Full text data of PRG3
PRG3
(MBPH)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Proteoglycan 3 (Eosinophil major basic protein homolog; Prepro-major basic protein homolog; Prepro-MBPH; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteoglycan 3 (Eosinophil major basic protein homolog; Prepro-major basic protein homolog; Prepro-MBPH; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y2Y8
ID PRG3_HUMAN Reviewed; 225 AA.
AC Q9Y2Y8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 2.
DT 22-JAN-2014, entry version 105.
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; Synonyms=MBPH; ORFNames=UNQ486/PRO1002;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND VARIANTS ARG-3
RP AND 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
RT major basic protein.";
RL J. Biol. Chem. 274:14464-14473(1999).
RN [2]
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
RT location of the human eosinophil major basic protein genes.";
RL Genomics 71:271-281(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-3 AND
RP 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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics 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.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-3 AND
RP THR-109.
RC TISSUE=Liver;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Possesses similar cytotoxic and cytostimulatory
CC activities to PRG2/MBP. In vitro, stimulates neutrophil superoxide
CC production and IL8 release, and histamine and leukotriene C4
CC release from basophils.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Localized to the
CC eosinophil secondary granule.
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow. Not detected in
CC placenta.
CC -!- SIMILARITY: Contains 1 C-type lectin domain.
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";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_006084.2; NM_006093.3.
DR UniGene; Hs.251386; -.
DR ProteinModelPortal; Q9Y2Y8; -.
DR SMR; Q9Y2Y8; 110-225.
DR MEROPS; I63.001; -.
DR PhosphoSite; Q9Y2Y8; -.
DR DMDM; 296452870; -.
DR PaxDb; Q9Y2Y8; -.
DR PRIDE; Q9Y2Y8; -.
DR DNASU; 10394; -.
DR Ensembl; ENST00000287143; ENSP00000287143; ENSG00000156575.
DR GeneID; 10394; -.
DR KEGG; hsa:10394; -.
DR UCSC; uc001njv.2; human.
DR CTD; 10394; -.
DR GeneCards; GC11M057144; -.
DR H-InvDB; HIX0035870; -.
DR HGNC; HGNC:9363; PRG3.
DR MIM; 606814; gene.
DR neXtProt; NX_Q9Y2Y8; -.
DR PharmGKB; PA33735; -.
DR eggNOG; NOG278428; -.
DR HOGENOM; HOG000261603; -.
DR HOVERGEN; HBG005583; -.
DR InParanoid; Q9Y2Y8; -.
DR OMA; LPFVCSF; -.
DR OrthoDB; EOG779P0F; -.
DR PhylomeDB; Q9Y2Y8; -.
DR GenomeRNAi; 10394; -.
DR NextBio; 39378; -.
DR PRO; PR:Q9Y2Y8; -.
DR Bgee; Q9Y2Y8; -.
DR CleanEx; HS_PRG3; -.
DR Genevestigator; Q9Y2Y8; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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:0045416; P:positive regulation of interleukin-8 biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042554; P:superoxide anion generation; IDA:UniProtKB.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin.
DR InterPro; IPR016186; C-type_lectin-like.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; C-type_lectin_fold.
DR InterPro; IPR002352; Eosinophil_major_basic.
DR PANTHER; PTHR10068; PTHR10068; 1.
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 Complete proteome; Disulfide bond; Lectin; Polymorphism;
KW Reference proteome; Signal.
FT SIGNAL 1 17 Potential.
FT CHAIN 18 225 Proteoglycan 3.
FT /FTId=PRO_0000250421.
FT DOMAIN 107 224 C-type lectin.
FT DISULFID 128 223 By similarity.
FT DISULFID 200 215 By similarity.
FT VARIANT 3 3 C -> R (in dbSNP:rs669661).
FT /FTId=VAR_050117.
FT VARIANT 109 109 I -> T (in dbSNP:rs540687).
FT /FTId=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
//
ID PRG3_HUMAN Reviewed; 225 AA.
AC Q9Y2Y8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 2.
DT 22-JAN-2014, entry version 105.
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; Synonyms=MBPH; ORFNames=UNQ486/PRO1002;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND VARIANTS ARG-3
RP AND 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
RT major basic protein.";
RL J. Biol. Chem. 274:14464-14473(1999).
RN [2]
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
RT location of the human eosinophil major basic protein genes.";
RL Genomics 71:271-281(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-3 AND
RP 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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics 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.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-3 AND
RP THR-109.
RC TISSUE=Liver;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Possesses similar cytotoxic and cytostimulatory
CC activities to PRG2/MBP. In vitro, stimulates neutrophil superoxide
CC production and IL8 release, and histamine and leukotriene C4
CC release from basophils.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Localized to the
CC eosinophil secondary granule.
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow. Not detected in
CC placenta.
CC -!- SIMILARITY: Contains 1 C-type lectin domain.
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";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_006084.2; NM_006093.3.
DR UniGene; Hs.251386; -.
DR ProteinModelPortal; Q9Y2Y8; -.
DR SMR; Q9Y2Y8; 110-225.
DR MEROPS; I63.001; -.
DR PhosphoSite; Q9Y2Y8; -.
DR DMDM; 296452870; -.
DR PaxDb; Q9Y2Y8; -.
DR PRIDE; Q9Y2Y8; -.
DR DNASU; 10394; -.
DR Ensembl; ENST00000287143; ENSP00000287143; ENSG00000156575.
DR GeneID; 10394; -.
DR KEGG; hsa:10394; -.
DR UCSC; uc001njv.2; human.
DR CTD; 10394; -.
DR GeneCards; GC11M057144; -.
DR H-InvDB; HIX0035870; -.
DR HGNC; HGNC:9363; PRG3.
DR MIM; 606814; gene.
DR neXtProt; NX_Q9Y2Y8; -.
DR PharmGKB; PA33735; -.
DR eggNOG; NOG278428; -.
DR HOGENOM; HOG000261603; -.
DR HOVERGEN; HBG005583; -.
DR InParanoid; Q9Y2Y8; -.
DR OMA; LPFVCSF; -.
DR OrthoDB; EOG779P0F; -.
DR PhylomeDB; Q9Y2Y8; -.
DR GenomeRNAi; 10394; -.
DR NextBio; 39378; -.
DR PRO; PR:Q9Y2Y8; -.
DR Bgee; Q9Y2Y8; -.
DR CleanEx; HS_PRG3; -.
DR Genevestigator; Q9Y2Y8; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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:0045416; P:positive regulation of interleukin-8 biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042554; P:superoxide anion generation; IDA:UniProtKB.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin.
DR InterPro; IPR016186; C-type_lectin-like.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; C-type_lectin_fold.
DR InterPro; IPR002352; Eosinophil_major_basic.
DR PANTHER; PTHR10068; PTHR10068; 1.
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 Complete proteome; Disulfide bond; Lectin; Polymorphism;
KW Reference proteome; Signal.
FT SIGNAL 1 17 Potential.
FT CHAIN 18 225 Proteoglycan 3.
FT /FTId=PRO_0000250421.
FT DOMAIN 107 224 C-type lectin.
FT DISULFID 128 223 By similarity.
FT DISULFID 200 215 By similarity.
FT VARIANT 3 3 C -> R (in dbSNP:rs669661).
FT /FTId=VAR_050117.
FT VARIANT 109 109 I -> T (in dbSNP:rs540687).
FT /FTId=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
//
MIM
606814
*RECORD*
*FIELD* NO
606814
*FIELD* TI
*606814 PROTEOGLYCAN 3; PRG3
;;PREPRO-MAJOR BASIC PROTEIN HOMOLOG; MBPH
*FIELD* TX
read more
CLONING
Through large-scale sequencing, Plager et al. (1999) identified PRG3 as
one of several transcripts upregulated in umbilical cord precursor cells
following stimulation with interleukin-5 (147850). Using this sequence
as probe, Plager et al. (2001) cloned PRG3 from a phage genomic library
of placental tissues. Plager et al. (1999) found that the cDNA sequence
predicts a mature 117-amino acid protein with a prepro- region of 108
amino acids. PRG3 shares 49% amino acid sequence identity with PRG2
(605601). RT-PCR demonstrated that PRG3 is expressed exclusively in bone
marrow. Protein purified from eosinophil granules showed a molecular
mass of 13.4 kD.
