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Bone marrow proteoglycan (BMPG) (Proteoglycan 2) [Cleaved into: Eosinophil granule major basic protein (EMBP) (MBP) (Pregnancy-associated major basic protein)]

 PRG2_HUMAN              Reviewed;         222 AA.
P13727; A6XMW0; B2R5I1; P81448; Q14227; Q6ICT2;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
15-DEC-2009, sequence version 2.
25-OCT-2017, entry version 184.
RecName: Full=Bone marrow proteoglycan;
Short=BMPG;
AltName: Full=Proteoglycan 2;
Contains:
RecName: Full=Eosinophil granule major basic protein;
Short=EMBP;
Short=MBP;
AltName: Full=Pregnancy-associated major basic protein;
Flags: Precursor;
Name=PRG2; Synonyms=MBP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT TYR-206.
TISSUE=Promyelocyte;
PubMed=3171483; DOI=10.1084/jem.168.4.1493;
Barker R.L., Gleich G.J., Pease L.R.;
"Acidic precursor revealed in human eosinophil granule major basic
protein cDNA.";
J. Exp. Med. 168:1493-1498(1988).
[2]
SEQUENCE REVISION TO 84.
Barker R.L.;
Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-206.
PubMed=2323577; DOI=10.1016/0378-1119(90)90292-Y;
Barker R.L., Loegering D.A., Arakawa K.C., Pease L.R., Gleich G.J.;
"Cloning and sequence analysis of the human gene encoding eosinophil
major basic protein.";
Gene 86:285-289(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT TYR-206.
PubMed=3199069; DOI=10.1084/jem.168.6.2295;
McGrogan M., Simonsen C., Scott R., Giffith J., Ellis N., Kennedy J.,
Campanelli D., Nathan C., Gabay J.;
"Isolation of a complementary DNA clone encoding a precursor to human
eosinophil major basic protein.";
J. Exp. Med. 168:2295-2308(1988).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
VARIANT TYR-206.
PubMed=1565101; DOI=10.1016/0161-5890(92)90012-M;
Yoshimatsu K., Ohya Y., Shikata Y., Seto T., Hasegawa Y., Tanaka I.,
Kawamura T., Kitoh K., Toyoshima S., Osawa T.;
"Purification and cDNA cloning of a novel factor produced by a human
T-cell hybridoma: sequence homology with animal lectins.";
Mol. Immunol. 29:537-546(1992).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT TYR-206.
TISSUE=Bone marrow;
PubMed=7531438; DOI=10.1042/bj3050921;
Li M.S., Sun L., Satoh T., Fisher L.M., Spry C.J.;
"Human eosinophil major basic protein, a mediator of allergic
inflammation, is expressed by alternative splicing from two
promoters.";
Biochem. J. 305:921-927(1995).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
TYR-206.
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
TYR-206.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Yu Z., Zheng Z., Tang T., Fu Y.;
"A computer system platform used to predict novel genes.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
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., 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.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-206.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PROTEIN SEQUENCE OF 17-222, AND GLYCOSYLATION AT SER-24; THR-25;
SER-62 AND ASN-86.
TISSUE=Liver;
PubMed=8507662; DOI=10.1016/0167-4838(93)90158-N;
Shikata Y., Hayashi Y., Yoshimatsu K., Ohya Y., Seto T., Fukushima K.,
Yoshida Y.;
"Pro-major basic protein has three types of sugar chains at the pro-
portion.";
Biochim. Biophys. Acta 1163:243-249(1993).
[13]
PROTEIN SEQUENCE OF 17-26; 47-52; 98-108; 172-179 AND 210-222,
SUBUNIT, AND INTERCHAIN DISULFIDE BOND.
TISSUE=Serum;
PubMed=7685339;
Oxvig C., Sand O., Kristensen T., Gleich G.J., Sottrup-Jensen L.;
"Circulating human pregnancy-associated plasma protein-A is disulfide-
bridged to the proform of eosinophil major basic protein.";
J. Biol. Chem. 268:12243-12246(1993).
[14]
PROTEIN SEQUENCE OF 17-29, SUBUNIT, AND DEVELOPMENTAL STAGE.
TISSUE=Serum;
PubMed=7539791; DOI=10.1074/jbc.270.23.13645;
Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I.,
Stigbrand T., Gleich G.J., Sottrup-Jensen L.;
"Identification of angiotensinogen and complement C3dg as novel
proteins binding the proform of eosinophil major basic protein in
human pregnancy serum and plasma.";
J. Biol. Chem. 270:13645-13651(1995).
[15]
PROTEIN SEQUENCE OF 106-222.
