GP2_MOUSE
ID GP2_MOUSE Reviewed; 531 AA.
AC Q9D733;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Pancreatic secretory granule membrane major glycoprotein GP2 {ECO:0000305};
DE AltName: Full=Pancreatic zymogen granule membrane protein GP-2 {ECO:0000250|UniProtKB:P55259};
DE Flags: Precursor;
GN Name=Gp2 {ECO:0000312|MGI:MGI:1914383};
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=Tongue;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
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).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19907495; DOI=10.1038/nature08529;
RA Hase K., Kawano K., Nochi T., Pontes G.S., Fukuda S., Ebisawa M.,
RA Kadokura K., Tobe T., Fujimura Y., Kawano S., Yabashi A., Waguri S.,
RA Nakato G., Kimura S., Murakami T., Iimura M., Hamura K., Fukuoka S.,
RA Lowe A.W., Itoh K., Kiyono H., Ohno H.;
RT "Uptake through glycoprotein 2 of FimH(+) bacteria by M cells initiates
RT mucosal immune response.";
RL Nature 462:226-230(2009).
CC -!- FUNCTION: Functions as an intestinal M-cell transcytotic receptor
CC specific of type-I-piliated bacteria that participates in the mucosal
CC immune response toward these bacteria. At the apical membrane of M-
CC cells it binds fimH, a protein of the bacteria type I pilus tip.
CC Internalizes bound bacteria, like E.coli and S.typhimurium, from the
CC lumen of the intestine and delivers them, through M-cells, to the
CC underlying organized lymphoid follicles where they are captured by
CC antigen-presenting dendritic cells to elicit a mucosal immune response.
CC {ECO:0000269|PubMed:19907495}.
CC -!- SUBUNIT: Interacts with SYCN. {ECO:0000250|UniProtKB:P19218}.
CC -!- SUBCELLULAR LOCATION: Zymogen granule membrane
CC {ECO:0000250|UniProtKB:P19218}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:P19218}. Secreted
CC {ECO:0000250|UniProtKB:P19218}. Cell membrane
CC {ECO:0000305|PubMed:19907495}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:P19218}. Apical cell membrane
CC {ECO:0000269|PubMed:19907495}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:P19218}. Membrane raft
CC {ECO:0000250|UniProtKB:P19218}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:P19218}. Endosome {ECO:0000305|PubMed:19907495}.
CC Note=Secreted, after cleavage, in the pancreatic juice.
CC {ECO:0000250|UniProtKB:P19218}.
CC -!- TISSUE SPECIFICITY: Specifically expressed by M (microfold) cells which
CC are atypical epithelial cells of the intestine.
CC {ECO:0000269|PubMed:19907495}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P19218}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice lacking Gp2 fail to induce antigen-
CC specific helper-T-cells and antibody immune responses after oral
CC immunization with FimH positive bacteria (PubMed:19907495). This is not
CC due to a general defect in the immunological functions, since a normal
CC response is induced by other systemic immunizations (PubMed:19907495).
CC {ECO:0000269|PubMed:19907495}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26423.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK009661; BAB26423.2; ALT_INIT; mRNA.
DR CCDS; CCDS21779.1; -.
DR RefSeq; NP_080265.2; NM_025989.3.
DR AlphaFoldDB; Q9D733; -.
DR SMR; Q9D733; -.
DR STRING; 10090.ENSMUSP00000033255; -.
DR GlyGen; Q9D733; 6 sites.
DR iPTMnet; Q9D733; -.
DR PhosphoSitePlus; Q9D733; -.
DR MaxQB; Q9D733; -.
DR PaxDb; Q9D733; -.
DR PRIDE; Q9D733; -.
DR ProteomicsDB; 271260; -.
DR Antibodypedia; 2620; 405 antibodies from 22 providers.
DR DNASU; 67133; -.
DR Ensembl; ENSMUST00000033255; ENSMUSP00000033255; ENSMUSG00000030954.
DR GeneID; 67133; -.
DR KEGG; mmu:67133; -.
DR UCSC; uc009jla.1; mouse.
DR CTD; 2813; -.
DR MGI; MGI:1914383; Gp2.
DR VEuPathDB; HostDB:ENSMUSG00000030954; -.
DR eggNOG; ENOG502QT6B; Eukaryota.
DR GeneTree; ENSGT00940000156038; -.
DR InParanoid; Q9D733; -.
DR OMA; QGYGNPS; -.
DR OrthoDB; 665331at2759; -.
DR PhylomeDB; Q9D733; -.
DR TreeFam; TF330284; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 67133; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q9D733; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D733; protein.
DR Bgee; ENSMUSG00000030954; Expressed in pyloric antrum and 33 other tissues.
DR ExpressionAtlas; Q9D733; baseline and differential.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0042589; C:zymogen granule membrane; ISS:UniProtKB.
DR GO; GO:0003823; F:antigen binding; IDA:MGI.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0002412; P:antigen transcytosis by M cells in mucosal-associated lymphoid tissue; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1990266; P:neutrophil migration; IBA:GO_Central.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00241; ZP; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Disulfide bond; EGF-like domain;
KW Endosome; Glycoprotein; GPI-anchor; Immunity; Innate immunity; Lipoprotein;
KW Membrane; Receptor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:P25291"
FT CHAIN 22..?
FT /note="Pancreatic secretory granule membrane major
FT glycoprotein GP2"
FT /id="PRO_0000041659"
FT PROPEP ?..531
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041660"
FT DOMAIN 180..224
FT /note="EGF-like"
FT /evidence="ECO:0000305"
FT DOMAIN 222..478
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 184..194
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 188..203
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 205..235
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 223..314
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 255..278
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 395..455
FT /evidence="ECO:0000250|UniProtKB:P07911,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 416..471
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 460..467
FT /evidence="ECO:0000250|UniProtKB:P07911"
SQ SEQUENCE 531 AA; 59154 MW; B2BEE2F4B8E63F79 CRC64;
MVGCDLLWLA AASCVLTLVS PSTIHQGYGR PRNSSNLDLD CGSPDSPSSG ICFDPCQNHT
VLNDPTRSTE NNDSSVAWCD DNLHGWYRFV GDGGVKMPET CVSVFRCHTS APMWLSGSHP
ILGDGIVSHT ACANWNENCC FWRSEVQVKA CSEELGEYHV YKLQGTPECS LRYCTDPSTA
PKNCEITCRP EEECVFQNNN WSCVCRQDLH VSDSQSLQPL LDCGDNEIKV KLDKCLLGGM
GFKEEIIAYL NDRNCNGTMQ DEPNNWVSMT SPVVANYCGN ILEKNGTHAI YRNTLSLATD
FIIRDFRVNV NFQCAYPLDM SVSLETALQP IVSSLTVDVD GAGEFNVKMA LFQDQSYTNP
YEGAEVLLPV ESILYVGVLL NRGDTSRFKL LLTNCYATPS EDRHDPVKYF IIKNRCPNQR
DSTINVRENG VSSESRFSVQ MFMFAGNYDL VFLHCEVYLC DSTTEQCQPS CSTNRLRSSR
PAIDYNRVLD LGPITKRSAQ SSATSKGTPH TTGFLLAWPM FFLPVFLALL F
