PRG2_HUMAN
ID PRG2_HUMAN Reviewed; 222 AA.
AC P13727; A6XMW0; B2R5I1; P81448; Q14227; Q6ICT2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Bone marrow proteoglycan;
DE Short=BMPG;
DE AltName: Full=Proteoglycan 2;
DE Contains:
DE RecName: Full=Eosinophil granule major basic protein;
DE Short=EMBP;
DE Short=MBP;
DE AltName: Full=Pregnancy-associated major basic protein;
DE Flags: Precursor;
GN Name=PRG2; Synonyms=MBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT TYR-206.
RC TISSUE=Promyelocyte;
RX PubMed=3171483; DOI=10.1084/jem.168.4.1493;
RA Barker R.L., Gleich G.J., Pease L.R.;
RT "Acidic precursor revealed in human eosinophil granule major basic protein
RT cDNA.";
RL J. Exp. Med. 168:1493-1498(1988).
RN [2]
RP SEQUENCE REVISION TO 84.
RA Barker R.L.;
RL Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-206.
RX PubMed=2323577; DOI=10.1016/0378-1119(90)90292-y;
RA Barker R.L., Loegering D.A., Arakawa K.C., Pease L.R., Gleich G.J.;
RT "Cloning and sequence analysis of the human gene encoding eosinophil major
RT basic protein.";
RL Gene 86:285-289(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT TYR-206.
RX PubMed=3199069; DOI=10.1084/jem.168.6.2295;
RA McGrogan M., Simonsen C., Scott R., Giffith J., Ellis N., Kennedy J.,
RA Campanelli D., Nathan C., Gabay J.;
RT "Isolation of a complementary DNA clone encoding a precursor to human
RT eosinophil major basic protein.";
RL J. Exp. Med. 168:2295-2308(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP VARIANT TYR-206.
RX PubMed=1565101; DOI=10.1016/0161-5890(92)90012-m;
RA Yoshimatsu K., Ohya Y., Shikata Y., Seto T., Hasegawa Y., Tanaka I.,
RA Kawamura T., Kitoh K., Toyoshima S., Osawa T.;
RT "Purification and cDNA cloning of a novel factor produced by a human T-cell
RT hybridoma: sequence homology with animal lectins.";
RL Mol. Immunol. 29:537-546(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT TYR-206.
RC TISSUE=Bone marrow;
RX PubMed=7531438; DOI=10.1042/bj3050921;
RA Li M.S., Sun L., Satoh T., Fisher L.M., Spry C.J.;
RT "Human eosinophil major basic protein, a mediator of allergic inflammation,
RT is expressed by alternative splicing from two promoters.";
RL Biochem. J. 305:921-927(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TYR-206.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TYR-206.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Yu Z., Zheng Z., Tang T., Fu Y.;
RT "A computer system platform used to predict novel genes.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-206.
RC TISSUE=Placenta;
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 [12]
RP PROTEIN SEQUENCE OF 17-222, AND GLYCOSYLATION AT SER-24; THR-25; SER-62 AND
RP ASN-86.
RC TISSUE=Liver;
RX PubMed=8507662; DOI=10.1016/0167-4838(93)90158-n;
RA Shikata Y., Hayashi Y., Yoshimatsu K., Ohya Y., Seto T., Fukushima K.,
RA Yoshida Y.;
RT "Pro-major basic protein has three types of sugar chains at the pro-
RT portion.";
RL Biochim. Biophys. Acta 1163:243-249(1993).
RN [13]
RP PROTEIN SEQUENCE OF 17-26; 47-52; 98-108; 172-179 AND 210-222, SUBUNIT, AND
RP INTERCHAIN DISULFIDE BOND.
RC TISSUE=Serum;
RX PubMed=7685339; DOI=10.1016/s0021-9258(18)31378-4;
RA Oxvig C., Sand O., Kristensen T., Gleich G.J., Sottrup-Jensen L.;
RT "Circulating human pregnancy-associated plasma protein-A is disulfide-
RT bridged to the proform of eosinophil major basic protein.";
RL J. Biol. Chem. 268:12243-12246(1993).
RN [14]
RP PROTEIN SEQUENCE OF 17-29, SUBUNIT, AND DEVELOPMENTAL STAGE.
