PRG3_MOUSE
ID PRG3_MOUSE Reviewed; 222 AA.
AC Q9JL95; A2AW01; Q3SXA9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Proteoglycan 3;
DE AltName: Full=Eosinophil major basic protein 2;
DE Flags: Precursor;
GN Name=Prg3 {ECO:0000312|MGI:MGI:1858200};
GN Synonyms=Mbp2 {ECO:0000312|EMBL:AAF26366.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAF26366.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAF26366.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:AAF26366.1};
RX PubMed=10770291; DOI=10.1002/jlb.67.4.567;
RA Macias M.P., Welch K.C., Denzler K.L., Larson K.A., Lee N.A., Lee J.J.;
RT "Identification of a new murine eosinophil major basic protein (mMBP) gene:
RT cloning and characterization of mMBP-2.";
RL J. Leukoc. Biol. 67:567-576(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAE34360.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE34360.1};
RC TISSUE=Inner ear {ECO:0000312|EMBL:BAE34360.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAI04389.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Note=Localized to the eosinophil secondary
CC granule. {ECO:0000269|PubMed:10770291}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:10770291};
CC IsoId=Q9JL95-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JL95-3; Sequence=VSP_034564;
CC -!- TISSUE SPECIFICITY: Expressed in bone marrow, spleen, and thymus. Not
CC detected in heart, liver or lung. {ECO:0000269|PubMed:10770291}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI04390.2; Type=Frameshift; Evidence={ECO:0000305};
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_mou_Ctlect_152";
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DR EMBL; AF202533; AAF26366.1; -; mRNA.
DR EMBL; AK158110; BAE34360.1; -; mRNA.
DR EMBL; AL935159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104388; AAI04389.1; -; mRNA.
DR EMBL; BC104389; AAI04390.2; ALT_FRAME; mRNA.
DR CCDS; CCDS16199.1; -. [Q9JL95-1]
DR RefSeq; NP_058610.1; NM_016914.2. [Q9JL95-1]
DR RefSeq; XP_006499964.1; XM_006499901.1. [Q9JL95-1]
DR AlphaFoldDB; Q9JL95; -.
DR SMR; Q9JL95; -.
DR STRING; 10090.ENSMUSP00000028466; -.
DR MEROPS; I63.001; -.
DR PhosphoSitePlus; Q9JL95; -.
DR MaxQB; Q9JL95; -.
DR PaxDb; Q9JL95; -.
DR PRIDE; Q9JL95; -.
DR ProteomicsDB; 289407; -. [Q9JL95-1]
DR ProteomicsDB; 289408; -. [Q9JL95-3]
DR Antibodypedia; 27347; 26 antibodies from 12 providers.
DR DNASU; 53856; -.
DR Ensembl; ENSMUST00000028466; ENSMUSP00000028466; ENSMUSG00000027072. [Q9JL95-1]
DR GeneID; 53856; -.
DR KEGG; mmu:53856; -.
DR UCSC; uc008kjq.1; mouse. [Q9JL95-1]
DR CTD; 10394; -.
DR MGI; MGI:1858200; Prg3.
DR VEuPathDB; HostDB:ENSMUSG00000027072; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00440000039859; -.
DR HOGENOM; CLU_107200_1_0_1; -.
DR InParanoid; Q9JL95; -.
DR OMA; FCWTDGS; -.
DR OrthoDB; 1328472at2759; -.
DR PhylomeDB; Q9JL95; -.
DR TreeFam; TF336281; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 53856; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q9JL95; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9JL95; protein.
DR Bgee; ENSMUSG00000027072; Expressed in peripheral lymph node and 18 other tissues.
DR Genevisible; Q9JL95; MM.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0045575; P:basophil activation; ISO:MGI.
DR GO; GO:0001694; P:histamine biosynthetic process; ISO:MGI.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0019370; P:leukotriene biosynthetic process; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0042119; P:neutrophil activation; ISO:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0042554; P:superoxide anion generation; ISO: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; 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 Alternative splicing; Disulfide bond; Lectin; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..222
FT /note="Proteoglycan 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000248860"
FT DOMAIN 105..221
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 27..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 126..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 197..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 22..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034564"
SQ SEQUENCE 222 AA; 25204 MW; 1A28C69888FC52FF CRC64;
MKQPLILSFL LLGMVSAFHL ETAHLENPKR EESLKQEADG SREQGRELAL TQETKQTEGE
EVEGSQHQDI FEDEEAMESD PDALNKDSAC PKEEDTTHFQ GTPGCKSCNY VLVRTPETFD
KAQRVCRRCY RGNLASVHSY SFNYQIQNLA RKINQSIVWI GGILRGWFWK KFCWMDGSCW
DFGYWAPGQP GSGGGHCVTL CTKGGHWRRA SCKSHLPFIC SF
