T132A_RAT
ID T132A_RAT Reviewed; 1021 AA.
AC Q80WF4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Transmembrane protein 132A;
DE AltName: Full=GRP78-binding protein;
DE AltName: Full=HSPA5-binding protein 1;
DE Flags: Precursor;
GN Name=Tmem132a; Synonyms=Gbp, Hspa5bp1;
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, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH HSPA5, AND REGION.
RC STRAIN=Sprague-Dawley;
RX PubMed=12514190; DOI=10.1074/jbc.m212083200;
RA Oh-hashi K., Naruse Y., Amaya F., Shimosato G., Tanaka M.;
RT "Cloning and characterization of a novel GRP78-binding protein in the rat
RT brain.";
RL J. Biol. Chem. 278:10531-10537(2003).
RN [2]
RP FUNCTION.
RX PubMed=16806201; DOI=10.1016/j.febslet.2006.06.028;
RA Oh-hashi K., Hirata Y., Koga H., Kiuchi K.;
RT "GRP78-binding protein regulates cAMP-induced glial fibrillary acidic
RT protein expression in rat C6 glioblastoma cells.";
RL FEBS Lett. 580:3943-3947(2006).
CC -!- FUNCTION: May play a role in embryonic and postnatal development of the
CC brain. Increased resistance to cell death induced by serum starvation
CC in cultured cells. Regulates cAMP-induced GFAP gene expression via
CC STAT3 phosphorylation. {ECO:0000269|PubMed:12514190,
CC ECO:0000269|PubMed:16806201}.
CC -!- SUBUNIT: Interacts with HSPA5/GRP78. {ECO:0000269|PubMed:12514190}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12514190}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12514190}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12514190}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12514190}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain in neuronal cells of the
CC hypothalamus, thalamus, cerebral cortex, amygdala, and cerebellum.
CC {ECO:0000269|PubMed:12514190}.
CC -!- DEVELOPMENTAL STAGE: Detected in the brain at E12 with increasing level
CC reaching a peak within 2 weeks after birth.
CC {ECO:0000269|PubMed:12514190}.
CC -!- SIMILARITY: Belongs to the TMEM132 family. {ECO:0000305}.
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DR EMBL; AY216677; AAO65155.1; -; mRNA.
DR RefSeq; NP_821140.1; NM_178021.1.
DR AlphaFoldDB; Q80WF4; -.
DR STRING; 10116.ENSRNOP00000037012; -.
DR GlyGen; Q80WF4; 1 site.
DR jPOST; Q80WF4; -.
DR PaxDb; Q80WF4; -.
DR PRIDE; Q80WF4; -.
DR GeneID; 338474; -.
DR KEGG; rno:338474; -.
DR UCSC; RGD:727936; rat.
DR CTD; 54972; -.
DR RGD; 727936; Tmem132a.
DR eggNOG; KOG4789; Eukaryota.
DR InParanoid; Q80WF4; -.
DR OrthoDB; 598074at2759; -.
DR PhylomeDB; Q80WF4; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q80WF4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IMP:RGD.
DR InterPro; IPR026307; TMEM132.
DR InterPro; IPR031436; TMEM132_C.
DR InterPro; IPR031437; TMEM132_M.
DR InterPro; IPR031435; TMEM132_N.
DR PANTHER; PTHR13388; PTHR13388; 1.
DR Pfam; PF16070; TMEM132; 1.
DR Pfam; PF15706; TMEM132D_C; 1.
DR Pfam; PF15705; TMEM132D_N; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..1021
FT /note="Transmembrane protein 132A"
FT /id="PRO_0000287098"
FT TOPO_DOM 33..848
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 849..869
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 870..1021
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 207..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..913
FT /note="Binds to HSPA5/GRP78"
FT REGION 666..1021
FT /note="Confers cellular localization similar to full-length
FT form"
FT REGION 793..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..832
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1021 AA; 110574 MW; C3E207A53340BCD6 CRC64;
MTERAAAAPR GPYGAWLCLL VALALEVVRV GSNQNTLDPI YLPVALELLD APEHFRVQQV
GHYPPANSSL GSRSETFLLM QPWPRAQPLL RASYPPFATQ QVVPPRVTEP HRRPVPWDVR
AVSVEAAVTP AEPYARVLFH LKGQDWPPGP GSLPCARLHA THPAGTAHQA CRFQPSLGAC
VVELQFPSQW FSQSATTRAE LAYTLEPAGE GPGGCGPGTE EEPKEQALPV GSVELHPEDP
PQHQEVPLDE VVTLRAPDVP VRPGQLFTAT LLLRHNFTAS LLTLRIKVKK GLQVTAARPA
QPTFWTAKLD RFKGSKHHTS LITCHRTGPA GPDSRPLELP EFLWVDFAVE NSTGGGVAVT
RPVTWQLEYP GQAPEAEKDK MVWEILFSER DIRALIPLAK AEELVNTAPL TGVPQRIPVR
LVTVDSGGAL EEVTEHIGCE SANTQVLQVS EACDAVFVAG QESRGAKGVR VDFWWRRLRA
SLKLTVWAPL LPLRIELTDT TLEQIRGWRV PGPAEGQLEP EAAAEEVERR SRGCRLQYQR
AGVRFLVPFA AHPLDGGRRL THLLGPDWLL DVSHLVAAHA HVQDPRIATL EGGRILVGRE
PGVTSIEVRS PLSDSILGEQ ALAVTDDKVS VLDLRVQPVM GISLSLSRGV SHPGEVTATC
WAQSALPAPK QEVALSLWLS FSDHTLAPAE LYDRNDLGLS VSAEEPSAVV PAEEQRAQLG
VVVSGVGAKG LPLHVALHPP EPCRRGRHRV PLASGTAWLG LPPLPTPAPA LPSSPARTPP
FTEASVEGKR QVAGDMGSHV GPGIRGKFER AEEEAGKEEN EAKEEEEDEE EMVPAPQRVT
DLELGMYALL GIFCLAFLIF LVNGVVFVLR YQRKEPPDSV TDPASPQPHN WVWLGTNQEE
LSRQLDRCSS SSPPKGEGGC PCESGAGGDT STVAPSASES PAGSTSTLAR KEAGGRRKRV
EFVTFAPAPP AQEAPEEPVG APAVQSILVA GEEDIRWVCE DMGLKDPEEL RNYMERIRGS
S
