GAPT_MOUSE
ID GAPT_MOUSE Reviewed; 157 AA.
AC Q8CB93;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein GAPT;
DE AltName: Full=Growth factor receptor-bound protein 2-binding adapter protein, transmembrane;
GN Name=Gapt;
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 STRAIN=C57BL/6J; TISSUE=Bone;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18559951; DOI=10.1189/jlb.0208087;
RA Liu Y., Zhang W.;
RT "Identification of a new transmembrane adaptor protein that constitutively
RT binds Grb2 in B cells.";
RL J. Leukoc. Biol. 84:842-851(2008).
CC -!- FUNCTION: Negatively regulates B-cell proliferation following
CC stimulation through the B-cell receptor. May play an important role in
CC maintenance of marginal zone (MZ) B-cells.
CC {ECO:0000269|PubMed:18559951}.
CC -!- SUBUNIT: Interacts with GRB2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed primarily in B220+ splenocytes and total
CC bone marrow cells. Expressed at lower levels in mast cells and
CC dendritic cells. Not detected in T-cells and macrophages (at protein
CC level). {ECO:0000269|PubMed:18559951}.
CC -!- DISRUPTION PHENOTYPE: Mice are normal in appearance, size and
CC fertility. In aged mice, the number of MZ B-cells is increased, and
CC serum concentrations of IgM, IgG2b, and IgG3 are elevated.
CC {ECO:0000269|PubMed:18559951}.
CC -!- SIMILARITY: Belongs to the GAPT family. {ECO:0000305}.
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DR EMBL; AK036534; BAC29466.1; -; mRNA.
DR EMBL; AK155882; BAE33480.1; -; mRNA.
DR EMBL; BC116629; AAI16630.1; -; mRNA.
DR EMBL; BC118005; AAI18006.1; -; mRNA.
DR CCDS; CCDS26766.1; -.
DR RefSeq; NP_808381.1; NM_177713.3.
DR RefSeq; XP_006517713.1; XM_006517650.3.
DR RefSeq; XP_006517714.1; XM_006517651.3.
DR RefSeq; XP_006517715.1; XM_006517652.3.
DR AlphaFoldDB; Q8CB93; -.
DR STRING; 10090.ENSMUSP00000053775; -.
DR iPTMnet; Q8CB93; -.
DR PhosphoSitePlus; Q8CB93; -.
DR MaxQB; Q8CB93; -.
DR PaxDb; Q8CB93; -.
DR PRIDE; Q8CB93; -.
DR ProteomicsDB; 271668; -.
DR Antibodypedia; 2638; 85 antibodies from 15 providers.
DR Ensembl; ENSMUST00000058806; ENSMUSP00000053775; ENSMUSG00000046006.
DR Ensembl; ENSMUST00000224534; ENSMUSP00000153170; ENSMUSG00000046006.
DR GeneID; 238875; -.
DR KEGG; mmu:238875; -.
DR UCSC; uc007rvq.1; mouse.
DR CTD; 202309; -.
DR MGI; MGI:3608341; Gapt.
DR VEuPathDB; HostDB:ENSMUSG00000046006; -.
DR eggNOG; ENOG502TKNI; Eukaryota.
DR GeneTree; ENSGT00390000011255; -.
DR HOGENOM; CLU_1668861_0_0_1; -.
DR InParanoid; Q8CB93; -.
DR OMA; WHWKHRN; -.
DR OrthoDB; 1524349at2759; -.
DR PhylomeDB; Q8CB93; -.
DR TreeFam; TF338585; -.
DR BioGRID-ORCS; 238875; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8CB93; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8CB93; protein.
DR Bgee; ENSMUSG00000046006; Expressed in granulocyte and 24 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
DR GO; GO:0002322; P:B cell proliferation involved in immune response; IMP:MGI.
DR InterPro; IPR021082; Protein_GAPT.
DR PANTHER; PTHR37350; PTHR37350; 1.
DR Pfam; PF11770; GAPT; 1.
DR PRINTS; PR02077; PROTEINGAPT.
PE 1: Evidence at protein level;
KW B-cell activation; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..157
FT /note="Protein GAPT"
FT /id="PRO_0000271124"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 117..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 157 AA; 17601 MW; 61C4C15FBABC5410 CRC64;
MLECFESSPV AVAVGVSLLV LLLLCGIGCA WHWNRRESTP FTLPKFMQRR SSRQKDVTKT
VSSSAYVISP SMKASVESKG HKSTAKRNKM HGNYENVEVC PPCTEGTTEK ALYENTQPSN
LEEHVYGNQT DPLYYNFQKP SPPPPQDDDI YILPDCD
