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P13727 (PRG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bone marrow proteoglycan

Short name=BMPG
Alternative name(s):
Proteoglycan 2

Cleaved into the following chain:

  1. Eosinophil granule major basic protein
    Short name=EMBP
    Short name=MBP
    Alternative name(s):
    Pregnancy-associated major basic protein
Gene names
Name:PRG2
Synonyms:MBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytotoxin and helminthotoxin. Also induces non-cytolytic histamine release from human basophils. Involved in antiparasitic defense mechanisms and immune hypersensitivity reactions. The proform acts as a proteinase inhibitor, reducing the activity of PAPPA. Ref.22

Subunit structure

In pregnancy serum, the proform exists as a disulfide-linked 2:2 heterotetramer with PAPPA, as a disulfide-linked 2:2 heterotetramer with AGT, and as a complex (probably a 2:2:2 heterohexamer) with AGT and C3dg. Ref.11 Ref.12 Ref.16 Ref.19 Ref.22 Ref.23

Subcellular location

Bone marrow proteoglycan: Secreted. Note: The proform is secreted.

Eosinophil granule major basic protein: Cytoplasmic vesiclesecretory vesicle. Note: The proform is secreted. The mature protein is found in the matrix of the eosinophil's large specific granule (crystalloid core).

Tissue specificity

High levels of the proform in placenta and pregnancy serum; in placenta, localized to X cells of septa and anchoring villi. Lower levels in a variety of other tissues including kidney, myometrium, endometrium, ovaries, breast, prostate, bone marrow and colon. Ref.20 Ref.21

Developmental stage

Levels of the proform increase in serum and placenta during pregnancy. Ref.12 Ref.21

Post-translational modification

Nitrated.

Miscellaneous

Binds heparin. Does not bind calcium.

Sequence similarities

Contains 1 C-type lectin domain.

Ontologies

Keywords
   Biological processImmunity
   Cellular componentCytoplasmic vesicle
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandHeparin-binding
Lectin
   Molecular functionAntibiotic
Antimicrobial
   PTMDisulfide bond
Glycoprotein
Nitration
Proteoglycan
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

immune response

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Traceable author statement PubMed 8547309. Source: ProtInc

transport vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbohydrate binding

Traceable author statement Ref.5. Source: ProtInc

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.10 Ref.11 Ref.12
Chain17 – 222206Bone marrow proteoglycan
PRO_0000259923
Propeptide17 – 10589Acidic
PRO_0000017385
Chain106 – 222117Eosinophil granule major basic protein
PRO_0000017386

Regions

Domain104 – 222119C-type lectin

Amino acid modifications

Glycosylation231O-linked (GalNAc...); partial Ref.18
Glycosylation241O-linked (GalNAc...) Ref.10 Ref.18
Glycosylation251O-linked (GalNAc...) Ref.10 Ref.18
Glycosylation341O-linked (GalNAc...); partial Ref.18
Glycosylation621O-linked (Xyl...) (chondroitin sulfate) Ref.10 Ref.18
Glycosylation861N-linked (GlcNAc...) Ref.10 Ref.18
Disulfide bond51Interchain (with C-461 in PAPPA) Ref.11 Ref.19 Ref.23
Disulfide bond125 ↔ 220 Ref.11 Ref.19 Ref.23
Disulfide bond169Interchain (with C-732 in PAPPA) Ref.11 Ref.19 Ref.23
Disulfide bond197 ↔ 212 Ref.11 Ref.19 Ref.23

Natural variations

Natural variant1791R → C in a colorectal cancer sample; somatic mutation. Ref.26
VAR_036401
Natural variant2061H → Y. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.9
Corresponds to variant rs536455 [ dbSNP | Ensembl ].
VAR_060729

Experimental info

Sequence conflict841D → H in AAA36203. Ref.1
Sequence conflict1921S → T in CAA81207. Ref.6

Secondary structure

....................... 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13727 [UniParc].

Last modified December 15, 2009. Version 2.
Checksum: CDD545642555E2D0

FASTA22225,206
        10         20         30         40         50         60 
MKLPLLLALL FGAVSALHLR SETSTFETPL GAKTLPEDEE TPEQEMEETP CRELEEEEEW 

        70         80         90        100        110        120 
GSGSEDASKK DGAVESISVP DMVDKNLTCP EEEDTVKVVG IPGCQTCRYL LVRSLQTFSQ 

       130        140        150        160        170        180 
AWFTCRRCYR GNLVSIHNFN INYRIQCSVS ALNQGQVWIG GRITGSGRCR RFQWVDGSRW 

