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Database: UniProt
Entry: P19218
LinkDB: P19218
Original site: P19218 
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   23-MAY-2018, entry version 123.
DE   RecName: Full=Pancreatic secretory granule membrane major glycoprotein GP2;
DE   AltName: Full=Glycoprotein 80;
DE            Short=gp80;
DE   AltName: Full=Pancreatic zymogen granule membrane protein GP-2;
DE   Flags: Precursor;
GN   Name=Gp2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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], AND PROTEIN SEQUENCE OF 293-303 AND
RP   477-495.
RX   PubMed=1999417;
RA   Hoops T.C., Rindler M.J.;
RT   "Isolation of the cDNA encoding glycoprotein-2 (GP-2), the major
RT   zymogen granule membrane protein. Homology to uromodulin/Tamm-Horsfall
RT   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.,
RA   Beaudoin A.R., Rubin R.P.;
RT   "Glycoprotein 2 of zymogen granule membranes shares immunological
RT   cross-reactivity and sequence similarity with phospholipase A2.";
RL   Biochem. Biophys. Res. Commun. 194:1167-1174(1993).
RN   [4]
RP   INTERACTION WITH SYCN.
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
RT   microdomains.";
RL   Biochem. J. 362:433-442(2002).
CC   -!- SUBUNIT: Interacts with SYCN. {ECO:0000269|PubMed:11853552}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC       Secreted. Note=Secreted after cleavage in the pancreatic juice.
CC   -!- TISSUE SPECIFICITY: Pancreatic secretory (zymogen) granule.
DR   EMBL; X53935; CAA37882.1; -; mRNA.
DR   EMBL; M58716; AAA41268.1; -; mRNA.
DR   PIR; A38690; A38690.
DR   UniGene; Rn.11223; -.
DR   SMR; P19218; -.
DR   STRING; 10116.ENSRNOP00000021249; -.
DR   PaxDb; P19218; -.
DR   PRIDE; P19218; -.
DR   UCSC; RGD:621695; rat.
DR   RGD; 621695; Gp2.
DR   eggNOG; ENOG410IVSV; Eukaryota.
DR   eggNOG; ENOG410YDU6; LUCA.
DR   HOGENOM; HOG000293303; -.
DR   HOVERGEN; HBG004349; -.
DR   InParanoid; P19218; -.
DR   PhylomeDB; P19218; -.
DR   PRO; PR:P19218; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Glycoprotein; GPI-anchor;
KW   Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    505       Pancreatic secretory granule membrane
FT                                major glycoprotein GP2.
FT                                /FTId=PRO_0000041661.
FT   PROPEP      506    530       Removed in mature form. {ECO:0000255}.
FT                                /FTId=PRO_0000041662.
FT   DOMAIN      179    223       EGF-like.
FT   DOMAIN      221    477       ZP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00375}.
FT   LIPID       505    505       GPI-anchor amidated asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     33     33       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     58     58       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    127    127       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    197    197       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    209    209       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    284    284       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    320    320       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    183    193       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    187    202       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    204    234       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    222    313       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    254    277       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    394    454       {ECO:0000250|UniProtKB:P07911,
FT                                ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    415    470       {ECO:0000250|UniProtKB:P07911}.
FT   DISULFID    459    466       {ECO:0000250|UniProtKB:P07911}.
FT   CONFLICT    287    287       Q -> H (in Ref. 2; AAA41268).
FT                                {ECO:0000305}.
FT   CONFLICT    377    377       A -> V (in Ref. 2; AAA41268).
FT                                {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
//
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