PubMed=3410852;
Wasmoen T.L., Bell M.P., Loegering D.A., Gleich G.J.,
Prendergast F.G., McKean D.J.;
"Biochemical and amino acid sequence analysis of human eosinophil
granule major basic protein.";
J. Biol. Chem. 263:12559-12563(1988).
[16]
PROTEIN SEQUENCE OF 106-125.
PubMed=2501794; DOI=10.1073/pnas.86.14.5610;
Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C.,
Marra M.N., Seeger M., Nathan C.F.;
"Antibiotic proteins of human polymorphonuclear leukocytes.";
Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
[17]
PROTEIN SEQUENCE OF 108-124.
PubMed=3422083;
Weller P.F., Ackerman S.J., Smith J.A.;
"Eosinophil granule cationic proteins: major basic protein is distinct
from the smaller subunit of eosinophil peroxidase.";
J. Leukoc. Biol. 43:1-4(1988).
[18]
PROTEIN SEQUENCE OF 172-179 AND 210-222, AND SUBUNIT.
TISSUE=Serum;
PubMed=7508748; DOI=10.1021/bi00172a040;
Kristensen T., Oxvig C., Sand O., Moller N.P.H., Sottrup-Jensen L.;
"Amino acid sequence of human pregnancy-associated plasma protein-A
derived from cloned cDNA.";
Biochemistry 33:1592-1598(1994).
[19]
PROTEIN SEQUENCE OF 177-196.
TISSUE=Placenta;
PubMed=2584934; DOI=10.1084/jem.170.6.2051;
Wasmoen T.L., McKean D.J., Benirschke K., Coulam C.B., Gleich G.J.;
"Evidence of eosinophil granule major basic protein in human
placenta.";
J. Exp. Med. 170:2051-2063(1989).
[20]
GLYCOSYLATION AT THR-23; SER-24; THR-25; THR-34; SER-62 AND ASN-86.
PubMed=7524900;
Oxvig C., Haaning J., Hojrup P., Sottrup-Jensen L.;
"Location and nature of carbohydrate groups in proform of human major
basic protein isolated from pregnancy serum.";
Biochem. Mol. Biol. Int. 33:329-336(1994).
[21]
DISULFIDE BONDS.
PubMed=8137941; DOI=10.1016/0014-5793(94)80459-1;
Oxvig C., Gleich G.J., Sottrup-Jensen L.;
"Localization of disulfide bridges and free sulfhydryl groups in human
eosinophil granule major basic protein.";
FEBS Lett. 341:213-217(1994).
[22]
TISSUE SPECIFICITY.
PubMed=7526035;
Bonno M., Oxvig C., Kephart G.M., Wagner J.M., Kristensen T.,
Sottrup-Jensen L., Gleich G.J.;
"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.";
Lab. Invest. 71:560-566(1994).
[23]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=10491647; DOI=10.1095/biolreprod61.4.1083;
Overgaard M.T., Oxvig C., Christiansen M., Lawrence J.B.,
Conover C.A., Gleich G.J., Sottrup-Jensen L., Haaning J.;
"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.";
Biol. Reprod. 61:1083-1089(1999).
[24]
FUNCTION, AND SUBUNIT.
PubMed=10913121; DOI=10.1074/jbc.M001384200;
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.;
"Expression of recombinant human pregnancy-associated plasma protein-A
and identification of the proform of eosinophil major basic protein as
its physiological inhibitor.";
J. Biol. Chem. 275:31128-31133(2000).
[25]
INTERCHAIN DISULFIDE BONDS.
PubMed=12421832; DOI=10.1074/jbc.M208777200;
Overgaard M.T., Sorensen E.S., Stachowiak D., Boldt H.B.,
Kristensen L., Sottrup-Jensen L., Oxvig C.;
"Complex of pregnancy-associated plasma protein-A and the proform of
eosinophil major basic protein. Disulfide structure and carbohydrate
attachment sites.";
J. Biol. Chem. 278:2106-2117(2003).
[26]
NITRATION.
PubMed=18694936; DOI=10.1074/jbc.M801196200;
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., Lee J.J., Przybylski M.,
Doering G.;
"Post-translational tyrosine nitration of eosinophil granule toxins
mediated by eosinophil peroxidase.";
J. Biol. Chem. 283:28629-28640(2008).
[27]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 107-222, AND HEPARIN-BINDING.
PubMed=11319227; DOI=10.1074/jbc.M100848200;
Swaminathan G.J., Weaver A.J., Loegering D.A., Checkel J.L.,
Leonidas D.D., Gleich G.J., Acharya K.R.;
"Crystal structure of the eosinophil major basic protein at 1.8-A. An
atypical lectin with a paradigm shift in specificity.";
J. Biol. Chem. 276:26197-26203(2001).
[28]
VARIANT [LARGE SCALE ANALYSIS] CYS-179.