       190        200        210        220 
NFAYWAAHQP WSRGGHCVAL CTRGGHWRRA HCLRRLPFIC SY 

« Hide

References

« Hide 'large scale' references
[1]"Acidic precursor revealed in human eosinophil granule major basic protein cDNA."
Barker R.L., Gleich G.J., Pease L.R.
J. Exp. Med. 168:1493-1498(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-206.
Tissue: Promyelocyte.
[2]Barker R.L.
Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 84.
[3]"Cloning and sequence analysis of the human gene encoding eosinophil major basic protein."
Barker R.L., Loegering D.A., Arakawa K.C., Pease L.R., Gleich G.J.
Gene 86:285-289(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-206.
[4]"Isolation of a complementary DNA clone encoding a precursor to human eosinophil major basic protein."
McGrogan M., Simonsen C., Scott R., Giffith J., Ellis N., Kennedy J., Campanelli D., Nathan C., Gabay J.
J. Exp. Med. 168:2295-2308(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-206.
[5]"Purification and cDNA cloning of a novel factor produced by a human T-cell hybridoma: sequence homology with animal lectins."
Yoshimatsu K., Ohya Y., Shikata Y., Seto T., Hasegawa Y., Tanaka I., Kawamura T., Kitoh K., Toyoshima S., Osawa T.
Mol. Immunol. 29:537-546(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT TYR-206.
[6]"Human eosinophil major basic protein, a mediator of allergic inflammation, is expressed by alternative splicing from two promoters."
Li M.S., Sun L., Satoh T., Fisher L.M., Spry C.J.
Biochem. J. 305:921-927(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-206.
Tissue: Bone marrow.
[7]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TYR-206.
[8]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TYR-206.
Tissue: Placenta.
[10]"Pro-major basic protein has three types of sugar chains at the pro-portion."
Shikata Y., Hayashi Y., Yoshimatsu K., Ohya Y., Seto T., Fukushima K., Yoshida Y.
Biochim. Biophys. Acta 1163:243-249(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-222, GLYCOSYLATION AT SER-24; THR-25; SER-62 AND ASN-86.
Tissue: Liver.
[11]"Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein."
Oxvig C., Sand O., Kristensen T., Gleich G.J., Sottrup-Jensen L.
J. Biol. Chem. 268:12243-12246(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-26; 47-52; 98-108; 172-179 AND 210-222, SUBUNIT, INTERCHAIN DISULFIDE BOND.
Tissue: Serum.
[12]"Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma."
Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., Stigbrand T., Gleich G.J., Sottrup-Jensen L.
J. Biol. Chem. 270:13645-13651(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-29, SUBUNIT, DEVELOPMENTAL STAGE.
Tissue: Serum.
[13]"Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein."
Wasmoen T.L., Bell M.P., Loegering D.A., Gleich G.J., Prendergast F.G., McKean D.J.
J. Biol. Chem. 263:12559-12563(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 106-222.
[14]"Antibiotic proteins of human polymorphonuclear leukocytes."
Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N., Seeger M., Nathan C.F.
Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 106-125.
[15]"Eosinophil granule cationic proteins: major basic protein is distinct from the smaller subunit of eosinophil peroxidase."
Weller P.F., Ackerman S.J., Smith J.A.
J. Leukoc. Biol. 43:1-4(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 108-124.
[16]"Amino acid sequence of human pregnancy-associated plasma protein-A derived from cloned cDNA."
Kristensen T., Oxvig C., Sand O., Moller N.P.H., Sottrup-Jensen L.
Biochemistry 33:1592-1598(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 172-179 AND 210-222, SUBUNIT.
Tissue: Serum.
[17]"Evidence of eosinophil granule major basic protein in human placenta."
Wasmoen T.L., McKean D.J., Benirschke K., Coulam C.B., Gleich G.J.
J. Exp. Med. 170:2051-2063(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 177-196.
Tissue: Placenta.
[18]"Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum."
Oxvig C., Haaning J., Hojrup P., Sottrup-Jensen L.
Biochem. Mol. Biol. Int. 33:329-336(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-23; SER-24; THR-25; THR-34; SER-62 AND ASN-86.
[19]"Localization of disulfide bridges and free sulfhydryl groups in human eosinophil granule major basic protein."
Oxvig C., Gleich G.J., Sottrup-Jensen L.
FEBS Lett. 341:213-217(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[20]"Localization of pregnancy-associated plasma protein-A and colocalization of pregnancy-associated plasma protein-A messenger ribonucleic acid and eosinophil granule major basic protein messenger ribonucleic acid in placenta."
Bonno M., Oxvig C., Kephart G.M., Wagner J.M., Kristensen T., Sottrup-Jensen L., Gleich G.J.
Lab. Invest. 71:560-566(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[21]"Messenger ribonucleic acid levels of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein: expression in human reproductive and nonreproductive tissues."
Overgaard M.T., Oxvig C., Christiansen M., Lawrence J.B., Conover C.A., Gleich G.J., Sottrup-Jensen L., Haaning J.
Biol. Reprod. 61:1083-1089(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[22]"Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor."
Overgaard M.T., Haaning J., Boldt H.B., Olsen I.M., Laursen L.S., Christiansen M., Gleich G.J., Sottrup-Jensen L., Conover C.A., Oxvig C.
J. Biol. Chem. 275:31128-31133(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[23]"Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein. Disulfide structure and carbohydrate attachment sites."
Overgaard M.T., Sorensen E.S., Stachowiak D., Boldt H.B., Kristensen L., Sottrup-Jensen L., Oxvig C.
J. Biol. Chem. 278:2106-2117(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERCHAIN DISULFIDE BONDS.
[24]"Post-translational tyrosine nitration of eosinophil granule toxins mediated by eosinophil peroxidase."
Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M., Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N., Acharya K.R., Schmid-Grendelmeier P., Simon H.-U., Schwarz H., Tsutsui M., Shimokawa H., Bellon G. expand/collapse author list , Lee J.J., Przybylski M., Doering G.
J. Biol. Chem. 283:28629-28640(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION.
[25]"Crystal structure of the eosinophil major basic protein at 1.8-A. An atypical lectin with a paradigm shift in specificity."
Swaminathan G.J., Weaver A.J., Loegering D.A., Checkel J.L., Leonidas D.D., Gleich G.J., Acharya K.R.
J. Biol. Chem. 276:26197-26203(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 107-222, HEPARIN-BINDING.
[26]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-179.
+Additional computationally mapped references.