RC TISSUE=Serum;
RX PubMed=7539791; DOI=10.1074/jbc.270.23.13645;
RA Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., Stigbrand T.,
RA Gleich G.J., Sottrup-Jensen L.;
RT "Identification of angiotensinogen and complement C3dg as novel proteins
RT binding the proform of eosinophil major basic protein in human pregnancy
RT serum and plasma.";
RL J. Biol. Chem. 270:13645-13651(1995).
RN [15]
RP PROTEIN SEQUENCE OF 106-222.
RX PubMed=3410852; DOI=10.1016/s0021-9258(18)37791-3;
RA Wasmoen T.L., Bell M.P., Loegering D.A., Gleich G.J., Prendergast F.G.,
RA McKean D.J.;
RT "Biochemical and amino acid sequence analysis of human eosinophil granule
RT major basic protein.";
RL J. Biol. Chem. 263:12559-12563(1988).
RN [16]
RP PROTEIN SEQUENCE OF 106-125.
RX PubMed=2501794; DOI=10.1073/pnas.86.14.5610;
RA Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N.,
RA Seeger M., Nathan C.F.;
RT "Antibiotic proteins of human polymorphonuclear leukocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
RN [17]
RP PROTEIN SEQUENCE OF 108-124.
RX PubMed=3422083; DOI=10.1002/jlb.43.1.1;
RA Weller P.F., Ackerman S.J., Smith J.A.;
RT "Eosinophil granule cationic proteins: major basic protein is distinct from
RT the smaller subunit of eosinophil peroxidase.";
RL J. Leukoc. Biol. 43:1-4(1988).
RN [18]
RP PROTEIN SEQUENCE OF 172-179 AND 210-222, AND SUBUNIT.
RC TISSUE=Serum;
RX PubMed=7508748; DOI=10.1021/bi00172a040;
RA Kristensen T., Oxvig C., Sand O., Moller N.P.H., Sottrup-Jensen L.;
RT "Amino acid sequence of human pregnancy-associated plasma protein-A derived
RT from cloned cDNA.";
RL Biochemistry 33:1592-1598(1994).
RN [19]
RP PROTEIN SEQUENCE OF 177-196.
RC TISSUE=Placenta;
RX PubMed=2584934; DOI=10.1084/jem.170.6.2051;
RA Wasmoen T.L., McKean D.J., Benirschke K., Coulam C.B., Gleich G.J.;
RT "Evidence of eosinophil granule major basic protein in human placenta.";
RL J. Exp. Med. 170:2051-2063(1989).
RN [20]
RP GLYCOSYLATION AT THR-23; SER-24; THR-25; THR-34; SER-62 AND ASN-86.
RX PubMed=7524900;
RA Oxvig C., Haaning J., Hojrup P., Sottrup-Jensen L.;
RT "Location and nature of carbohydrate groups in proform of human major basic
RT protein isolated from pregnancy serum.";
RL Biochem. Mol. Biol. Int. 33:329-336(1994).
RN [21]
RP DISULFIDE BONDS.
RX PubMed=8137941; DOI=10.1016/0014-5793(94)80459-1;
RA Oxvig C., Gleich G.J., Sottrup-Jensen L.;
RT "Localization of disulfide bridges and free sulfhydryl groups in human
RT eosinophil granule major basic protein.";
RL FEBS Lett. 341:213-217(1994).
RN [22]
RP TISSUE SPECIFICITY.
RX PubMed=7526035;
RA Bonno M., Oxvig C., Kephart G.M., Wagner J.M., Kristensen T.,
RA Sottrup-Jensen L., Gleich G.J.;
RT "Localization of pregnancy-associated plasma protein-A and colocalization
RT of pregnancy-associated plasma protein-A messenger ribonucleic acid and
RT eosinophil granule major basic protein messenger ribonucleic acid in
RT placenta.";
RL Lab. Invest. 71:560-566(1994).
RN [23]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10491647; DOI=10.1095/biolreprod61.4.1083;
RA Overgaard M.T., Oxvig C., Christiansen M., Lawrence J.B., Conover C.A.,
RA Gleich G.J., Sottrup-Jensen L., Haaning J.;
RT "Messenger ribonucleic acid levels of pregnancy-associated plasma protein-A
RT and the proform of eosinophil major basic protein: expression in human
RT reproductive and nonreproductive tissues.";
RL Biol. Reprod. 61:1083-1089(1999).
