GP2_RAT
ID GP2_RAT Reviewed; 530 AA.
AC P19218;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Pancreatic secretory granule membrane major glycoprotein GP2 {ECO:0000305|PubMed:1999417};
DE AltName: Full=Glycoprotein 80 {ECO:0000303|PubMed:2216794};
DE Short=gp80 {ECO:0000303|PubMed:2216794};
DE AltName: Full=Pancreatic zymogen granule membrane protein GP-2 {ECO:0000305|PubMed:1999417};
DE Flags: Precursor;
GN Name=Gp2 {ECO:0000312|RGD:621695};
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].
RC STRAIN=Wistar; TISSUE=Pancreas;
RX PubMed=2216794; DOI=10.1093/nar/18.19.5900;
RA Fukuoka S., Scheele G.;
RT "Nucleotide sequence encoding the major glycoprotein (GP2) of rat
RT pancreatic secretory (zymogen) granule membranes.";
RL Nucleic Acids Res. 18:5900-5900(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 293-303 AND 477-495,
RP SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=1999417; DOI=10.1016/s0021-9258(20)64315-0;
RA Hoops T.C., Rindler M.J.;
RT "Isolation of the cDNA encoding glycoprotein-2 (GP-2), the major zymogen
RT granule membrane protein. Homology to uromodulin/Tamm-Horsfall protein.";
RL J. Biol. Chem. 266:4257-4263(1991).
RN [3]
RP PROTEIN SEQUENCE OF 327-512.
RX PubMed=8352773; DOI=10.1006/bbrc.1993.1945;
RA Withiam-Leitch M., Aletta J.M., Koshlukova S.E., Rupp G., Beaudoin A.R.,
RA Rubin R.P.;
RT "Glycoprotein 2 of zymogen granule membranes shares immunological cross-
RT reactivity and sequence similarity with phospholipase A2.";
RL Biochem. Biophys. Res. Commun. 194:1167-1174(1993).
RN [4]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=6479170; DOI=10.1111/j.1432-1033.1984.tb08446.x;
RA Havinga J.R., Strous G.J., Poort C.;
RT "Intracellular transport of the major glycoprotein of zymogen granule
RT membranes in the rat pancreas. Demonstration of high turnover at the plasma
RT membrane.";
RL Eur. J. Biochem. 144:177-183(1984).
RN [5]
RP INTERACTION WITH SYCN, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11853552; DOI=10.1042/0264-6021:3620433;
RA Kalus I., Hodel A., Koch A., Kleene R., Edwardson J.M., Schrader M.;
RT "Interaction of syncollin with GP-2, the major membrane protein of
RT pancreatic zymogen granules, and association with lipid microdomains.";
RL Biochem. J. 362:433-442(2002).
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:0000250|UniProtKB:Q9D733}.
CC -!- SUBUNIT: Interacts with SYCN. {ECO:0000269|PubMed:11853552}.
CC -!- SUBCELLULAR LOCATION: Zymogen granule membrane
CC {ECO:0000269|PubMed:1999417, ECO:0000269|PubMed:6479170}; Lipid-anchor,
CC GPI-anchor {ECO:0000269|PubMed:11853552, ECO:0000269|PubMed:1999417}.
CC Secreted {ECO:0000305|PubMed:6479170}. Cell membrane
CC {ECO:0000269|PubMed:1999417, ECO:0000269|PubMed:6479170}; Lipid-anchor,
CC GPI-anchor {ECO:0000269|PubMed:11853552, ECO:0000269|PubMed:1999417}.
CC Apical cell membrane {ECO:0000250|UniProtKB:Q9D733}; Lipid-anchor, GPI-
CC anchor {ECO:0000269|PubMed:11853552, ECO:0000269|PubMed:1999417}.
CC Membrane raft {ECO:0000269|PubMed:11853552}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:11853552, ECO:0000269|PubMed:1999417}. Endosome
CC {ECO:0000250|UniProtKB:Q9D733}. Note=Secreted, after cleavage, in the
CC pancreatic juice. {ECO:0000305|PubMed:6479170}.
CC -!- TISSUE SPECIFICITY: Expressed in pancreas.
CC {ECO:0000269|PubMed:1999417}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:1999417,
CC ECO:0000269|PubMed:6479170}.
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DR EMBL; X53935; CAA37882.1; -; mRNA.
DR EMBL; M58716; AAA41268.1; -; mRNA.
DR PIR; A38690; A38690.
DR AlphaFoldDB; P19218; -.
DR SMR; P19218; -.
DR STRING; 10116.ENSRNOP00000021249; -.
DR GlyGen; P19218; 7 sites.
DR PaxDb; P19218; -.
DR PRIDE; P19218; -.
DR UCSC; RGD:621695; rat.
DR RGD; 621695; Gp2.
DR eggNOG; ENOG502QT6B; Eukaryota.
DR InParanoid; P19218; -.
DR PhylomeDB; P19218; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:P19218; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISS: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; IDA:UniProtKB.
DR GO; GO:0003823; F:antigen binding; ISO:RGD.
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; ISO:RGD.
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 InterPro; IPR017977; ZP_dom_CS.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00241; ZP; 1.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Endosome; Glycoprotein; GPI-anchor;
KW Immunity; Innate immunity; Lipoprotein; Membrane; Receptor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:P25291"
FT CHAIN 22..505
FT /note="Pancreatic secretory granule membrane major
FT glycoprotein GP2"
FT /id="PRO_0000041661"
FT PROPEP 506..530
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041662"
FT DOMAIN 179..223
FT /note="EGF-like"
FT /evidence="ECO:0000305"
FT DOMAIN 221..477
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT LIPID 505
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
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 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 183..193
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 187..202
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 204..234
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 222..313
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 254..277
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 394..454
FT /evidence="ECO:0000250|UniProtKB:P07911,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 415..470
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 459..466
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT CONFLICT 287
FT /note="Q -> H (in Ref. 2; AAA41268)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="A -> V (in Ref. 2; AAA41268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 58708 MW; 97A3CDD019BC7DFF CRC64;
MVACDLLWLA AASCLLTLVF PSTTHQGYGN PRNTSNVDLD CGAPGSSSAG ICFDPCQNHT
VLNDPSRSTE NTVSSEECDS HLRGWYRFVG DGGVKMPETC VNVYRCHTYA PMWLSGSHPI
LGDGIVNRTA CANWNENCCF WSSEVQVKAC LGESGEYHVY KLQGTPECSL RYCTDPSTAP
KKCEIACRPE EECVFQNNSW TCVCRQDLNV SDTLSLQPLL DCGANEIKVK LDKCLLGGLG
FKEDIITYLN DRNCRGTMKD EPNNWVSTTS PVVANDCGNI LENNGTQAIY RNTLSLATDF
IIRDFLVNVN FQCAYPLDMN VSLQTALQPI VSSLNVDVGG AGEFTVTMAL FQDQSYTHPY
EGSKVLLPVE NILYVGALLN RGDTSRFKLL LTNCYATPSG DRNDIVKYFI IRNRCPNQRD
STINVEENGV SSESRFSVQM FMFAGNYDLV FLHCEVYLCD STTEQCQPSC STSRLRSSEP
AIDLTRVLDI GPITKKSVQN PDTSNGTPRN TGFLLAWPTF FLPVFLAWLF