PubMed=16959974; DOI=10.1126/science.1133427;
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., 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.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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. {ECO:0000269|PubMed:10913121}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:10913121,
ECO:0000269|PubMed:7508748, ECO:0000269|PubMed:7539791,
ECO:0000269|PubMed:7685339, ECO:0000269|PubMed:8137941}.
-!- SUBCELLULAR LOCATION: Bone marrow proteoglycan: Secreted. Note=The
proform is secreted.
-!- SUBCELLULAR LOCATION: Eosinophil granule major basic protein:
Cytoplasmic vesicle, secretory vesicle. Note=The proform is
secreted. The mature protein is found in the matrix of the
eosinophil's large specific granule (crystalloid core).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P13727-1; Sequence=Displayed;
Name=2;
IsoId=P13727-2; Sequence=VSP_056735;
-!- 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. {ECO:0000269|PubMed:10491647,
ECO:0000269|PubMed:7526035}.
-!- DEVELOPMENTAL STAGE: Levels of the proform increase in serum and
placenta during pregnancy. {ECO:0000269|PubMed:10491647,
ECO:0000269|PubMed:7539791}.
-!- PTM: Nitrated. {ECO:0000269|PubMed:18694936}.
-!- MISCELLANEOUS: Binds heparin. Does not bind calcium.
-!- WEB RESOURCE: Name=Wikipedia; Note=Major basic protein entry;
URL="https://en.wikipedia.org/wiki/Major_basic_protein";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Eosinophil major basic protein;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_207";
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EMBL; Y00809; CAA68751.1; -; mRNA.
EMBL; M36805; AAA36203.1; -; mRNA.
EMBL; M34462; AAA35796.1; -; Genomic_DNA.
EMBL; M35670; AAA35965.1; -; mRNA.
EMBL; X14088; CAA32250.1; -; mRNA.
EMBL; X65787; CAA46670.1; -; mRNA.
EMBL; Z26248; CAA81207.1; -; mRNA.
EMBL; AK312195; BAG35128.1; -; mRNA.
EMBL; CR450311; CAG29307.1; -; mRNA.
EMBL; DQ846874; ABI63361.1; -; mRNA.
EMBL; AP000781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC005929; AAH05929.1; -; mRNA.
CCDS; CCDS58133.1; -. [P13727-2]
CCDS; CCDS7955.1; -. [P13727-1]
PIR; I54055; JL0085.
RefSeq; NP_001230174.1; NM_001243245.2. [P13727-2]
RefSeq; NP_001289855.1; NM_001302926.1. [P13727-1]
RefSeq; NP_001289856.1; NM_001302927.1. [P13727-1]
RefSeq; NP_002719.3; NM_002728.5. [P13727-1]
UniGene; Hs.512633; -.
PDB; 1H8U; X-ray; 1.80 A; A/B=106-222.
PDB; 2BRS; X-ray; 2.20 A; A/B=106-222.
PDB; 4QXX; X-ray; 1.45 A; Z=131-135.
PDBsum; 1H8U; -.
PDBsum; 2BRS; -.
PDBsum; 4QXX; -.
ProteinModelPortal; P13727; -.
SMR; P13727; -.
BioGrid; 111544; 66.
CORUM; P13727; -.
IntAct; P13727; 2.
MINT; MINT-1375191; -.
STRING; 9606.ENSP00000312134; -.
DrugBank; DB00020; Sargramostim.
MEROPS; I63.001; -.
iPTMnet; P13727; -.
PhosphoSitePlus; P13727; -.
BioMuta; PRG2; -.
DMDM; 281185479; -.
EPD; P13727; -.
PaxDb; P13727; -.
PeptideAtlas; P13727; -.
PRIDE; P13727; -.
TopDownProteomics; P13727-1; -. [P13727-1]
DNASU; 5553; -.
Ensembl; ENST00000311862; ENSP00000312134; ENSG00000186652. [P13727-1]
Ensembl; ENST00000525955; ENSP00000433016; ENSG00000186652. [P13727-1]
Ensembl; ENST00000533605; ENSP00000433231; ENSG00000186652. [P13727-2]
GeneID; 5553; -.
KEGG; hsa:5553; -.
UCSC; uc001nkc.4; human. [P13727-1]
CTD; 5553; -.
DisGeNET; 5553; -.
EuPathDB; HostDB:ENSG00000186652.9; -.
GeneCards; PRG2; -.
H-InvDB; HIX0009634; -.
HGNC; HGNC:9362; PRG2.
HPA; HPA038515; -.
MIM; 605601; gene.
neXtProt; NX_P13727; -.
OpenTargets; ENSG00000186652; -.
PharmGKB; PA33734; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00440000039859; -.
HOGENOM; HOG000261603; -.
HOVERGEN; HBG005583; -.
InParanoid; P13727; -.