RN [24]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10913121; DOI=10.1074/jbc.m001384200;
RA Overgaard M.T., Haaning J., Boldt H.B., Olsen I.M., Laursen L.S.,
RA Christiansen M., Gleich G.J., Sottrup-Jensen L., Conover C.A., Oxvig C.;
RT "Expression of recombinant human pregnancy-associated plasma protein-A and
RT identification of the proform of eosinophil major basic protein as its
RT physiological inhibitor.";
RL J. Biol. Chem. 275:31128-31133(2000).
RN [25]
RP INTERCHAIN DISULFIDE BONDS.
RX PubMed=12421832; DOI=10.1074/jbc.m208777200;
RA Overgaard M.T., Sorensen E.S., Stachowiak D., Boldt H.B., Kristensen L.,
RA Sottrup-Jensen L., Oxvig C.;
RT "Complex of pregnancy-associated plasma protein-A and the proform of
RT eosinophil major basic protein. Disulfide structure and carbohydrate
RT attachment sites.";
RL J. Biol. Chem. 278:2106-2117(2003).
RN [26]
RP NITRATION.
RX PubMed=18694936; DOI=10.1074/jbc.m801196200;
RA Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M.,
RA Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N., Acharya K.R.,
RA Schmid-Grendelmeier P., Simon H.-U., Schwarz H., Tsutsui M., Shimokawa H.,
RA Bellon G., Lee J.J., Przybylski M., Doering G.;
RT "Post-translational tyrosine nitration of eosinophil granule toxins
RT mediated by eosinophil peroxidase.";
RL J. Biol. Chem. 283:28629-28640(2008).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 107-222, AND HEPARIN-BINDING.
RX PubMed=11319227; DOI=10.1074/jbc.m100848200;
RA Swaminathan G.J., Weaver A.J., Loegering D.A., Checkel J.L., Leonidas D.D.,
RA Gleich G.J., Acharya K.R.;
RT "Crystal structure of the eosinophil major basic protein at 1.8-A. An
RT atypical lectin with a paradigm shift in specificity.";
RL J. Biol. Chem. 276:26197-26203(2001).
RN [28]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-179.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Cytotoxin and helminthotoxin. Also induces non-cytolytic
CC histamine release from human basophils. Involved in antiparasitic
CC defense mechanisms and immune hypersensitivity reactions. The proform
CC acts as a proteinase inhibitor, reducing the activity of PAPPA.
CC {ECO:0000269|PubMed:10913121}.
CC -!- SUBUNIT: In pregnancy serum, the proform exists as a disulfide-linked
CC 2:2 heterotetramer with PAPPA, as a disulfide-linked 2:2 heterotetramer
CC with AGT, and as a complex (probably a 2:2:2 heterohexamer) with AGT
CC and C3dg. {ECO:0000269|PubMed:10913121, ECO:0000269|PubMed:7508748,
CC ECO:0000269|PubMed:7539791, ECO:0000269|PubMed:7685339,
CC ECO:0000269|PubMed:8137941}.
CC -!- INTERACTION:
CC P13727; Q13219: PAPPA; NbExp=2; IntAct=EBI-716689, EBI-1221991;
CC -!- SUBCELLULAR LOCATION: [Bone marrow proteoglycan]: Secreted. Note=The
CC proform is secreted.
CC -!- SUBCELLULAR LOCATION: [Eosinophil granule major basic protein]:
CC Cytoplasmic vesicle, secretory vesicle. Note=The proform is secreted.
CC The mature protein is found in the matrix of the eosinophil's large
CC specific granule (crystalloid core).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P13727-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13727-2; Sequence=VSP_056735;
CC -!- TISSUE SPECIFICITY: High levels of the proform in placenta and
CC pregnancy serum; in placenta, localized to X cells of septa and
CC anchoring villi. Lower levels in a variety of other tissues including
CC kidney, myometrium, endometrium, ovaries, breast, prostate, bone marrow
CC and colon. {ECO:0000269|PubMed:10491647, ECO:0000269|PubMed:7526035}.
CC -!- DEVELOPMENTAL STAGE: Levels of the proform increase in serum and
CC placenta during pregnancy. {ECO:0000269|PubMed:10491647,
CC ECO:0000269|PubMed:7539791}.
CC -!- PTM: Nitrated. {ECO:0000269|PubMed:18694936}.
