GP2_CANLF
ID GP2_CANLF Reviewed; 509 AA.
AC P25291;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Pancreatic secretory granule membrane major glycoprotein GP2 {ECO:0000305|PubMed:2011597};
DE AltName: Full=Pancreatic zymogen granule membrane protein GP-2 {ECO:0000305|PubMed:2011597};
DE AltName: Full=ZAP75 {ECO:0000303|PubMed:7765250};
DE Flags: Precursor;
GN Name=GP2 {ECO:0000250|UniProtKB:P55259};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-39; 243-254 AND 456-474,
RP SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION, TISSUE SPECIFICITY, AND
RP SIGNAL PEPTIDE.
RC TISSUE=Pancreas;
RX PubMed=2011597; DOI=10.1073/pnas.88.7.2898;
RA Fukuoka S., Freedman S.D., Scheele G.A.;
RT "A single gene encodes membrane-bound and free forms of GP-2, the major
RT glycoprotein in pancreatic secretory (zymogen) granule membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2898-2902(1991).
RN [2]
RP PROTEIN SEQUENCE OF 22-32.
RX PubMed=7765250; DOI=10.1271/bbb.58.1282;
RA Fukuoka S.;
RT "Analysis of ZAPs, zymogen granule membrane associated proteins, in the
RT regulated exocytosis of the pancreas.";
RL Biosci. Biotechnol. Biochem. 58:1282-1285(1994).
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:0000250|UniProtKB:P19218}.
CC -!- SUBCELLULAR LOCATION: Zymogen granule membrane
CC {ECO:0000269|PubMed:2011597}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:2011597}. Secreted {ECO:0000269|PubMed:2011597}.
CC Cell membrane {ECO:0000269|PubMed:2011597}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:2011597}. Apical cell membrane
CC {ECO:0000305|PubMed:2011597}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:2011597}. Membrane raft
CC {ECO:0000250|UniProtKB:P19218}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:2011597}. Endosome {ECO:0000250|UniProtKB:Q9D733}.
CC Note=Secreted, after cleavage, in the pancreatic juice.
CC {ECO:0000269|PubMed:2011597}.
CC -!- TISSUE SPECIFICITY: Expressed in pancreas.
CC {ECO:0000269|PubMed:2011597}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:2011597}.
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DR EMBL; M64083; AAA30904.1; -; mRNA.
DR PIR; A37259; A37259.
DR AlphaFoldDB; P25291; -.
DR SMR; P25291; -.
DR STRING; 9615.ENSCAFP00000026630; -.
DR PaxDb; P25291; -.
DR eggNOG; ENOG502QT6B; Eukaryota.
DR InParanoid; P25291; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0042589; C:zymogen granule membrane; IDA:UniProtKB.
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; ISS:UniProtKB.
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:0000269|PubMed:2011597,
FT ECO:0000269|PubMed:7765250"
FT CHAIN 22..484
FT /note="Pancreatic secretory granule membrane major
FT glycoprotein GP2"
FT /id="PRO_0000041655"
FT PROPEP 485..509
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041656"
FT DOMAIN 158..202
FT /note="EGF-like"
FT /evidence="ECO:0000305"
FT DOMAIN 200..456
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT LIPID 484
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 162..172
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 166..181
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 183..213
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 201..292
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 233..256
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 373..433
FT /evidence="ECO:0000250|UniProtKB:P07911,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 394..449
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 438..445
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT CONFLICT 246
FT /note="S -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="S -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="L -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 56773 MW; 3113C13A4A96A1B2 CRC64;
MVGSYVLWLA LASCILTLAS PEQQGNRNLI NTRSYDPCQN YTLLDEPSRS TENTEGSQVC
DKDKHGWYRF VGDGGVRMPE TCVPMYRCQT DAPLWLNGTH PTLAEGIVNR TACAHWSGNC
CLWKTVVQVK ACPGEFHVYR LEGTPKCSLR YCTDASTATD KCKNLCRPEE ACSFLNGTWD
CFCRSDLNSS DVHSLQPRLN CGAKEIQVSL DKCQLGGLGF GDEVIAYLRD WNCSNMMQRE
ERNWISVTSP TQARACGNIL ERNGTHAIYK NTLSLANEFI IRDTILNINF QCAYPLDMKV
SLQTALHPIV SSLNISVDGE GEFTVRMALF QDQSYISPYE GAAAVLAVES MLYVGAILEK
GDTSRFNLLL RNCYATPTKD KTDPVKYFII RNSCPNQYDS TIHVEENGVS SESRFSVQMF
MFAGNYDLVF LHCEIHLCDS LNEQCQPCCS RSQQRSEIVA LNPARVLDLG PITRRSSASV
DITDGTPSTA GFLLAWPMLL LPILLAELF
