ID   PRG2_RAT                Reviewed;         227 AA.
AC   Q63189;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 135.
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   Flags: Precursor;
GN   Name=Prg2; Synonyms=Mbp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Bone marrow;
RX   PubMed=8547309; DOI=10.1016/0167-4781(95)00183-2;
RA   Nittoh T., Watanabe M., Okayama H., Misawa S., Isobe Y., Hayashi H.,
RA   Mue S., Ohuchi K.;
RT   "Cloning of cDNA for rat eosinophil major basic protein.";
RL   Biochim. Biophys. Acta 1264:261-264(1995).
RN   [2]
RP   ERRATUM OF PUBMED:8547309.
RX   PubMed=8611616; DOI=10.1016/0167-4781(96)82205-6;
RA   Nittoh T., Watanabe M., Okoyama H., Misawa S., Isobe Y., Hayashi H.,
RA   Mue S., Ohuchi K.;
RL   Biochim. Biophys. Acta 1306:115-116(1996).
CC   -!- FUNCTION: Cytotoxin and helminthotoxin. MBP also induces non-cytolytic
CC       histamine release from basophils. It is involved in antiparasitic
CC       defense mechanisms and immune hypersensitivity reactions (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000250}. Note=Matrix of
CC       eosinophil's large specific granule (crystalloid core). {ECO:0000250}.
CC   -!- PTM: Nitrated. {ECO:0000250}.
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DR   EMBL; D50568; BAA09129.1; -; mRNA.
DR   PIR; S68150; S68150.
DR   RefSeq; NP_113807.2; NM_031619.2.
DR   AlphaFoldDB; Q63189; -.
DR   SMR; Q63189; -.
DR   BioGRID; 248633; 1.
DR   IntAct; Q63189; 1.
DR   STRING; 10116.ENSRNOP00000011168; -.
DR   MEROPS; I63.001; -.
DR   PhosphoSitePlus; Q63189; -.
DR   PaxDb; Q63189; -.
DR   PRIDE; Q63189; -.
DR   GeneID; 58826; -.
DR   KEGG; rno:58826; -.
DR   UCSC; RGD:69336; rat.
DR   CTD; 5553; -.
DR   RGD; 69336; Prg2.
DR   eggNOG; KOG4297; Eukaryota.
DR   InParanoid; Q63189; -.
DR   OrthoDB; 1328472at2759; -.
DR   PhylomeDB; Q63189; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:Q63189; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; NAS:RGD.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0002215; P:defense response to nematode; ISO:RGD.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0032693; P:negative regulation of interleukin-10 production; ISO:RGD.
DR   GO; GO:0032753; P:positive regulation of interleukin-4 production; ISO:RGD.
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   2: Evidence at transcript level;
KW   Antibiotic; Antimicrobial; Disulfide bond; Immunity; Lectin; Nitration;
KW   Reference proteome; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..227
FT                   /note="Bone marrow proteoglycan"
FT                   /id="PRO_0000259925"
FT   PROPEP          17..110
FT                   /note="Acidic"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000017389"
FT   CHAIN           111..227
FT                   /note="Eosinophil granule major basic protein"
FT                   /id="PRO_0000017390"
FT   DOMAIN          128..227
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   REGION          21..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..72
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        130..225
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        202..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   227 AA;  25129 MW;  34F2BE514090DE82 CRC64;
     MKFPLLLALL VGGAFALHLS SEASDSKSPL VDESLPREAE ISRPEVEESP PGEQLMSLEE
     EEEEEEEEGS GSEGALGNEG AVSGQDVTDE NLQSPKEEDT TSLMGDSGFK TGRYLLVRRP
     ECFNKAQLVC RSCYRGTLAS IHSFSVNFRI QSFVRGINQG QVWIGGRIVG WGRCKRFRWI
     DGSSWNFAYW AAGQPRRGGG RCVTLCTRGG HWRRSGCGKR RPFICAY