PDGFB_MOUSE
ID PDGFB_MOUSE Reviewed; 241 AA.
AC P31240; Q6P3C4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Platelet-derived growth factor subunit B;
DE Short=PDGF subunit B;
DE AltName: Full=PDGF-2;
DE AltName: Full=Platelet-derived growth factor B chain;
DE AltName: Full=Platelet-derived growth factor beta polypeptide;
DE AltName: Full=Proto-oncogene c-Sis;
DE Flags: Precursor;
GN Name=Pdgfb; Synonyms=Sis;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2045107; DOI=10.1016/0888-7543(91)90515-g;
RA Bonthron D.T., Sultan P., Collins T.;
RT "Structure of the murine c-sis proto-oncogene (Sis, PDGFB) encoding the B
RT chain of platelet-derived growth factor.";
RL Genomics 10:287-292(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Mammary gland;
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 DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=7958863; DOI=10.1101/gad.8.16.1875;
RA Leveen P., Pekny M., Gebre-Medhin S., Swolin B., Larsson E., Betsholtz C.;
RT "Mice deficient for PDGF B show renal, cardiovascular, and hematological
RT abnormalities.";
RL Genes Dev. 8:1875-1887(1994).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=9211853; DOI=10.1126/science.277.5323.242;
RA Lindahl P., Johansson B.R., Leveen P., Betsholtz C.;
RT "Pericyte loss and microaneurysm formation in PDGF-B-deficient mice.";
RL Science 277:242-245(1997).
RN [5]
RP FUNCTION.
RX PubMed=10734101; DOI=10.1074/jbc.275.13.9527;
RA Arar M., Xu Y.C., Elshihabi I., Barnes J.L., Choudhury G.G., Abboud H.E.;
RT "Platelet-derived growth factor receptor beta regulates migration and DNA
RT synthesis in metanephric mesenchymal cells.";
RL J. Biol. Chem. 275:9527-9533(2000).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=11264163; DOI=10.1182/blood.v97.7.1990;
RA Kaminski W.E., Lindahl P., Lin N.L., Broudy V.C., Crosby J.R.,
RA Hellstrom M., Swolin B., Bowen-Pope D.F., Martin P.J., Ross R.,
RA Betsholtz C., Raines E.W.;
RT "Basis of hematopoietic defects in platelet-derived growth factor (PDGF)-B
RT and PDGF beta-receptor null mice.";
RL Blood 97:1990-1998(2001).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=14514732; DOI=10.1097/01.asn.0000089828.73014.c8;
RA Taneda S., Hudkins K.L., Topouzis S., Gilbertson D.G., Ophascharoensuk V.,
RA Truong L., Johnson R.J., Alpers C.E.;
RT "Obstructive uropathy in mice and humans: potential role for PDGF-D in the
RT progression of tubulointerstitial injury.";
RL J. Am. Soc. Nephrol. 14:2544-2555(2003).
RN [8]
RP FUNCTION.
RX PubMed=14561699; DOI=10.1172/jci200318549;
RA Abramsson A., Lindblom P., Betsholtz C.;
RT "Endothelial and nonendothelial sources of PDGF-B regulate pericyte
RT recruitment and influence vascular pattern formation in tumors.";
RL J. Clin. Invest. 112:1142-1151(2003).
RN [9]
RP REVIEW.
RX PubMed=15207812; DOI=10.1016/j.cytogfr.2004.03.003;
RA Tallquist M., Kazlauskas A.;
RT "PDGF signaling in cells and mice.";
RL Cytokine Growth Factor Rev. 15:205-213(2004).
RN [10]
RP REVIEW ON FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15207813; DOI=10.1016/j.cytogfr.2004.03.005;
RA Betsholtz C.;
RT "Insight into the physiological functions of PDGF through genetic studies
RT in mice.";
RL Cytokine Growth Factor Rev. 15:215-228(2004).
RN [11]
RP FUNCTION.
RX PubMed=19030102; DOI=10.1371/journal.pone.0003794;
RA Wu E., Palmer N., Tian Z., Moseman A.P., Galdzicki M., Wang X., Berger B.,
RA Zhang H., Kohane I.S.;
RT "Comprehensive dissection of PDGF-PDGFR signaling pathways in PDGFR
RT genetically defined cells.";
RL PLoS ONE 3:E3794-E3794(2008).
CC -!- FUNCTION: Growth factor that plays an essential role in the regulation
CC of embryonic development, cell proliferation, cell migration, survival
CC and chemotaxis. Potent mitogen for cells of mesenchymal origin.
CC Required for normal proliferation and recruitment of pericytes and
CC vascular smooth muscle cells in the central nervous system, skin, lung,
CC heart and placenta. Required for normal blood vessel development, and
CC for normal development of kidney glomeruli. Plays an important role in
CC wound healing. Signaling is modulated by the formation of heterodimers
CC with PDGFA. {ECO:0000269|PubMed:10734101, ECO:0000269|PubMed:14561699,
CC ECO:0000269|PubMed:19030102, ECO:0000269|PubMed:7958863}.
