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PRG2_MOUSE
ID   PRG2_MOUSE              Reviewed;         223 AA.
AC   Q61878;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 148.
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-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=CBA/J; TISSUE=Liver;
RX   PubMed=7673718;
RA   Larson K.A., Horton M.A., Madden B.J., Gleich G.J., Lee N.A., Lee J.J.;
RT   "The identification and cloning of a murine major basic protein gene
RT   expressed in eosinophils.";
RL   J. Immunol. 155:3002-3012(1995).
RN   [2]
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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:0000269|PubMed:18694936}.
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_mou_Ctlect_151";
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DR   EMBL; L46768; AAA83027.1; -; Genomic_DNA.
DR   CCDS; CCDS16198.1; -.
DR   RefSeq; NP_032946.1; NM_008920.4.
DR   AlphaFoldDB; Q61878; -.
DR   SMR; Q61878; -.
DR   BioGRID; 202360; 1.
DR   STRING; 10090.ENSMUSP00000028467; -.
DR   MEROPS; I63.001; -.
DR   CarbonylDB; Q61878; -.
DR   PhosphoSitePlus; Q61878; -.
DR   jPOST; Q61878; -.
DR   MaxQB; Q61878; -.
DR   PaxDb; Q61878; -.
DR   PRIDE; Q61878; -.
DR   ProteomicsDB; 289406; -.
DR   DNASU; 19074; -.
DR   Ensembl; ENSMUST00000028467; ENSMUSP00000028467; ENSMUSG00000027073.
DR   GeneID; 19074; -.
DR   KEGG; mmu:19074; -.
DR   UCSC; uc008kjp.1; mouse.
DR   CTD; 5553; -.
DR   MGI; MGI:103294; Prg2.
DR   VEuPathDB; HostDB:ENSMUSG00000027073; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00440000039859; -.
DR   HOGENOM; CLU_107200_1_0_1; -.
DR   InParanoid; Q61878; -.
DR   OMA; WGRCKRF; -.
DR   OrthoDB; 1328472at2759; -.
DR   PhylomeDB; Q61878; -.
DR   TreeFam; TF336281; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 19074; 2 hits in 75 CRISPR screens.
DR   PRO; PR:Q61878; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q61878; protein.
DR   Bgee; ENSMUSG00000027073; Expressed in femorotibial joint and 67 other tissues.
DR   ExpressionAtlas; Q61878; baseline and differential.
DR   Genevisible; Q61878; MM.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0030246; F:carbohydrate 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; IMP:MGI.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:MGI.
DR   GO; GO:0010936; P:negative regulation of macrophage cytokine production; IMP:MGI.
DR   GO; GO:0032753; P:positive regulation of interleukin-4 production; IMP:MGI.
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; 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; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Immunity; Lectin; Nitration; Reference proteome; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..223
FT                   /note="Bone marrow proteoglycan"
FT                   /id="PRO_0000259924"
FT   PROPEP          17..106
FT                   /note="Acidic"
FT                   /id="PRO_0000017387"
FT   CHAIN           107..223
FT                   /note="Eosinophil granule major basic protein"
FT                   /id="PRO_0000017388"
FT   DOMAIN          124..223
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   REGION          20..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        126..221
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        198..213
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   223 AA;  24255 MW;  7D66D946DCEADA00 CRC64;
     MKFPLLLALL VGGASALHLS SETSDSKSPL MDENLPRDAE ISGPEGEECP PGEELMPLEG
     EKEEGSGSEG VPGDEGAVSG QDVTDVDLQC PKEEDTTSLM GDSGCKTCRY LLVRRAECFD
     KAQSVCRRCY RGTLASIHSF SVNFGIQSAV RGINQGQVWI GGRIKGWGRC KRFRWVDGSS
     WNFAYWAAGQ PCPGGGRCVT LCTQGGHWRL SHCVKRRPFI CSY
 
 
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