CC -!- MISCELLANEOUS: Binds heparin. Does not bind calcium.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Major basic protein entry;
CC URL="https://en.wikipedia.org/wiki/Major_basic_protein";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Eosinophil major basic protein;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_207";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y00809; CAA68751.1; -; mRNA.
DR EMBL; M36805; AAA36203.1; -; mRNA.
DR EMBL; M34462; AAA35796.1; -; Genomic_DNA.
DR EMBL; M35670; AAA35965.1; -; mRNA.
DR EMBL; X14088; CAA32250.1; -; mRNA.
DR EMBL; X65787; CAA46670.1; -; mRNA.
DR EMBL; Z26248; CAA81207.1; -; mRNA.
DR EMBL; AK312195; BAG35128.1; -; mRNA.
DR EMBL; CR450311; CAG29307.1; -; mRNA.
DR EMBL; DQ846874; ABI63361.1; -; mRNA.
DR EMBL; AP000781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005929; AAH05929.1; -; mRNA.
DR CCDS; CCDS58133.1; -. [P13727-2]
DR CCDS; CCDS7955.1; -. [P13727-1]
DR PIR; I54055; JL0085.
DR RefSeq; NP_001230174.1; NM_001243245.2. [P13727-2]
DR RefSeq; NP_001289855.1; NM_001302926.1. [P13727-1]
DR RefSeq; NP_001289856.1; NM_001302927.1. [P13727-1]
DR RefSeq; NP_002719.3; NM_002728.5. [P13727-1]
DR PDB; 1H8U; X-ray; 1.80 A; A/B=106-222.
DR PDB; 2BRS; X-ray; 2.20 A; A/B=106-222.
DR PDB; 4QXX; X-ray; 1.45 A; Z=131-135.
DR PDBsum; 1H8U; -.
DR PDBsum; 2BRS; -.
DR PDBsum; 4QXX; -.
DR AlphaFoldDB; P13727; -.
DR SMR; P13727; -.
DR BioGRID; 111544; 302.
DR CORUM; P13727; -.
DR IntAct; P13727; 46.
DR STRING; 9606.ENSP00000312134; -.
DR DrugBank; DB06752; Chymopapain.
DR DrugBank; DB00020; Sargramostim.
DR MEROPS; I63.001; -.
DR GlyGen; P13727; 6 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P13727; -.
DR PhosphoSitePlus; P13727; -.
DR BioMuta; PRG2; -.
DR DMDM; 281185479; -.
DR EPD; P13727; -.
DR jPOST; P13727; -.
DR MassIVE; P13727; -.
DR PaxDb; P13727; -.
DR PeptideAtlas; P13727; -.
DR PRIDE; P13727; -.
DR ProteomicsDB; 1773; -.
DR ProteomicsDB; 52978; -. [P13727-1]
DR TopDownProteomics; P13727-1; -. [P13727-1]
DR Antibodypedia; 14105; 312 antibodies from 28 providers.
DR DNASU; 5553; -.
DR Ensembl; ENST00000311862.10; ENSP00000312134.5; ENSG00000186652.10. [P13727-1]
DR Ensembl; ENST00000525955.1; ENSP00000433016.1; ENSG00000186652.10. [P13727-1]
DR Ensembl; ENST00000533605.5; ENSP00000433231.1; ENSG00000186652.10. [P13727-2]
DR GeneID; 5553; -.
DR KEGG; hsa:5553; -.
DR MANE-Select; ENST00000311862.10; ENSP00000312134.5; NM_002728.6; NP_002719.3.
DR UCSC; uc001nkc.4; human. [P13727-1]
DR CTD; 5553; -.
DR DisGeNET; 5553; -.
DR GeneCards; PRG2; -.
DR HGNC; HGNC:9362; PRG2.
DR HPA; ENSG00000186652; Tissue enriched (placenta).
DR MIM; 605601; gene.
DR neXtProt; NX_P13727; -.
DR OpenTargets; ENSG00000186652; -.
DR PharmGKB; PA33734; -.
DR VEuPathDB; HostDB:ENSG00000186652; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00440000039859; -.
DR HOGENOM; CLU_107200_1_0_1; -.
DR InParanoid; P13727; -.
DR OMA; WGRCKRF; -.
DR OrthoDB; 1328472at2759; -.
DR PhylomeDB; P13727; -.
DR TreeFam; TF336281; -.