Web resources

Wikipedia

Major basic protein entry

Functional Glycomics Gateway - Glycan Binding

Eosinophil major basic protein

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00809 mRNA. Translation: CAA68751.1.
M36805 mRNA. Translation: AAA36203.1.
M34462 Genomic DNA. Translation: AAA35796.1.
M35670 mRNA. Translation: AAA35965.1.
X14088 mRNA. Translation: CAA32250.1.
X65787 mRNA. Translation: CAA46670.1.
Z26248 mRNA. Translation: CAA81207.1.
CR450311 mRNA. Translation: CAG29307.1.
AP000781 Genomic DNA. No translation available.
BC005929 mRNA. Translation: AAH05929.1.
PIRJL0085. I54055.
RefSeqNP_001230174.1. NM_001243245.1.
NP_002719.3. NM_002728.4.
UniGeneHs.512633.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H8UX-ray1.80A/B106-222[»]
2BRSX-ray2.20A/B106-222[»]
ProteinModelPortalP13727.
SMRP13727. Positions 107-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111544. 4 interactions.
IntActP13727. 2 interactions.
MINTMINT-1375191.
STRING9606.ENSP00000312134.

Chemistry

DrugBankDB00020. Sargramostim.

Protein family/group databases

MEROPSI63.001.

Polymorphism databases

DMDM281185479.

Proteomic databases

PaxDbP13727.
PRIDEP13727.

Protocols and materials databases

DNASU5553.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311862; ENSP00000312134; ENSG00000186652.
ENST00000525955; ENSP00000433016; ENSG00000186652.
GeneID5553.
KEGGhsa:5553.
UCSCuc001nkc.3. human.

Organism-specific databases

CTD5553.
GeneCardsGC11M057154.
H-InvDBHIX0009634.
HGNCHGNC:9362. PRG2.
HPAHPA038515.
MIM605601. gene.
neXtProtNX_P13727.
PharmGKBPA33734.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266233.
HOGENOMHOG000261603.
HOVERGENHBG005583.
InParanoidP13727.
KOK10786.
OMAFTCRRCY.
OrthoDBEOG779P0F.
PhylomeDBP13727.
TreeFamTF336281.

Gene expression databases

CleanExHS_MBP.
HS_PRG2.
GenevestigatorP13727.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR002352. Eosinophil_major_basic.
[Graphical view]
PANTHERPTHR10068. PTHR10068. 1 hit.
PfamPF00059. Lectin_C. 1 hit.
[Graphical view]
PRINTSPR00770. EMAJORBASICP.
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRG2. human.
EvolutionaryTraceP13727.
GeneWikiMajor_basic_protein.
GenomeRNAi5553.
NextBio21522.
PROP13727.
SOURCESearch...

Entry information

Entry namePRG2_HUMAN
AccessionPrimary (citable) accession number: P13727
Secondary accession number(s): P81448, Q14227, Q6ICT2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: December 15, 2009
Last modified: April 16, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM