PRG3_HUMAN
ID PRG3_HUMAN Reviewed; 225 AA.
AC Q9Y2Y8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Proteoglycan 3;
DE AltName: Full=Eosinophil major basic protein homolog;
DE AltName: Full=Prepro-major basic protein homolog;
DE Short=Prepro-MBPH;
DE Flags: Precursor;
GN Name=PRG3 {ECO:0000312|HGNC:HGNC:9363};
GN Synonyms=MBPH {ECO:0000303|PubMed:10318872, ECO:0000303|PubMed:11170744};
GN ORFNames=UNQ486/PRO1002;
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] {ECO:0000305, ECO:0000312|EMBL:AAD24471.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND VARIANTS ARG-3 AND
RP THR-109.
RX PubMed=10318872; DOI=10.1074/jbc.274.20.14464;
RA Plager D.A., Loegering D.A., Weiler D.A., Checkel J.L., Wagner J.M.,
RA Clarke N.J., Naylor S., Page S.M., Thomas L.L., Akerblom I., Cocks B.,
RA Stuart S., Gleich G.J.;
RT "A novel and highly divergent homolog of human eosinophil granule major
RT basic protein.";
RL J. Biol. Chem. 274:14464-14473(1999).
RN [2] {ECO:0000312|EMBL:AAG41952.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-3 AND THR-109.
RX PubMed=11170744; DOI=10.1006/geno.2000.6391;
RA Plager D.A., Weiler D.A., Loegering D.A., Johnson W.B., Haley L.,
RA Eddy R.L., Shows T.B., Gleich G.J.;
RT "Comparative structure, proximal promoter elements, and chromosome location
RT of the human eosinophil major basic protein genes.";
RL Genomics 71:271-281(2001).
RN [3] {ECO:0000312|EMBL:AAQ89289.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-3 AND THR-109.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
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 [5] {ECO:0000312|EMBL:AAH69126.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-3 AND THR-109.
RC TISSUE=Liver {ECO:0000312|EMBL:AAI01614.1};
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).
CC -!- FUNCTION: Possesses similar cytotoxic and cytostimulatory activities to
CC PRG2/MBP. In vitro, stimulates neutrophil superoxide production and IL8
CC release, and histamine and leukotriene C4 release from basophils.
CC {ECO:0000269|PubMed:10318872}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC {ECO:0000269|PubMed:10318872}. Note=Localized to the eosinophil
CC secondary granule.
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow. Not detected in placenta.
CC {ECO:0000269|PubMed:10318872}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Eosinophil major basic protein homolog;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_208";
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DR EMBL; AF132209; AAD24471.1; -; mRNA.
DR EMBL; AF304354; AAG41952.1; -; Genomic_DNA.
DR EMBL; AY358930; AAQ89289.1; -; mRNA.
DR EMBL; AP000781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069126; AAH69126.1; -; mRNA.
DR EMBL; BC101613; AAI01614.1; -; mRNA.
DR EMBL; BC113411; AAI13412.1; -; mRNA.
DR CCDS; CCDS7954.1; -.
DR RefSeq; NP_006084.2; NM_006093.3.
DR AlphaFoldDB; Q9Y2Y8; -.
DR SMR; Q9Y2Y8; -.
DR BioGRID; 115666; 56.
DR IntAct; Q9Y2Y8; 31.
DR STRING; 9606.ENSP00000287143; -.
DR MEROPS; I63.001; -.
DR iPTMnet; Q9Y2Y8; -.
DR PhosphoSitePlus; Q9Y2Y8; -.
DR BioMuta; PRG3; -.
DR DMDM; 296452870; -.
DR jPOST; Q9Y2Y8; -.
DR MassIVE; Q9Y2Y8; -.
DR PaxDb; Q9Y2Y8; -.
DR PeptideAtlas; Q9Y2Y8; -.
DR PRIDE; Q9Y2Y8; -.
DR ProteomicsDB; 85938; -.
DR Antibodypedia; 27347; 26 antibodies from 12 providers.
DR DNASU; 10394; -.
DR Ensembl; ENST00000287143.2; ENSP00000287143.2; ENSG00000156575.2.
DR GeneID; 10394; -.
DR KEGG; hsa:10394; -.
DR MANE-Select; ENST00000287143.2; ENSP00000287143.2; NM_006093.4; NP_006084.2.
DR UCSC; uc001njv.2; human.
DR CTD; 10394; -.
DR DisGeNET; 10394; -.
DR GeneCards; PRG3; -.
DR HGNC; HGNC:9363; PRG3.
DR HPA; ENSG00000156575; Tissue enriched (bone).
DR MIM; 606814; gene.
DR neXtProt; NX_Q9Y2Y8; -.
DR OpenTargets; ENSG00000156575; -.
DR PharmGKB; PA33735; -.
DR VEuPathDB; HostDB:ENSG00000156575; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00440000039859; -.
DR HOGENOM; CLU_107200_1_0_1; -.
DR InParanoid; Q9Y2Y8; -.
DR OMA; FCWTDGS; -.
DR OrthoDB; 1328472at2759; -.
DR PhylomeDB; Q9Y2Y8; -.
DR TreeFam; TF336281; -.
DR PathwayCommons; Q9Y2Y8; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9Y2Y8; -.
DR BioGRID-ORCS; 10394; 10 hits in 1064 CRISPR screens.
DR ChiTaRS; PRG3; human.
DR GenomeRNAi; 10394; -.
DR Pharos; Q9Y2Y8; Tbio.
DR PRO; PR:Q9Y2Y8; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y2Y8; protein.
DR Bgee; ENSG00000156575; Expressed in trabecular bone tissue and 40 other tissues.
DR Genevisible; Q9Y2Y8; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; HDA:BHF-UCL.
DR GO; GO:0045575; P:basophil activation; IDA:UniProtKB.
DR GO; GO:0001694; P:histamine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0019370; P:leukotriene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR GO; GO:0042119; P:neutrophil activation; IDA:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:UniProtKB.
DR GO; GO:0042554; P:superoxide anion generation; IDA:UniProtKB.
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 Disulfide bond; Lectin; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..225
FT /note="Proteoglycan 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000250421"
FT DOMAIN 107..224
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 128..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 200..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VARIANT 3
FT /note="C -> R (in dbSNP:rs669661)"
FT /evidence="ECO:0000269|PubMed:10318872,
FT ECO:0000269|PubMed:11170744, ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_050117"
FT VARIANT 109
FT /note="I -> T (in dbSNP:rs540687)"
FT /evidence="ECO:0000269|PubMed:10318872,
FT ECO:0000269|PubMed:11170744, ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_050118"
SQ SEQUENCE 225 AA; 25406 MW; AA073254496F9624 CRC64;
MQCLLLLPFL LLGTVSALHL ENDAPHLESL ETQADLGQDL DSSKEQERDL ALTEEVIQAE
GEEVKASACQ DNFEDEEAME SDPAALDKDF QCPREEDIVE VQGSPRCKIC RYLLVRTPKT
FAEAQNVCSR CYGGNLVSIH DFNFNYRIQC CTSTVNQAQV WIGGNLRGWF LWKRFCWTDG
SHWNFAYWSP GQPGNGQGSC VALCTKGGYW RRAQCDKQLP FVCSF