KO; K10786; -.
OMA; GHWRRAH; -.
OrthoDB; EOG091G0LK4; -.
PhylomeDB; P13727; -.
TreeFam; TF336281; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; PRG2; human.
EvolutionaryTrace; P13727; -.
GeneWiki; Major_basic_protein; -.
GenomeRNAi; 5553; -.
PRO; PR:P13727; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000186652; -.
CleanEx; HS_MBP; -.
CleanEx; HS_PRG2; -.
Genevisible; P13727; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0002215; P:defense response to nematode; IEA:Ensembl.
GO; GO:0032693; P:negative regulation of interleukin-10 production; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
GO; GO:0042035; P:regulation of cytokine biosynthetic process; IBA:GO_Central.
CDD; cd03598; CLECT_EMBP_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR033816; EMBP_CTLD.
InterPro; IPR002352; Eosinophil_major_basic.
Pfam; PF00059; Lectin_C; 1.
PRINTS; PR00770; EMAJORBASICP.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Antibiotic; Antimicrobial;
Complete proteome; Cytoplasmic vesicle; Direct protein sequencing;
Disulfide bond; Glycoprotein; Heparin-binding; Immunity; Lectin;
Nitration; Polymorphism; Proteoglycan; Reference proteome; Secreted;
Signal.
SIGNAL 1 16 {ECO:0000269|PubMed:7539791,
ECO:0000269|PubMed:7685339,
ECO:0000269|PubMed:8507662}.
CHAIN 17 222 Bone marrow proteoglycan.
/FTId=PRO_0000259923.
PROPEP 17 105 Acidic. {ECO:0000269|PubMed:2501794,
ECO:0000269|PubMed:3410852}.
/FTId=PRO_0000017385.
CHAIN 106 222 Eosinophil granule major basic protein.
/FTId=PRO_0000017386.
DOMAIN 104 222 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
CARBOHYD 23 23 O-linked (GalNAc...) threonine; partial.
{ECO:0000269|PubMed:7524900}.
CARBOHYD 24 24 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:7524900,
ECO:0000269|PubMed:8507662}.
CARBOHYD 25 25 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:7524900,
ECO:0000269|PubMed:8507662}.
CARBOHYD 34 34 O-linked (GalNAc...) threonine; partial.
{ECO:0000269|PubMed:7524900}.
CARBOHYD 62 62 O-linked (Xyl...) (chondroitin sulfate)
serine. {ECO:0000269|PubMed:7524900,
ECO:0000269|PubMed:8507662}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:7524900,
ECO:0000269|PubMed:8507662}.
DISULFID 51 51 Interchain (with C-461 in PAPPA).
{ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:8137941}.
DISULFID 125 220 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:8137941}.
DISULFID 169 169 Interchain (with C-732 in PAPPA).
{ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:8137941}.
DISULFID 197 212 {ECO:0000255|PROSITE-ProRule:PRU00040,
ECO:0000269|PubMed:8137941}.
VAR_SEQ 112 122 Missing (in isoform 2).
{ECO:0000303|Ref.9}.
/FTId=VSP_056735.
VARIANT 179 179 R -> C (in a colorectal cancer sample;
somatic mutation; dbSNP:rs142359007).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036401.
VARIANT 206 206 H -> Y (in dbSNP:rs536455).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1565101,
ECO:0000269|PubMed:2323577,
ECO:0000269|PubMed:3171483,
ECO:0000269|PubMed:3199069,
ECO:0000269|PubMed:7531438,
ECO:0000269|Ref.8}.
/FTId=VAR_060729.
CONFLICT 84 84 D -> H (in Ref. 1; AAA36203).
{ECO:0000305}.
CONFLICT 190 190 P -> L (in Ref. 7; BAG35128).
{ECO:0000305}.
CONFLICT 192 192 S -> T (in Ref. 6; CAA81207).
{ECO:0000305}.
STRAND 109 116 {ECO:0000244|PDB:1H8U}.
HELIX 118 129 {ECO:0000244|PDB:1H8U}.
STRAND 130 133 {ECO:0000244|PDB:1H8U}.
HELIX 139 149 {ECO:0000244|PDB:1H8U}.
STRAND 153 164 {ECO:0000244|PDB:1H8U}.
STRAND 166 168 {ECO:0000244|PDB:1H8U}.
STRAND 171 174 {ECO:0000244|PDB:1H8U}.
STRAND 187 189 {ECO:0000244|PDB:1H8U}.
STRAND 196 201 {ECO:0000244|PDB:1H8U}.
TURN 202 205 {ECO:0000244|PDB:1H8U}.
STRAND 207 210 {ECO:0000244|PDB:1H8U}.
STRAND 216 221 {ECO:0000244|PDB:1H8U}.
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


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