CC -!- SUBUNIT: Antiparallel homodimer; disulfide-linked. Antiparallel
CC heterodimer with PDGFA; disulfide-linked. The PDGFB homodimer interacts
CC with PDGFRA and PDGFRB homodimers, and with heterodimers formed by
CC PDGFRA and PDGFRB. The heterodimer composed of PDGFA and PDGFB
CC interacts with PDGFRB homodimers, and with heterodimers formed by
CC PDGFRA and PDGFRB. Interacts with XLKD1 (By similarity). Interacts with
CC LRP1 (By similarity). Interacts with SORL1 (via the N-terminal
CC ectodomain) (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P01127}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon
CC wounding. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Localized to vascular smooth muscle cells. Also
CC weakly expressed by cortical interstitial cells but absent in tubules.
CC Up-regulated in areas of renal fibrosis. In mice with unilateral
CC ureteral obstruction, an increased expression in interstitial cells and
CC in some tubules observed after day 4. {ECO:0000269|PubMed:14514732}.
CC -!- DISRUPTION PHENOTYPE: Perinatal lethality, due to severe hemorrhages
CC shortly before birth. Kidney glomerular tufts do not form, apparently
CC because of absence of mesangial cells. The heart and some large
CC arteries are dilated in late-stage embryos. Mice lack microvascular
CC pericytes, which normally form part of the capillary wall, and develop
CC numerous capillary microaneurysms, leading to hemorrhages. Mice display
CC erythroblastosis, macrocytic anemia, and thrombocytopenia.
CC {ECO:0000269|PubMed:11264163, ECO:0000269|PubMed:15207813,
CC ECO:0000269|PubMed:7958863, ECO:0000269|PubMed:9211853}.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; M84453; AAA40113.1; -; Genomic_DNA.
DR EMBL; M84448; AAA40113.1; JOINED; Genomic_DNA.
DR EMBL; M84449; AAA40113.1; JOINED; Genomic_DNA.
DR EMBL; M84450; AAA40113.1; JOINED; Genomic_DNA.
DR EMBL; M84451; AAA40113.1; JOINED; Genomic_DNA.
DR EMBL; M84452; AAA40113.1; JOINED; Genomic_DNA.
DR EMBL; M64849; AAA37485.1; -; Genomic_DNA.
DR EMBL; M64844; AAA37485.1; JOINED; Genomic_DNA.
DR EMBL; M64845; AAA37485.1; JOINED; Genomic_DNA.
DR EMBL; M64846; AAA37485.1; JOINED; Genomic_DNA.
DR EMBL; M64847; AAA37485.1; JOINED; Genomic_DNA.
DR EMBL; M64848; AAA37485.1; JOINED; Genomic_DNA.
DR EMBL; BC053430; AAH53430.1; -; mRNA.
DR EMBL; BC064056; AAH64056.1; -; mRNA.
DR CCDS; CCDS27656.1; -.
DR PIR; A39073; PFMSGB.
DR RefSeq; NP_035187.2; NM_011057.3.
DR RefSeq; XP_017171991.1; XM_017316502.1.
DR AlphaFoldDB; P31240; -.
DR SMR; P31240; -.
DR ComplexPortal; CPX-2900; Platelet-derived growth factor AB complex.
DR ComplexPortal; CPX-2901; PDGF receptor alpha - PDGF-AB complex.
DR ComplexPortal; CPX-2903; PDGF receptor alpha-beta - PDGF-AB complex.
DR ComplexPortal; CPX-2904; PDGF receptor beta - PDGF-AB complex.
DR ComplexPortal; CPX-2905; Platelet-derived growth factor BB complex.
DR ComplexPortal; CPX-2906; PDGF receptor alpha - PDGF-BB complex.
DR ComplexPortal; CPX-2907; PDGF receptor alpha-beta - PDGF-BB complex.
DR ComplexPortal; CPX-2908; PDGF receptor beta - PDGF-BB complex.
DR IntAct; P31240; 1.
DR STRING; 10090.ENSMUSP00000000500; -.
DR GlyGen; P31240; 1 site.
DR iPTMnet; P31240; -.
DR PhosphoSitePlus; P31240; -.
DR MaxQB; P31240; -.
DR PaxDb; P31240; -.
DR PeptideAtlas; P31240; -.
DR PRIDE; P31240; -.
DR ProteomicsDB; 294045; -.
DR DNASU; 18591; -.
DR GeneID; 18591; -.
DR KEGG; mmu:18591; -.
DR UCSC; uc007wuz.1; mouse.
DR CTD; 5155; -.
DR MGI; MGI:97528; Pdgfb.
DR eggNOG; ENOG502S2VW; Eukaryota.
DR InParanoid; P31240; -.
DR OrthoDB; 1439735at2759; -.
DR PhylomeDB; P31240; -.
DR TreeFam; TF319554; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-186763; Downstream signal transduction.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR BioGRID-ORCS; 18591; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Pdgfb; mouse.
DR PRO; PR:P31240; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P31240; protein.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:1990265; C:platelet-derived growth factor complex; ISO:MGI.
