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 24-JAN-2024, entry version 206. 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/"; 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; 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 GlyCosmos; Q99075; 7 sites, 6 glycans. DR GlyGen; Q99075; 10 sites, 7 O-linked glycans (9 sites). DR iPTMnet; Q99075; -. DR PhosphoSitePlus; Q99075; -. DR BioMuta; HBEGF; -. DR DMDM; 544477; -. DR MassIVE; Q99075; -. DR PaxDb; 9606-ENSP00000230990; -. DR PeptideAtlas; Q99075; -. DR ProteomicsDB; 78230; -. DR Pumba; Q99075; -. DR ABCD; Q99075; 9 sequenced antibodies. DR Antibodypedia; 26845; 528 antibodies from 32 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 AGR; HGNC:3059; -. 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; 5322886at2759; -. 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 1149 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 174 other cell types or tissues. 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:0005886; C:plasma membrane; ISS:BHF-UCL. 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:0051549; P:positive regulation of keratinocyte migration; IEA:Ensembl. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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 Gene3D; 2.10.25.10; Laminin; 1. DR IDEAL; IID00579; -. DR InterPro; IPR000742; EGF-like_dom. DR PANTHER; PTHR10740:SF4; PROHEPARIN-BINDING EGF-LIKE GROWTH FACTOR; 1. DR PANTHER; PTHR10740; TRANSFORMING GROWTH FACTOR ALPHA; 1. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. DR Genevisible; Q99075; HS. 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 //