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