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Bone morphogenetic protein 2 (BMP-2) (Bone morphogenetic protein 2A) (BMP-2A)

 BMP2_HUMAN              Reviewed;         396 AA.
P12643;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
25-OCT-2017, entry version 203.
RecName: Full=Bone morphogenetic protein 2;
Short=BMP-2;
AltName: Full=Bone morphogenetic protein 2A;
Short=BMP-2A;
Flags: Precursor;
Name=BMP2; Synonyms=BMP2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=3201241; DOI=10.1126/science.3201241;
Wozney J.M., Rosen V., Celeste A.J., Mitsock L.M., Whitters M.J.,
Kriz R.W., Hewick R.M., Wang E.A.;
"Novel regulators of bone formation: molecular clones and
activities.";
Science 242:1528-1534(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Shore E.M., Xu M.-Q., Calvert G., Moriatis J., Kaplan F.S.;
"Human bone morphogenetic protein 2 (BMP-2) genomic DNA sequence.";
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
GLYCOSYLATION AT ASN-338.
PubMed=9265423; DOI=10.1021/ac9611172;
Yeung B., Porter T.J., Vath J.E.;
"Direct isoform analysis of high-mannose-containing glycoproteins by
on-line capillary electrophoresis electrospray mass spectrometry.";
Anal. Chem. 69:2510-2516(1997).
[5]
INTERACTION WITH SOSTDC1.
PubMed=15020244; DOI=10.1016/j.bbrc.2004.02.075;
Yanagita M., Oka M., Watabe T., Iguchi H., Niida A., Takahashi S.,
Akiyama T., Miyazono K., Yanagisawa M., Sakurai T.;
"USAG-1: a bone morphogenetic protein antagonist abundantly expressed
in the kidney.";
Biochem. Biophys. Res. Commun. 316:490-500(2004).
[6]
INTERACTION WITH FBN1 AND FBN2.
PubMed=18339631; DOI=10.1074/jbc.M707820200;
Sengle G., Charbonneau N.L., Ono R.N., Sasaki T., Alvarez J.,
Keene D.R., Baechinger H.P., Sakai L.Y.;
"Targeting of bone morphogenetic protein growth factor complexes to
fibrillin.";
J. Biol. Chem. 283:13874-13888(2008).
[7]
PROTEOLYTIC PROCESSING, AND PROPEPTIDE.
PubMed=20555025; DOI=10.1210/en.2010-0326;
Heng S., Paule S., Hardman B., Li Y., Singh H., Rainczuk A.,
Stephens A.N., Nie G.;
"Posttranslational activation of bone morphogenetic protein 2 is
mediated by proprotein convertase 6 during decidualization for
pregnancy establishment.";
Endocrinology 151:3909-3917(2010).
[8]
FUNCTION.
PubMed=24362451; DOI=10.1007/s00223-013-9828-1;
Tanaka K., Kaji H., Yamaguchi T., Kanazawa I., Canaff L., Hendy G.N.,
Sugimoto T.;
"Involvement of the osteoinductive factors, Tmem119 and BMP-2, and the
ER stress response PERK-eIF2alpha-ATF4 pathway in the commitment of
myoblastic into osteoblastic cells.";
Calcif. Tissue Int. 94:454-464(2014).
[9]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 292-396, AND SUBUNIT.
PubMed=10074410; DOI=10.1006/jmbi.1999.2590;
Scheufler C., Sebald W., Huelsmeyer M.;
"Crystal structure of human bone morphogenetic protein-2 at 2.7 A
resolution.";
J. Mol. Biol. 287:103-115(1999).
-!- FUNCTION: Induces cartilage and bone formation (PubMed:3201241).
Stimulates the differentiation of myoblasts into osteoblasts via
the EIF2AK3-EIF2A- ATF4 pathway. BMP2 activation of EIF2AK3
stimulates phosphorylation of EIF2A which leads to increased
expression of ATF4 which plays a central role in osteoblast
differentiation. In addition stimulates TMEM119, which upregulates
the expression of ATF4 (PubMed:24362451).
{ECO:0000269|PubMed:24362451, ECO:0000269|PubMed:3201241}.
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:10074410). Interacts
with SOSTDC1 (PubMed:15020244). Interacts with GREM2, RGMA, RGMB
and RGMC. Interacts with ASPN (By similarity). Interacts with
MAFP5 (By similarity). Interacts with FBN1 (via N-terminal domain)
and FBN2 (PubMed:18339631). {ECO:0000250|UniProtKB:P21274,
ECO:0000269|PubMed:10074410, ECO:0000269|PubMed:15020244,
ECO:0000269|PubMed:18339631}.
