TM158_RAT
ID TM158_RAT Reviewed; 285 AA.
AC Q91XV7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Transmembrane protein 158;
DE AltName: Full=40 kDa BINP-binding protein;
DE Short=p40BBP;
DE AltName: Full=Brain-specific binding protein;
DE AltName: Full=Ras-induced senescence protein 1;
DE Flags: Precursor;
GN Name=Tmem158; Synonyms=Ris1;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC TISSUE=Hippocampus;
RX PubMed=11399754; DOI=10.1074/jbc.m100617200;
RA Hama T., Maruyama M., Katoh-Semba R., Takizawa M., Iwashima M., Nara K.;
RT "Identification and molecular cloning of a novel brain-specific receptor
RT protein that binds to brain injury-derived neurotrophic peptide. Possible
RT role for neuronal survival.";
RL J. Biol. Chem. 276:31929-31935(2001).
CC -!- FUNCTION: Receptor for brain injury-derived neurotrophic peptide
CC (BINP), a synthetic 13-mer peptide. {ECO:0000250,
CC ECO:0000269|PubMed:11399754}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected only in the brain.
CC {ECO:0000269|PubMed:11399754}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11399754}.
CC -!- SIMILARITY: Belongs to the TMEM158 family. {ECO:0000305}.
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DR EMBL; AB028891; BAB63459.1; -; mRNA.
DR RefSeq; NP_476560.1; NM_057212.1.
DR AlphaFoldDB; Q91XV7; -.
DR STRING; 10116.ENSRNOP00000006300; -.
DR GlyGen; Q91XV7; 1 site.
DR PhosphoSitePlus; Q91XV7; -.
DR jPOST; Q91XV7; -.
DR PaxDb; Q91XV7; -.
DR Ensembl; ENSRNOT00000006300; ENSRNOP00000006300; ENSRNOG00000004757.
DR GeneID; 117582; -.
DR KEGG; rno:117582; -.
DR UCSC; RGD:708473; rat.
DR CTD; 25907; -.
DR RGD; 708473; Tmem158.
DR eggNOG; ENOG502RYJ7; Eukaryota.
DR GeneTree; ENSGT00390000009719; -.
DR HOGENOM; CLU_085099_0_0_1; -.
DR InParanoid; Q91XV7; -.
DR OMA; RLHFCCL; -.
DR OrthoDB; 1276094at2759; -.
DR PhylomeDB; Q91XV7; -.
DR TreeFam; TF339241; -.
DR PRO; PR:Q91XV7; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000004757; Expressed in frontal cortex and 17 other tissues.
DR Genevisible; Q91XV7; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042277; F:peptide binding; IMP:RGD.
DR GO; GO:0038023; F:signaling receptor activity; TAS:RGD.
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..285
FT /note="Transmembrane protein 158"
FT /id="PRO_0000285130"
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 COMPBIAS 29..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 285 AA; 29005 MW; E1815ED358A07AF7 CRC64;
MLPLLAALLA AACPLPPARG GATDAPGLSG TPPNASANAS FTGEHSTPRL LASAASAPPE
RAGPEEAPAA PCNISVQRQM LSSLLVRWGR PRGLQCDLLL FSTNAHGRAF FAAAFHRVGP
PLLIEHLGLA AGGAQQDLRL CVGCGWVRGR LRAPAGAPTA LPAYPAAEPG PLWLQGEPRH
FCCLDFSLEE LQGEPGWRLN RKPIESTLVA CFMTLVIVVW SVAALIWPVP IIAGFLPNGM
EQRRTTAGAP AAAPAAVPAG TTAAAAAAAA AAAAAAAVTS GVAPK