HBEGF_HUMAN
ID HBEGF_HUMAN Reviewed; 208 AA.
AC Q99075; B2R821;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Proheparin-binding EGF-like growth factor;
DE Contains:
DE RecName: Full=Heparin-binding EGF-like growth factor;
DE Short=HB-EGF;
DE Short=HBEGF;
DE AltName: Full=Diphtheria toxin receptor;
DE Short=DT-R;
DE Flags: Precursor;
GN Name=HBEGF; Synonyms=DTR, DTS, HEGFL;
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], AND PROTEIN SEQUENCE OF 73-93.
RC TISSUE=Macrophage;
RX PubMed=1840698; DOI=10.1126/science.1840698;
RA Higashiyama S., Abraham J.A., Miller J., Fiddes J.C., Klagsbrun M.;
RT "A heparin-binding growth factor secreted by macrophage-like cells that is
RT related to EGF.";
RL Science 251:936-939(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [7]
RP PROTEIN SEQUENCE OF 63-141 AND 143-148, AND GLYCOSYLATION AT THR-75 AND
RP THR-85.
RC TISSUE=Histiocytic lymphoma;
RX PubMed=1556128; DOI=10.1016/s0021-9258(18)42682-8;
RA Higashiyama S., Lau K., Besner G.E., Abraham J.A., Klagsbrun M.;
RT "Structure of heparin-binding EGF-like growth factor. Multiple forms,
RT primary structure, and glycosylation of the mature protein.";
RL J. Biol. Chem. 267:6205-6212(1992).
RN [8]
RP DOMAIN TOXIN BINDING.
RX PubMed=7836353; DOI=10.1074/jbc.270.3.1015;
RA Mitamura T., Higashiyama S., Taniguchi N., Klagsbrun M., Mekada E.;
RT "Diphtheria toxin binds to the epidermal growth factor (EGF)-like domain of
RT human heparin-binding EGF-like growth factor/diphtheria toxin receptor and
RT inhibits specifically its mitogenic activity.";
RL J. Biol. Chem. 270:1015-1019(1995).
RN [9]
RP INTERACTION WITH ERBB4.
RX PubMed=9135143; DOI=10.1093/emboj/16.6.1268;
RA Elenius K., Paul S., Allison G., Sun J., Klagsbrun M.;
RT "Activation of HER4 by heparin-binding EGF-like growth factor stimulates
RT chemotaxis but not proliferation.";
RL EMBO J. 16:1268-1278(1997).
RN [10]
RP REVIEW.
RX PubMed=16508205; DOI=10.1247/csf.31.1;
RA Iwamoto R., Mekada E.;
RT "ErbB and HB-EGF signaling in heart development and function.";
RL Cell Struct. Funct. 31:1-14(2006).
RN [11]
RP GLYCOSYLATION AT THR-44 AND THR-47, STRUCTURE OF CARBOHYDRATES, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
RN [12]
RP GLYCOSYLATION AT THR-37; SER-38 AND THR-44, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 73-147 IN COMPLEX WITH TOX.
RX PubMed=9659904; DOI=10.1016/s1097-2765(00)80008-8;
RA Louie G.V., Yang W., Bowman M.E., Choe S.;
RT "Crystal structure of the complex of diphtheria toxin with an extracellular
RT fragment of its receptor.";
RL Mol. Cell 1:67-78(1997).
CC -!- FUNCTION: Growth factor that mediates its effects via EGFR, ERBB2 and
CC ERBB4. Required for normal cardiac valve formation and normal heart
CC function. Promotes smooth muscle cell proliferation. May be involved in
CC macrophage-mediated cellular proliferation. It is mitogenic for
CC fibroblasts, but not endothelial cells. It is able to bind EGF
CC receptor/EGFR with higher affinity than EGF itself and is a far more
CC potent mitogen for smooth muscle cells than EGF. Also acts as a
CC diphtheria toxin receptor.
CC -!- SUBUNIT: Interacts with FBLN1 (By similarity). Interacts with EGFR and
CC ERBB4. {ECO:0000250, ECO:0000269|PubMed:9135143,
CC ECO:0000269|PubMed:9659904}.
CC -!- INTERACTION:
CC Q99075; P00533: EGFR; NbExp=3; IntAct=EBI-7211558, EBI-297353;
CC Q99075; Q15303: ERBB4; NbExp=2; IntAct=EBI-7211558, EBI-80371;
CC Q99075; P22607: FGFR3; NbExp=3; IntAct=EBI-7211558, EBI-348399;
CC Q99075; P06396: GSN; NbExp=3; IntAct=EBI-7211558, EBI-351506;
CC -!- SUBCELLULAR LOCATION: [Heparin-binding EGF-like growth factor]:
CC Secreted, extracellular space. Note=Mature HB-EGF is released into the
CC extracellular space and probably binds to a receptor.
CC -!- SUBCELLULAR LOCATION: [Proheparin-binding EGF-like growth factor]: Cell
CC membrane; Single-pass type I membrane protein.
CC -!- PTM: Several N-termini have been identified by direct sequencing. The
CC forms with N-termini 63, 73 and 74 have been tested and found to be
CC biologically active.
CC -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans. Thr-47 is a
CC minor glycosylation site compared to Thr-44.
CC {ECO:0000269|PubMed:1556128, ECO:0000269|PubMed:22171320,
CC ECO:0000269|PubMed:23234360}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/dtr/";
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DR EMBL; M60278; AAA35956.1; -; mRNA.
DR EMBL; AY164533; AAN46738.1; -; Genomic_DNA.
DR EMBL; AK313202; BAG36018.1; -; mRNA.
DR EMBL; AC004634; AAC15470.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62069.1; -; Genomic_DNA.
DR EMBL; BC033097; AAH33097.1; -; mRNA.
DR CCDS; CCDS4223.1; -.
DR PIR; A38432; A38432.
DR RefSeq; NP_001936.1; NM_001945.2.
DR PDB; 1XDT; X-ray; 2.65 A; R=73-147.
DR PDB; 2M8S; NMR; -; B=185-208.
DR PDBsum; 1XDT; -.
DR PDBsum; 2M8S; -.
DR AlphaFoldDB; Q99075; -.
DR SMR; Q99075; -.
DR BioGRID; 108172; 16.
DR DIP; DIP-114N; -.
DR IntAct; Q99075; 5.
DR MINT; Q99075; -.
DR STRING; 9606.ENSP00000230990; -.
DR BindingDB; Q99075; -.
DR ChEMBL; CHEMBL3286070; -.
DR GlyConnect; 809; 7 O-Linked glycans (4 sites).
DR GlyGen; Q99075; 7 sites, 6 O-linked glycans (4 sites).
DR iPTMnet; Q99075; -.
DR PhosphoSitePlus; Q99075; -.
DR BioMuta; HBEGF; -.
DR DMDM; 544477; -.
DR MassIVE; Q99075; -.
DR PaxDb; Q99075; -.
DR PeptideAtlas; Q99075; -.
DR PRIDE; Q99075; -.
DR ProteomicsDB; 78230; -.
DR ABCD; Q99075; 9 sequenced antibodies.
DR Antibodypedia; 26845; 400 antibodies from 31 providers.
DR DNASU; 1839; -.
DR Ensembl; ENST00000230990.7; ENSP00000230990.6; ENSG00000113070.8.
DR GeneID; 1839; -.
DR KEGG; hsa:1839; -.
DR MANE-Select; ENST00000230990.7; ENSP00000230990.6; NM_001945.3; NP_001936.1.
DR UCSC; uc003lfi.4; human.
DR CTD; 1839; -.
DR DisGeNET; 1839; -.
DR GeneCards; HBEGF; -.
DR HGNC; HGNC:3059; HBEGF.
DR HPA; ENSG00000113070; Tissue enhanced (urinary).
DR MIM; 126150; gene.
DR neXtProt; NX_Q99075; -.
DR OpenTargets; ENSG00000113070; -.
DR PharmGKB; PA27513; -.
DR VEuPathDB; HostDB:ENSG00000113070; -.
DR eggNOG; ENOG502S0ZP; Eukaryota.
DR GeneTree; ENSGT00940000156901; -.
DR HOGENOM; CLU_096527_2_0_1; -.
DR InParanoid; Q99075; -.
DR OMA; YSYDHTT; -.
DR OrthoDB; 1348306at2759; -.
DR PhylomeDB; Q99075; -.
DR TreeFam; TF332773; -.
DR PathwayCommons; Q99075; -.
DR Reactome; R-HSA-1227986; Signaling by ERBB2.
DR Reactome; R-HSA-1236394; Signaling by ERBB4.
DR Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-HSA-1250342; PI3K events in ERBB4 signaling.
DR Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-177929; Signaling by EGFR.