GENE FUNCTION
Plager et al. (1999) found that the biologic activity of PRG3 is similar
to that of PRG2 in cell killing and in neutrophil and basophil
stimulation assays, but usually with reduced potency.
GENE STRUCTURE
Plager et al. (2001) determined that PRG3 contains 6 exons and spans 6.9
kb of genomic DNA. It has potential transcription factor binding sites
for IK2 (603023), STAT (see 600555), and GATA (see 600576).
MAPPING
By FISH, Plager et al. (2001) mapped the PRG2 and PRG3 genes to
chromosome 11cen-q12.
*FIELD* RF
1. Plager, D. A.; Loegering, D. A.; Weiler, D. A.; Checkel, J. L.;
Wagner, J. M.; Clarke, N. J.; Naylor, S.; Page, S. M.; Thomas, L.
L.; Akerblom, I.; Cocks, B.; Stuart, S.; Gleich, G. J.: A novel and
highly divergent homolog of human eosinophil granule major basic protein. J.
Biol. Chem. 274: 14464-14473, 1999.
2. Plager, D. A.; Weiler, D. A.; Loegering, D. A.; Johnson, W. B.;
Haley, L.; Eddy, R. L.; Shows, T. B.; Gleich, G. J.: Comparative
structure, proximal promoter elements, and chromosome location of
the human eosinophil major basic protein genes. Genomics 71: 271-281,
2001.
*FIELD* CD
Patricia A. Hartz: 4/2/2002
*FIELD* ED
carol: 04/02/2002
*RECORD*
*FIELD* NO
606814
*FIELD* TI
*606814 PROTEOGLYCAN 3; PRG3
;;PREPRO-MAJOR BASIC PROTEIN HOMOLOG; MBPH
*FIELD* TX
read more
CLONING
Through large-scale sequencing, Plager et al. (1999) identified PRG3 as
one of several transcripts upregulated in umbilical cord precursor cells
following stimulation with interleukin-5 (147850). Using this sequence
as probe, Plager et al. (2001) cloned PRG3 from a phage genomic library
of placental tissues. Plager et al. (1999) found that the cDNA sequence
predicts a mature 117-amino acid protein with a prepro- region of 108
amino acids. PRG3 shares 49% amino acid sequence identity with PRG2
(605601). RT-PCR demonstrated that PRG3 is expressed exclusively in bone
marrow. Protein purified from eosinophil granules showed a molecular
mass of 13.4 kD.
GENE FUNCTION
Plager et al. (1999) found that the biologic activity of PRG3 is similar
to that of PRG2 in cell killing and in neutrophil and basophil
stimulation assays, but usually with reduced potency.
GENE STRUCTURE
Plager et al. (2001) determined that PRG3 contains 6 exons and spans 6.9
kb of genomic DNA. It has potential transcription factor binding sites
for IK2 (603023), STAT (see 600555), and GATA (see 600576).
MAPPING
By FISH, Plager et al. (2001) mapped the PRG2 and PRG3 genes to
chromosome 11cen-q12.
*FIELD* RF
1. Plager, D. A.; Loegering, D. A.; Weiler, D. A.; Checkel, J. L.;
Wagner, J. M.; Clarke, N. J.; Naylor, S.; Page, S. M.; Thomas, L.
L.; Akerblom, I.; Cocks, B.; Stuart, S.; Gleich, G. J.: A novel and
highly divergent homolog of human eosinophil granule major basic protein. J.
Biol. Chem. 274: 14464-14473, 1999.
2. Plager, D. A.; Weiler, D. A.; Loegering, D. A.; Johnson, W. B.;
Haley, L.; Eddy, R. L.; Shows, T. B.; Gleich, G. J.: Comparative
structure, proximal promoter elements, and chromosome location of
the human eosinophil major basic protein genes. Genomics 71: 271-281,
2001.
*FIELD* CD
Patricia A. Hartz: 4/2/2002
*FIELD* ED
carol: 04/02/2002