-!- INTERACTION:
P27038:Acvr2a (xeno); NbExp=2; IntAct=EBI-1029262, EBI-1036102;
P36894:BMPR1A; NbExp=17; IntAct=EBI-1029262, EBI-1029237;
O00238:BMPR1B; NbExp=3; IntAct=EBI-1029262, EBI-7527193;
Q12841:FSTL1; NbExp=2; IntAct=EBI-1029262, EBI-2349801;
Q6ZVN8:HFE2; NbExp=2; IntAct=EBI-1029262, EBI-10900704;
Q6ZVN8-1:HFE2; NbExp=2; IntAct=EBI-1029262, EBI-16155543;
Q13253:NOG; NbExp=2; IntAct=EBI-1029262, EBI-1035205;
Q96B86-1:RGMA; NbExp=2; IntAct=EBI-1029262, EBI-16155394;
Q6NW40:RGMB; NbExp=7; IntAct=EBI-1029262, EBI-16155464;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Particularly abundant in lung, spleen and
colon and in low but significant levels in heart, brain, placenta,
liver, skeletal muscle, kidney, pancreas, prostate, ovary and
small intestine.
-!- PHARMACEUTICAL: Available under the name Infuse (Medtronic Sofamor
Danek). Used for treating open tibial shaft fractures.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Bone morphogenetic protein 2
entry;
URL="https://en.wikipedia.org/wiki/Bone_morphogenetic_protein_2";
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EMBL; M22489; AAA51834.1; -; mRNA.
EMBL; AF040249; AAF21646.1; -; Genomic_DNA.
EMBL; AL035668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS13099.1; -.
PIR; B37278; BMHU2.
RefSeq; NP_001191.1; NM_001200.3.
UniGene; Hs.73853; -.
PDB; 1ES7; X-ray; 2.90 A; A/C=283-396.
PDB; 1REU; X-ray; 2.65 A; A=294-396.
PDB; 1REW; X-ray; 1.86 A; A/B=283-396.
PDB; 2GOO; X-ray; 2.20 A; A/D=283-396.
PDB; 2H62; X-ray; 1.85 A; A/B=283-396.
PDB; 2H64; X-ray; 1.92 A; A=283-396.
PDB; 2QJ9; X-ray; 2.44 A; A/B=283-396.
PDB; 2QJA; X-ray; 2.60 A; A/B=283-396.
PDB; 2QJB; X-ray; 2.50 A; A/B=283-396.
PDB; 3BK3; X-ray; 2.70 A; A/B=283-396.
PDB; 3BMP; X-ray; 2.70 A; A=283-396.
PDB; 4MID; X-ray; 2.14 A; A=283-314.
PDB; 4N1D; X-ray; 1.91 A; A=283-305, A=362-396.
PDB; 4UHY; X-ray; 3.20 A; A/B=283-396.
PDB; 4UHZ; X-ray; 2.85 A; A=283-396.
PDB; 4UI0; X-ray; 2.80 A; A/B=283-396.
PDB; 4UI1; X-ray; 2.35 A; A/B=283-396.
PDB; 4UI2; X-ray; 3.15 A; B=283-396.
PDBsum; 1ES7; -.
PDBsum; 1REU; -.
PDBsum; 1REW; -.
PDBsum; 2GOO; -.
PDBsum; 2H62; -.
PDBsum; 2H64; -.
PDBsum; 2QJ9; -.
PDBsum; 2QJA; -.
PDBsum; 2QJB; -.
PDBsum; 3BK3; -.
PDBsum; 3BMP; -.
PDBsum; 4MID; -.
PDBsum; 4N1D; -.
PDBsum; 4UHY; -.
PDBsum; 4UHZ; -.
PDBsum; 4UI0; -.
PDBsum; 4UI1; -.
PDBsum; 4UI2; -.
ProteinModelPortal; P12643; -.
SMR; P12643; -.
BioGrid; 107118; 9.
CORUM; P12643; -.
DIP; DIP-5792N; -.
IntAct; P12643; 17.
MINT; MINT-6772716; -.
STRING; 9606.ENSP00000368104; -.
BindingDB; P12643; -.
ChEMBL; CHEMBL1926496; -.
iPTMnet; P12643; -.
PhosphoSitePlus; P12643; -.
BioMuta; BMP2; -.
DMDM; 115068; -.
EPD; P12643; -.
