacrimal gland and 257 other tissues.
DR Genevisible; Q9DBJ6; MM.
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 1: Evidence at protein 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_0000053840"
FT DOMAIN 23..202
FT /note="Josephin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT REGION 1..22
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; 23152 MW; 8F04FB5C37529BF7 CRC64;
MSCVPWKGDK AKAESSDLPQ AAPPQIYHEK QRRELCALHA LNNVFQDSNA FTRETLQEIF
QRLSPNTMVT PHKKSMLGNG NYDVNVIMAA LQTKGYEAVW WDKRRDVGVI ALTNVMGFIM
NLPSSLCWGP LKLPLKRQHW ICVREVGGAY YNLDSKLKMP EWIGGESELR KFLKYHLRGK
NCELLLVVPE EVEAHQSWRA DV
