T132A_MOUSE
ID T132A_MOUSE Reviewed; 1018 AA.
AC Q922P8; Q69ZF9; Q8BX93;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Transmembrane protein 132A;
DE AltName: Full=HSPA5-binding protein 1;
DE Flags: Precursor;
GN Name=Tmem132a; Synonyms=Kiaa1583;
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 TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HSPA5/GRP78. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum
CC membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TMEM132 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33373.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD32485.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173207; BAD32485.1; ALT_INIT; mRNA.
DR EMBL; AK048556; BAC33373.1; ALT_SEQ; mRNA.
DR EMBL; BC006896; AAH06896.2; -; mRNA.
DR CCDS; CCDS29589.1; -.
DR RefSeq; NP_598565.2; NM_133804.2.
DR AlphaFoldDB; Q922P8; -.
DR IntAct; Q922P8; 1.
DR MINT; Q922P8; -.
DR STRING; 10090.ENSMUSP00000025645; -.
DR GlyConnect; 2789; 2 N-Linked glycans (1 site).
DR GlyGen; Q922P8; 2 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q922P8; -.
DR PhosphoSitePlus; Q922P8; -.
DR MaxQB; Q922P8; -.
DR PaxDb; Q922P8; -.
DR PeptideAtlas; Q922P8; -.
DR PRIDE; Q922P8; -.
DR ProteomicsDB; 254520; -.
DR Antibodypedia; 52906; 73 antibodies from 20 providers.
DR DNASU; 98170; -.
DR Ensembl; ENSMUST00000025645; ENSMUSP00000025645; ENSMUSG00000024736.
DR GeneID; 98170; -.
DR KEGG; mmu:98170; -.
DR UCSC; uc008grc.1; mouse.
DR CTD; 54972; -.
DR MGI; MGI:2147810; Tmem132a.
DR VEuPathDB; HostDB:ENSMUSG00000024736; -.
DR eggNOG; KOG4789; Eukaryota.
DR GeneTree; ENSGT00940000161414; -.
DR HOGENOM; CLU_009871_0_0_1; -.
DR InParanoid; Q922P8; -.
DR OMA; GPCGPWL; -.
DR OrthoDB; 598074at2759; -.
DR PhylomeDB; Q922P8; -.
DR TreeFam; TF314981; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 98170; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Tmem132a; mouse.
DR PRO; PR:Q922P8; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q922P8; protein.
DR Bgee; ENSMUSG00000024736; Expressed in embryonic brain and 219 other tissues.
DR ExpressionAtlas; Q922P8; baseline and differential.
DR Genevisible; Q922P8; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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:0043069; P:negative regulation of programmed cell death; ISO:MGI.
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..1018
FT /note="Transmembrane protein 132A"
FT /id="PRO_0000287097"
FT TOPO_DOM 33..846
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 847..867
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 868..1018
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 606..911
FT /note="Binds to HSPA5/GRP78"
FT /evidence="ECO:0000250"
FT REGION 666..1018
FT /note="Confers cellular localization similar to full-length
FT form"
FT /evidence="ECO:0000250"
FT REGION 807..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..830
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 386
FT /note="L -> M (in Ref. 2; BAC33373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1018 AA; 110239 MW; 7BDFA487B5B51648 CRC64;
MTERKAAAPR GPYGAWFCLL VALALEVVRV SSNHDTLDPI YLPVALELLD APEHFRVQQV
GHYPPANSSL ASRSETFLLM QPWPRAQPLL RASYPPFATQ QVVPPRVTEP HRRPVPWDVR
AVSVEAAVTP AEPYARVLFH LKGQDWPPGP GSLPCARLHA THPAGTAHRA CRFQPSLGAC
VVELQFPSHW FSQSATTRAE LAYTLEPAGE GPGGCGLGTE EEPREQALPV GGVELHPEDP
PQYQEVPLDE AVTLRAPDVP MRPGQLFTAT LLLRHNFTAS LLTLRIKVKK GLQVIAARPA
QPTLWTAKLD RFKGSKHHTS LITCHRAGPA GPDSSPLELS EFLWVDFAVE NSTGGGVAVT
RPVTWQLEYP GQAPEAEKDK MVWEILVSER DIRALIPLAK AEELVNTAPL TGVPQRIPVR
LVTVDSGGAL EEVTEHIGCE SANTQVLQVS EACDAVFVAG QESRGAKGVR VDFWWRRLRA
SLKLTVWAPL LPLRIELTDT TLEQIRGWRV PGSAEGQLEP ETAAEEVERR SRGCRLQYQR
AGVRFLVPFA AHPLDGGRRL THLLGPDWLL DVSHLVAAHA HVQDPRIASL EGGRILVGRE
PGVTSIEVRS PLSDAILGEQ ALAVTDDKVS VLDLRVQPVM GISLSLSRGM SHPGEVTATC
WAQSALPAPK QEVALSLWLS FSDHTLAPAE LYDRNDLGLS VSAEEPSAVL PAEEQGAQLG
VVVSGVGAEG LPLHVALHPP EPCRRGRHRV PLASGTAWLG LPPLPTPVPA LPSSPVRTSP
FTEATVEGKR QIAGDMGGHV GIRGKFERAE EEAGKEENEA KEEEEDEEEM VPAPQRVTDL
ELGMYALLGI FCLAILIFLV NGVVFVLRYQ RKEPPDSATD PASPQPHNWV WLGTNQEELS
RQLDRCSSSG PPKGEGGCPC ESGAGGDAST VAPSASESPA GSSSTLARKE AGGRRKRVEF
VTFAPAPPTQ PPEEPVGAPA VQSILVAGEE DIRWVCEDMG LKDPEELRNY MERIRGSS
