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TM158_MOUSE
ID   TM158_MOUSE             Reviewed;         286 AA.
AC   Q6F5E0;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Transmembrane protein 158;
DE   AltName: Full=40 kDa BINP-binding protein;
DE            Short=p40BBP;
DE   AltName: Full=Ras-induced senescence protein 1;
DE   Flags: Precursor;
GN   Name=Tmem158; Synonyms=Mbbp, Ris1;
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 [MRNA].
RA   Hama A., Honda H.;
RT   "p40BBP, BINP-binding protein.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16964279; DOI=10.1038/sj.onc.1209978;
RA   Nieto M., Barradas M., Criado L.M., Flores J.M., Serrano M., Llano E.;
RT   "Normal cellular senescence and cancer susceptibility in mice genetically
RT   deficient in Ras-induced senescence-1 (Ris1).";
RL   Oncogene 26:1673-1680(2007).
CC   -!- FUNCTION: Receptor for brain injury-derived neurotrophic peptide
CC       (BINP), a synthetic 13-mer peptide. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q6F5E0; P09055: Itgb1; NbExp=3; IntAct=EBI-645317, EBI-644224;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Brain is the major site of
CC       expression. {ECO:0000269|PubMed:16964279}.
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed at day 9.5 dpc, with high
CC       levels in the endoderm, down-regulated at day 10.5 dpc, and expressed
CC       again at day 11.5 dpc, with high levels in the brain and neural tube.
CC       Then levels increase steadily until day 14.5 dpc.
CC       {ECO:0000269|PubMed:16964279}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TMEM158 family. {ECO:0000305}.
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DR   EMBL; AB114272; BAD27475.1; -; mRNA.
DR   CCDS; CCDS23658.1; -.
DR   AlphaFoldDB; Q6F5E0; -.
DR   IntAct; Q6F5E0; 1.
DR   STRING; 10090.ENSMUSP00000069161; -.
DR   GlyConnect; 2790; 1 N-Linked glycan (1 site).
DR   GlyGen; Q6F5E0; 1 site, 1 N-linked glycan (1 site).
DR   PhosphoSitePlus; Q6F5E0; -.
DR   PaxDb; Q6F5E0; -.
DR   PRIDE; Q6F5E0; -.
DR   ProteomicsDB; 259463; -.
DR   MGI; MGI:1919559; Tmem158.
DR   eggNOG; ENOG502RYJ7; Eukaryota.
DR   InParanoid; Q6F5E0; -.
DR   PhylomeDB; Q6F5E0; -.
DR   ChiTaRS; Mrvi1; mouse.
DR   PRO; PR:Q6F5E0; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q6F5E0; protein.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042277; F:peptide binding; ISO:MGI.
DR   InterPro; IPR038962; TMEM158.
DR   PANTHER; PTHR38324; PTHR38324; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..286
FT                   /note="Transmembrane protein 158"
FT                   /id="PRO_0000285129"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          20..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   286 AA;  29145 MW;  5F011667D8FC9801 CRC64;
     MLPLLAALLA AACQLPPAHG GATDAPGLAG TPPNASANAS FTNEHSTPRL LASAASAPPE
     RSGPEEAPAA PCNISVQRQM LSSLLVRWGR PRGLQCDLLL FSTNAHGRAF FAAAFHRVGP
     PLLIEHLGLA AGGAQQDLRL CVGCGWVRGR LRAPAGAPTA LPAYPAAEPG PLWLQGEPRH
     FCCLDFSLEE LQGEPGWRLN RKPIESTLVA CFMTLVIVVW SVAALIWPVP IIAGFLPNGM
     EQRRTTAGAP AAAPAAVPAG TTAAAAAAAA AAAAAAAAVT SGVAPK
 
 
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