PaxDb; P12643; -.
PeptideAtlas; P12643; -.
PRIDE; P12643; -.
DNASU; 650; -.
Ensembl; ENST00000378827; ENSP00000368104; ENSG00000125845.
GeneID; 650; -.
KEGG; hsa:650; -.
UCSC; uc002wmu.2; human.
CTD; 650; -.
DisGeNET; 650; -.
EuPathDB; HostDB:ENSG00000125845.6; -.
GeneCards; BMP2; -.
HGNC; HGNC:1069; BMP2.
HPA; HPA058610; -.
MalaCards; BMP2; -.
MIM; 112261; gene.
neXtProt; NX_P12643; -.
OpenTargets; ENSG00000125845; -.
Orphanet; 261295; 20p12.3 microdeletion syndrome.
Orphanet; 93396; Brachydactyly type A2.
PharmGKB; PA25379; -.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
GeneTree; ENSGT00760000118883; -.
HOGENOM; HOG000249478; -.
HOVERGEN; HBG004860; -.
InParanoid; P12643; -.
KO; K21283; -.
OMA; QGVSKRH; -.
OrthoDB; EOG091G0K7Z; -.
PhylomeDB; P12643; -.
TreeFam; TF351789; -.
Reactome; R-HSA-201451; Signaling by BMP.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
SignaLink; P12643; -.
SIGNOR; P12643; -.
ChiTaRS; BMP2; human.
EvolutionaryTrace; P12643; -.
GeneWiki; Bone_morphogenetic_protein_2; -.
GenomeRNAi; 650; -.
PRO; PR:P12643; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000125845; -.
CleanEx; HS_BMP2; -.
ExpressionAtlas; P12643; baseline and differential.
Genevisible; P12643; HS.
GO; GO:0070724; C:BMP receptor complex; IDA:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0070700; F:BMP receptor binding; IDA:MGI.
GO; GO:0039706; F:co-receptor binding; IPI:BHF-UCL.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0019211; F:phosphatase activator activity; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0005102; F:receptor binding; TAS:ProtInc.
GO; GO:0004745; F:retinol dehydrogenase activity; ISS:UniProtKB.
GO; GO:0046332; F:SMAD binding; IDA:BHF-UCL.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IBA:GO_Central.
GO; GO:0000187; P:activation of MAPK activity; IDA:AgBase.
GO; GO:0009887; P:animal organ morphogenesis; ISS:UniProtKB.
GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:UniProtKB.
GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0003130; P:BMP signaling pathway involved in heart induction; IDA:BHF-UCL.
GO; GO:0030282; P:bone mineralization; ISS:UniProtKB.
GO; GO:0035630; P:bone mineralization involved in bone maturation; IDA:BHF-UCL.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IDA:BHF-UCL.
GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:BHF-UCL.
GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISS:UniProtKB.
GO; GO:0035051; P:cardiocyte differentiation; IDA:MGI.
GO; GO:0048468; P:cell development; IBA:GO_Central.
GO; GO:0045165; P:cell fate commitment; ISS:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0071773; P:cellular response to BMP stimulus; IDA:BHF-UCL.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0002062; P:chondrocyte differentiation; IDA:AgBase.
GO; GO:0060128; P:corticotropin hormone secreting cell differentiation; ISS:UniProtKB.
GO; GO:0009790; P:embryo development; ISS:UniProtKB.
GO; GO:0035054; P:embryonic heart tube anterior/posterior pattern specification; ISS:UniProtKB.
GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:UniProtKB.
GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:BHF-UCL.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
GO; GO:0048762; P:mesenchymal cell differentiation; IDA:UniProtKB.
GO; GO:0072138; P:mesenchymal cell proliferation involved in ureteric bud development; ISS:UniProtKB.
GO; GO:0060485; P:mesenchyme development; IMP:BHF-UCL.
GO; GO:0032348; P:negative regulation of aldosterone biosynthetic process; IDA:BHF-UCL.
GO; GO:0051042; P:negative regulation of calcium-independent cell-cell adhesion; IDA:AgBase.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEP:AgBase.
GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; IDA:BHF-UCL.
GO; GO:0045786; P:negative regulation of cell cycle; IDA:HGNC.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:2000065; P:negative regulation of cortisol biosynthetic process; IDA:BHF-UCL.
GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0010894; P:negative regulation of steroid biosynthetic process; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0003308; P:negative regulation of Wnt signaling pathway involved in heart development; IDA:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; ISS:UniProtKB.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISS:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; IDA:MGI.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0060039; P:pericardium development; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISS:UniProtKB.