DR GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; ISS:UniProtKB.
DR GO; GO:0070851; F:growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:MGI.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISS:UniProtKB.
DR GO; GO:0001568; P:blood vessel development; IEP:UniProtKB.
DR GO; GO:0048514; P:blood vessel morphogenesis; IDA:MGI.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI.
DR GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; TAS:DFLAT.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IGI:MGI.
DR GO; GO:0030031; P:cell projection assembly; IDA:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:MGI.
DR GO; GO:0071506; P:cellular response to mycophenolic acid; ISS:UniProtKB.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IDA:BHF-UCL.
DR GO; GO:0001892; P:embryonic placenta development; IMP:UniProtKB.
DR GO; GO:0001935; P:endothelial cell proliferation; IGI:MGI.
DR GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; IMP:MGI.
DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:MGI.
DR GO; GO:0010761; P:fibroblast migration; IDA:MGI.
DR GO; GO:0021782; P:glial cell development; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0035655; P:interleukin-18-mediated signaling pathway; ISO:MGI.
DR GO; GO:0072264; P:metanephric glomerular endothelium development; IEP:UniProtKB.
DR GO; GO:0072255; P:metanephric glomerular mesangial cell development; IMP:UniProtKB.
DR GO; GO:0072262; P:metanephric glomerular mesangial cell proliferation involved in metanephros development; IMP:UniProtKB.
DR GO; GO:0002548; P:monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0010512; P:negative regulation of phosphatidylinositol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010544; P:negative regulation of platelet activation; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1905064; P:negative regulation of vascular associated smooth muscle cell differentiation; ISO:MGI.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IGI:MGI.
DR GO; GO:0016322; P:neuron remodeling; IMP:MGI.
DR GO; GO:0038001; P:paracrine signaling; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IGI:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0090280; P:positive regulation of calcium ion import; ISS:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; TAS:BHF-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IGI:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IDA:MGI.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IGI:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:0003104; P:positive regulation of glomerular filtration; IMP:UniProtKB.
DR GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; ISS:UniProtKB.
DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; ISO:MGI.
DR GO; GO:1904899; P:positive regulation of hepatic stellate cell proliferation; ISO:MGI.
DR GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:2000591; P:positive regulation of metanephric mesenchymal cell migration; ISO:MGI.
DR GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; ISS:UniProtKB.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0045977; P:positive regulation of mitotic cell cycle, embryonic; IGI:MGI.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IGI:MGI.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1905176; P:positive regulation of vascular associated smooth muscle cell dedifferentiation; ISO:MGI.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IGI:MGI.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; TAS:DFLAT.
DR GO; GO:0070528; P:protein kinase C signaling; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:MGI.
DR GO; GO:0006929; P:substrate-dependent cell migration; IDA:MGI.
DR GO; GO:0007416; P:synapse assembly; IMP:MGI.
DR GO; GO:1904738; P:vascular associated smooth muscle cell migration; IGI:MGI.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IGI:MGI.
DR GO; GO:0042310; P:vasoconstriction; TAS:DFLAT.
DR CDD; cd00135; PDGF; 1.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR023581; PD_growth_factor_CS.
DR InterPro; IPR000072; PDGF/VEGF_dom.
DR InterPro; IPR006782; PDGF_N.
DR InterPro; IPR015583; PDGF_suB.
DR PANTHER; PTHR11633:SF2; PTHR11633:SF2; 1.
DR Pfam; PF00341; PDGF; 1.
DR Pfam; PF04692; PDGF_N; 1.
DR SMART; SM00141; PDGF; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00249; PDGF_1; 1.
DR PROSITE; PS50278; PDGF_2; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Developmental protein; Disulfide bond;
KW Glycoprotein; Growth factor; Mitogen; Proto-oncogene; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT PROPEP 21..81
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023374"
FT CHAIN 82..190
FT /note="Platelet-derived growth factor subunit B"
FT /id="PRO_0000023375"
FT PROPEP 191..241
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023376"
FT REGION 217..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 108
FT /note="Involved in receptor binding"
FT SITE 111
FT /note="Involved in receptor binding"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..141
FT /evidence="ECO:0000250"
FT DISULFID 124
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 130..178
FT /evidence="ECO:0000250"
FT DISULFID 133
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 134..180
FT /evidence="ECO:0000250"
FT CONFLICT 183
FT /note="I -> V (in Ref. 2; AAH53430/AAH64056)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 241 AA; 27382 MW; 3C5EB7A2DAD64178 CRC64;
MNRCWALFLP LCCYLRLVSA EGDPIPEELY EMLSDHSIRS FDDLQRLLHR DSVDEDGAEL
DLNMTRAHSG VELESSSRGR RSLGSLAAAE PAVIAECKTR TEVFQISRNL IDRTNANFLV
WPPCVEVQRC SGCCNNRNVQ CRASQVQMRP VQVRKIEIVR KKPIFKKATV TLEDHLACKC
ETIVTPRPVT RSPGTSREQR AKTPQARVTI RTVRIRRPPK GKHRKFKHTH DKAALKETLG
A
