A2GL_HUMAN
ID A2GL_HUMAN Reviewed; 347 AA.
AC P02750; Q8N4F5; Q96QZ4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Leucine-rich alpha-2-glycoprotein;
DE Short=LRG;
DE Flags: Precursor;
GN Name=LRG1; Synonyms=LRG;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12223515;
RA O'Donnell L.C., Druhan L.J., Avalos B.R.;
RT "Molecular characterization and expression analysis of leucine-rich alpha2-
RT glycoprotein, a novel marker of granulocytic differentiation.";
RL J. Leukoc. Biol. 72:478-485(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-133.
RC TISSUE=Colon, Kidney, and Lung;
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).
RN [3]
RP PROTEIN SEQUENCE OF 36-347.
RX PubMed=3856868; DOI=10.1073/pnas.82.7.1906;
RA Takahashi N., Takahashi Y., Putnam F.W.;
RT "Periodicity of leucine and tandem repetition of a 24-amino acid segment in
RT the primary structure of leucine-rich alpha 2-glycoprotein of human
RT serum.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1906-1910(1985).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-186.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-186; ASN-269 AND ASN-325.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-186.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-186.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [8]
RP GLYCOSYLATION AT ASN-186 AND ASN-325.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79 AND ASN-186, AND STRUCTURE
RP OF CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- INTERACTION:
CC P02750; P37023: ACVRL1; NbExp=3; IntAct=EBI-9083443, EBI-8043559;
CC P02750; P17813-1: ENG; NbExp=4; IntAct=EBI-9083443, EBI-16065304;
CC P02750; P36897-1: TGFBR1; NbExp=6; IntAct=EBI-9083443, EBI-16065417;
CC P02750; P37173-2: TGFBR2; NbExp=3; IntAct=EBI-9083443, EBI-16065370;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF403428; AAK95527.1; -; mRNA.
DR EMBL; BC034389; AAH34389.1; -; mRNA.
DR EMBL; BC070198; AAH70198.1; -; mRNA.
DR CCDS; CCDS12130.1; -.
DR PIR; A03211; NBHUA2.
DR RefSeq; NP_443204.1; NM_052972.2.
DR AlphaFoldDB; P02750; -.
DR SMR; P02750; -.
DR BioGRID; 125537; 10.
DR DIP; DIP-60317N; -.
DR IntAct; P02750; 7.
DR STRING; 9606.ENSP00000302621; -.
DR DrugBank; DB09130; Copper.
DR GlyConnect; 676; 45 N-Linked glycans (5 sites).
DR GlyGen; P02750; 6 sites, 57 N-linked glycans (5 sites).
DR iPTMnet; P02750; -.
DR PhosphoSitePlus; P02750; -.
DR BioMuta; LRG1; -.
DR DMDM; 23503037; -.
DR DOSAC-COBS-2DPAGE; P02750; -.
DR SWISS-2DPAGE; P02750; -.
DR CPTAC; CPTAC-678; -.
DR CPTAC; non-CPTAC-1139; -.
DR EPD; P02750; -.
DR jPOST; P02750; -.
DR MassIVE; P02750; -.
DR PaxDb; P02750; -.
DR PeptideAtlas; P02750; -.
DR PRIDE; P02750; -.
DR ProteomicsDB; 51566; -.
DR Antibodypedia; 854; 459 antibodies from 34 providers.
DR DNASU; 116844; -.
DR Ensembl; ENST00000306390.7; ENSP00000302621.4; ENSG00000171236.10.
DR GeneID; 116844; -.
DR KEGG; hsa:116844; -.
DR MANE-Select; ENST00000306390.7; ENSP00000302621.4; NM_052972.3; NP_443204.1.
DR UCSC; uc002mau.4; human.
DR CTD; 116844; -.
DR DisGeNET; 116844; -.
DR GeneCards; LRG1; -.
DR HGNC; HGNC:29480; LRG1.
DR HPA; ENSG00000171236; Tissue enriched (liver).
DR MIM; 611289; gene.
DR neXtProt; NX_P02750; -.
DR OpenTargets; ENSG00000171236; -.
DR PharmGKB; PA134919634; -.
DR VEuPathDB; HostDB:ENSG00000171236; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000162412; -.
DR HOGENOM; CLU_000288_18_6_1; -.
DR InParanoid; P02750; -.
DR OMA; PKDCQVF; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P02750; -.
DR TreeFam; TF351919; -.
DR PathwayCommons; P02750; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P02750; -.
DR BioGRID-ORCS; 116844; 13 hits in 1084 CRISPR screens.
DR ChiTaRS; LRG1; human.
DR GeneWiki; LRG1; -.
DR GenomeRNAi; 116844; -.
DR Pharos; P02750; Tbio.
DR PRO; PR:P02750; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P02750; protein.
DR Bgee; ENSG00000171236; Expressed in right lobe of liver and 134 other tissues.
DR Genevisible; P02750; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IPI:BHF-UCL.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IPI:BHF-UCL.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0051546; P:keratinocyte migration; IMP:BHF-UCL.
DR GO; GO:0061756; P:leukocyte adhesion to vascular endothelial cell; IMP:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IMP:BHF-UCL.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:BHF-UCL.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IMP:BHF-UCL.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IMP:BHF-UCL.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00082; LRRCT; 1.
DR PROSITE; PS51450; LRR; 8.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Leucine-rich repeat; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000269|PubMed:3856868"
FT CHAIN 36..347
FT /note="Leucine-rich alpha-2-glycoprotein"
FT /id="PRO_0000020579"
FT REPEAT 93..114
FT /note="LRR 1"
FT REPEAT 117..138
FT /note="LRR 2"
FT REPEAT 141..162
FT /note="LRR 3"
FT REPEAT 165..186
FT /note="LRR 4"
FT REPEAT 189..210
FT /note="LRR 5"
FT REPEAT 213..234
FT /note="LRR 6"
FT REPEAT 237..258
FT /note="LRR 7"
FT REPEAT 261..282
FT /note="LRR 8"
FT DOMAIN 299..347
FT /note="LRRCT"
FT SITE 306
FT /note="Not glycosylated"
FT CARBOHYD 37
FT /note="O-linked (GalNAc...) threonine"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19838169"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19838169"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490"
FT DISULFID 43..56
FT DISULFID 303..329
FT VARIANT 64
FT /note="G -> S (in dbSNP:rs7251081)"
FT /id="VAR_050629"
FT VARIANT 133
FT /note="P -> S (in dbSNP:rs966384)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024245"
SQ SEQUENCE 347 AA; 38178 MW; 20C99ED50152FA9C CRC64;
MSSWSRQRPK SPGGIQPHVS RTLFLLLLLA ASAWGVTLSP KDCQVFRSDH GSSISCQPPA
EIPGYLPADT VHLAVEFFNL THLPANLLQG ASKLQELHLS SNGLESLSPE FLRPVPQLRV
LDLTRNALTG LPPGLFQASA TLDTLVLKEN QLEVLEVSWL HGLKALGHLD LSGNRLRKLP
PGLLANFTLL RTLDLGENQL ETLPPDLLRG PLQLERLHLE GNKLQVLGKD LLLPQPDLRY
LFLNGNKLAR VAAGAFQGLR QLDMLDLSNN SLASVPEGLW ASLGQPNWDM RDGFDISGNP
WICDQNLSDL YRWLQAQKDK MFSQNDTRCA GPEAVKGQTL LAVAKSQ