GO; GO:0030501; P:positive regulation of bone mineralization; IDA:BHF-UCL.
GO; GO:0061036; P:positive regulation of cartilage development; IDA:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:DFLAT.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:DFLAT.
GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
GO; GO:0042482; P:positive regulation of odontogenesis; ISS:UniProtKB.
GO; GO:0045778; P:positive regulation of ossification; IDA:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:BHF-UCL.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; ISS:UniProtKB.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:DFLAT.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:UniProtKB.
GO; GO:0010922; P:positive regulation of phosphatase activity; IDA:MGI.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0060804; P:positive regulation of Wnt signaling pathway by BMP signaling pathway; ISS:UniProtKB.
GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:DFLAT.
GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl.
GO; GO:0042487; P:regulation of odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:HGNC.
GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:UniProtKB.
GO; GO:0021537; P:telencephalon development; IDA:MGI.
GO; GO:0021978; P:telencephalon regionalization; ISS:UniProtKB.
GO; GO:0060129; P:thyroid-stimulating hormone-secreting cell differentiation; ISS:UniProtKB.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Chondrogenesis; Cleavage on pair of basic residues;
Complete proteome; Cytokine; Developmental protein; Differentiation;
Disulfide bond; Glycoprotein; Growth factor; Osteogenesis;
Pharmaceutical; Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 282 Cleaved by PCSK5.
/FTId=PRO_0000033824.
CHAIN 283 396 Bone morphogenetic protein 2.
/FTId=PRO_0000033825.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 163 163 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 338 338 N-linked (GlcNAc...) (high mannose)
asparagine. {ECO:0000269|PubMed:9265423}.
DISULFID 296 361
DISULFID 325 393
DISULFID 329 395
DISULFID 360 360 Interchain.
VARIANT 37 37 S -> A (in dbSNP:rs2273073).
/FTId=VAR_020061.
VARIANT 77 77 P -> S (in dbSNP:rs36105541).
/FTId=VAR_052568.
VARIANT 106 106 A -> T (in dbSNP:rs2273074).
/FTId=VAR_020062.
VARIANT 161 161 L -> S (in dbSNP:rs34183594).
/FTId=VAR_052569.
VARIANT 190 190 R -> S (in dbSNP:rs235768).
/FTId=VAR_024232.
VARIANT 387 387 D -> G (in dbSNP:rs11545591).
/FTId=VAR_052570.
STRAND 295 299 {ECO:0000244|PDB:2H62}.
STRAND 302 304 {ECO:0000244|PDB:2H62}.
HELIX 305 308 {ECO:0000244|PDB:2H62}.
TURN 311 313 {ECO:0000244|PDB:2H62}.
STRAND 314 316 {ECO:0000244|PDB:2H62}.
STRAND 318 321 {ECO:0000244|PDB:2H62}.
STRAND 324 326 {ECO:0000244|PDB:2H62}.
HELIX 333 336 {ECO:0000244|PDB:4UI2}.
STRAND 337 339 {ECO:0000244|PDB:2H62}.
HELIX 341 352 {ECO:0000244|PDB:2H62}.
STRAND 354 356 {ECO:0000244|PDB:1REU}.
STRAND 360 374 {ECO:0000244|PDB:2H62}.
HELIX 376 378 {ECO:0000244|PDB:4UI1}.
STRAND 380 396 {ECO:0000244|PDB:2H62}.
SEQUENCE 396 AA; 44702 MW; 20653A3987B25E60 CRC64;
MVAGTRCLLA LLLPQVLLGG AAGLVPELGR RKFAAASSGR PSSQPSDEVL SEFELRLLSM
FGLKQRPTPS RDAVVPPYML DLYRRHSGQP GSPAPDHRLE RAASRANTVR SFHHEESLEE
LPETSGKTTR RFFFNLSSIP TEEFITSAEL QVFREQMQDA LGNNSSFHHR INIYEIIKPA
TANSKFPVTR LLDTRLVNQN ASRWESFDVT PAVMRWTAQG HANHGFVVEV AHLEEKQGVS
KRHVRISRSL HQDEHSWSQI RPLLVTFGHD GKGHPLHKRE KRQAKHKQRK RLKSSCKRHP
LYVDFSDVGW NDWIVAPPGY HAFYCHGECP FPLADHLNST NHAIVQTLVN SVNSKIPKAC
CVPTELSAIS MLYLDENEKV VLKNYQDMVV EGCGCR


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