DR PathwayCommons; P13727; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P13727; -.
DR SIGNOR; P13727; -.
DR BioGRID-ORCS; 5553; 6 hits in 1077 CRISPR screens.
DR ChiTaRS; PRG2; human.
DR EvolutionaryTrace; P13727; -.
DR GeneWiki; Major_basic_protein; -.
DR GenomeRNAi; 5553; -.
DR Pharos; P13727; Tbio.
DR PRO; PR:P13727; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P13727; protein.
DR Bgee; ENSG00000186652; Expressed in placenta and 85 other tissues.
DR Genevisible; P13727; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
DR GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; HDA:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0002215; P:defense response to nematode; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; IEA:Ensembl.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; IEA:Ensembl.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
DR CDD; cd03598; CLECT_EMBP_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR033816; EMBP_CTLD.
DR InterPro; IPR002352; Eosinophil_major_basic.
DR Pfam; PF00059; Lectin_C; 1.
DR PRINTS; PR00770; EMAJORBASICP.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antibiotic; Antimicrobial;
KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Heparin-binding; Immunity; Lectin; Nitration; Proteoglycan;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:7539791,
FT ECO:0000269|PubMed:7685339, ECO:0000269|PubMed:8507662"
FT CHAIN 17..222
FT /note="Bone marrow proteoglycan"
FT /id="PRO_0000259923"
FT PROPEP 17..105
FT /note="Acidic"
FT /evidence="ECO:0000269|PubMed:2501794,
FT ECO:0000269|PubMed:3410852"
FT /id="PRO_0000017385"
FT CHAIN 106..222
FT /note="Eosinophil granule major basic protein"
FT /id="PRO_0000017386"
FT DOMAIN 104..222
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 25..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..62
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 23
FT /note="O-linked (GalNAc...) threonine; partial"
FT /evidence="ECO:0000269|PubMed:7524900"
FT CARBOHYD 24
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:7524900,
FT ECO:0000269|PubMed:8507662"
FT CARBOHYD 25
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7524900,
FT ECO:0000269|PubMed:8507662"
FT CARBOHYD 34
FT /note="O-linked (GalNAc...) threonine; partial"
FT /evidence="ECO:0000269|PubMed:7524900"
FT CARBOHYD 62
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:7524900,
FT ECO:0000269|PubMed:8507662"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7524900,
FT ECO:0000269|PubMed:8507662"
FT DISULFID 51
FT /note="Interchain (with C-461 in PAPPA)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:8137941"
FT DISULFID 125..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:8137941"
FT DISULFID 169
FT /note="Interchain (with C-732 in PAPPA)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:8137941"
FT DISULFID 197..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:8137941"
FT VAR_SEQ 112..122
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.9"
FT /id="VSP_056735"
FT VARIANT 179
FT /note="R -> C (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs142359007)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036401"
FT VARIANT 206
FT /note="H -> Y (in dbSNP:rs536455)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1565101,
FT ECO:0000269|PubMed:2323577, ECO:0000269|PubMed:3171483,
FT ECO:0000269|PubMed:3199069, ECO:0000269|PubMed:7531438,
FT ECO:0000269|Ref.8"
FT /id="VAR_060729"
FT CONFLICT 84
FT /note="D -> H (in Ref. 1; AAA36203)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="P -> L (in Ref. 7; BAG35128)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="S -> T (in Ref. 6; CAA81207)"
FT /evidence="ECO:0000305"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:1H8U"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:1H8U"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:1H8U"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:1H8U"
FT STRAND 153..164
FT /evidence="ECO:0007829|PDB:1H8U"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1H8U"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1H8U"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1H8U"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:1H8U"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:1H8U"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1H8U"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:1H8U"
SQ SEQUENCE 222 AA; 25206 MW; CDD545642555E2D0 CRC64;
MKLPLLLALL FGAVSALHLR SETSTFETPL GAKTLPEDEE TPEQEMEETP CRELEEEEEW
GSGSEDASKK DGAVESISVP DMVDKNLTCP EEEDTVKVVG IPGCQTCRYL LVRSLQTFSQ
AWFTCRRCYR GNLVSIHNFN INYRIQCSVS ALNQGQVWIG GRITGSGRCR RFQWVDGSRW
NFAYWAAHQP WSRGGHCVAL CTRGGHWRRA HCLRRLPFIC SY