DR Reactome; R-HSA-179812; GRB2 events in EGFR signaling.
DR Reactome; R-HSA-180292; GAB1 signalosome.
DR Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
DR Reactome; R-HSA-182971; EGFR downregulation.
DR Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-HSA-1963642; PI3K events in ERBB2 signaling.
DR Reactome; R-HSA-212718; EGFR interacts with phospholipase C-gamma.
DR Reactome; R-HSA-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-5336415; Uptake and function of diphtheria toxin.
DR Reactome; R-HSA-5638303; Inhibition of Signaling by Overexpressed EGFR.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6785631; ERBB2 Regulates Cell Motility.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-8847993; ERBB2 Activates PTK6 Signaling.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8857538; PTK6 promotes HIF1A stabilization.
DR Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-HSA-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR Reactome; R-HSA-9664565; Signaling by ERBB2 KD Mutants.
DR Reactome; R-HSA-9665686; Signaling by ERBB2 TMD/JMD mutants.
DR SignaLink; Q99075; -.
DR SIGNOR; Q99075; -.
DR BioGRID-ORCS; 1839; 11 hits in 1071 CRISPR screens.
DR ChiTaRS; HBEGF; human.
DR EvolutionaryTrace; Q99075; -.
DR GeneWiki; Heparin-binding_EGF-like_growth_factor; -.
DR GenomeRNAi; 1839; -.
DR Pharos; Q99075; Tbio.
DR PRO; PR:Q99075; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q99075; protein.
DR Bgee; ENSG00000113070; Expressed in synovial joint and 172 other tissues.
DR Genevisible; Q99075; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IMP:UniProtKB.
DR GO; GO:0048018; F:receptor ligand activity; IDA:MGI.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IDA:MGI.
DR GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:MGI.
DR GO; GO:0038134; P:ERBB2-EGFR signaling pathway; IEA:Ensembl.
DR GO; GO:0038135; P:ERBB2-ERBB4 signaling pathway; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0051545; P:negative regulation of elastin biosynthetic process; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IBA:GO_Central.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:BHF-UCL.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0090303; P:positive regulation of wound healing; IMP:BHF-UCL.
DR GO; GO:0008016; P:regulation of heart contraction; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IEA:Ensembl.
DR DisProt; DP01873; -.
DR IDEAL; IID00579; -.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR015497; EGF_rcpt_ligand.
DR PANTHER; PTHR10740; PTHR10740; 1.
DR Pfam; PF00008; EGF; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Glycoprotein; Growth factor; Heparin-binding; Membrane;
KW Receptor; Reference proteome; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..208
FT /note="Proheparin-binding EGF-like growth factor"
FT /id="PRO_0000302803"
FT PROPEP 20..62
FT /note="Or 72, or 73, or 76, or 81"
FT /evidence="ECO:0000269|PubMed:1556128"
FT /id="PRO_0000007611"
FT CHAIN 63..148
FT /note="Heparin-binding EGF-like growth factor"
FT /id="PRO_0000007612"
FT PROPEP 149..208
FT /note="C-terminal"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007613"
FT TOPO_DOM 20..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 104..144
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 33..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 141
FT /note="Plays a critical role in diphtheria toxin binding
FT and toxin sensitivity"
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305|PubMed:23234360"
FT CARBOHYD 38
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000305|PubMed:23234360"
FT CARBOHYD 44
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:22171320,
FT ECO:0000269|PubMed:23234360"
FT CARBOHYD 47
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:22171320"
FT CARBOHYD 75
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1556128"
FT CARBOHYD 85
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1556128"
FT DISULFID 108..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 116..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 134..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT TURN 108..114
FT /evidence="ECO:0007829|PDB:1XDT"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1XDT"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:1XDT"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1XDT"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1XDT"
FT STRAND 188..195
FT /evidence="ECO:0007829|PDB:2M8S"
SQ SEQUENCE 208 AA; 23067 MW; 2C43C9D1D8291B51 CRC64;
MKLLPSVVLK LFLAAVLSAL VTGESLERLR RGLAAGTSNP DPPTVSTDQL LPLGGGRDRK
VRDLQEADLD LLRVTLSSKP QALATPNKEE HGKRKKKGKG LGKKRDPCLR KYKDFCIHGE
CKYVKELRAP SCICHPGYHG ERCHGLSLPV ENRLYTYDHT TILAVVAVVL SSVCLLVIVG
LLMFRYHRRG GYDVENEEKV KLGMTNSH
