ID MFGM_HUMAN Reviewed; 387 AA. AC Q08431; B2R6M7; F5GZN3; Q53FU9; Q7Z3D2; Q9BTL9; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 12-SEP-2018, sequence version 3. DT 27-MAR-2024, entry version 203. DE RecName: Full=Lactadherin; DE AltName: Full=Breast epithelial antigen BA46; DE AltName: Full=HMFG; DE AltName: Full=MFGM; DE AltName: Full=Milk fat globule-EGF factor 8; DE Short=MFG-E8; DE AltName: Full=SED1; DE Contains: DE RecName: Full=Lactadherin short form; DE Contains: DE RecName: Full=Medin; DE Flags: Precursor; GN Name=MFGE8; 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] (ISOFORM 1), AND VARIANT MET-76. RC TISSUE=Mammary carcinoma, and Mammary gland; RX PubMed=8639264; DOI=10.1089/dna.1996.15.281; RA Couto J.R., Taylor M.R., Godwin S.G., Ceriani R.L., Peterson J.A.; RT "Cloning and sequence analysis of human breast epithelial antigen BA46 RT reveals an RGD cell adhesion sequence presented on an epidermal growth RT factor-like domain."; RL DNA Cell Biol. 15:281-286(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-76. RA Sivashanmugam P., Richardson R.T., Hamil K.G., Hall S.H., French F.S., RA O'Rand M.G.; RT "Characterization of human epididymal protein."; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT MET-76. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Dermoid cancer, and Pancreas; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Retina; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-76. 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT MET-76. RC TISSUE=Skin; 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 [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 170-387. RC TISSUE=Mammary gland; RX PubMed=1909932; RA Larocca D., Peterson J.A., Urrea R., Kuniyoshi J., Bistrain A.M., RA Ceriani R.L.; RT "A Mr 46,000 human milk fat globule protein that is highly expressed in RT human breast tumors contains factor VIII-like domains."; RL Cancer Res. 51:4994-4998(1991). RN [11] RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION. RC TISSUE=Milk; RX PubMed=9535276; DOI=10.1023/a:1022531500370; RA Giuffrida M.G., Cavaletto M., Giunta C., Conti A., Godovac-Zimmermann J.; RT "Isolation and characterization of full and truncated forms of human breast RT carcinoma protein BA46 from human milk fat globule membranes."; RL J. Protein Chem. 17:143-148(1998). RN [12] RP PROTEIN SEQUENCE OF 268-317, AND IDENTIFICATION OF MEDIN. RX PubMed=10411933; DOI=10.1073/pnas.96.15.8669; RA Haeggqvist B., Naeslund J., Sletten K., Westermark G.T., Mucchiano G., RA Tjernberg L.O., Nordstedt C., Engstroem U., Westermark P.; RT "Medin: an integral fragment of aortic smooth muscle cell-produced RT lactadherin forms the most common human amyloid."; RL Proc. Natl. Acad. Sci. U.S.A. 96:8669-8674(1999). RN [13] RP CHARACTERIZATION. RX PubMed=9260929; DOI=10.1089/dna.1997.16.861; RA Taylor M.R., Couto J.R., Scallan C.D., Ceriani R.L., Peterson J.A.; RT "Lactadherin (formerly BA46), a membrane-associated glycoprotein expressed RT in human milk and breast carcinomas, promotes Arg-Gly-Asp (RGD)-dependent RT cell adhesion."; RL DNA Cell Biol. 16:861-869(1997). RN [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-228; ASN-238; ASN-325; ASN-329 RP AND ASN-350. 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 [15] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=19204935; DOI=10.1002/jcb.22076; RA Raymond A., Ensslin M.A., Shur B.D.; RT "SED1/MFG-E8: a bi-motif protein that orchestrates diverse cellular RT interactions."; RL J. Cell. Biochem. 106:957-966(2009). RN [16] RP PHOSPHORYLATION AT SER-42. RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028; RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J., RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N., RA Pinna L.A., Pagliarini D.J., Dixon J.E.; RT "A single kinase generates the majority of the secreted phosphoproteome."; RL Cell 161:1619-1632(2015). CC -!- FUNCTION: Plays an important role in the maintenance of intestinal CC epithelial homeostasis and the promotion of mucosal healing. Promotes CC VEGF-dependent neovascularization (By similarity). Contributes to CC phagocytic removal of apoptotic cells in many tissues. Specific ligand CC for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to CC phosphatidylserine-enriched cell surfaces in a receptor-independent CC manner. Zona pellucida-binding protein which may play a role in gamete CC interaction. {ECO:0000250, ECO:0000269|PubMed:19204935}. CC -!- FUNCTION: [Medin]: Main constituent of aortic medial amyloid. CC {ECO:0000269|PubMed:19204935}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19204935}; CC Peripheral membrane protein {ECO:0000269|PubMed:19204935}. Secreted CC {ECO:0000269|PubMed:19204935}. Cytoplasmic vesicle, secretory vesicle, CC acrosome membrane {ECO:0000250|UniProtKB:P79385}; Peripheral membrane CC protein {ECO:0000250|UniProtKB:P79385}. Note=Located in the acrosomal CC region of zona-pellucida bound sperm. {ECO:0000250|UniProtKB:P79385}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q08431-1; Sequence=Displayed; CC Name=2; CC IsoId=Q08431-2; Sequence=VSP_039108; CC Name=3; CC IsoId=Q08431-3; Sequence=VSP_039953; CC Name=4; CC IsoId=Q08431-4; Sequence=VSP_059818; CC -!- TISSUE SPECIFICITY: Mammary epithelial cell surfaces and aortic media. CC Overexpressed in several carcinomas. CC -!- DOMAIN: The F5/8 type C 2 domain mediates high-affinity binding to CC phosphatidylserine-containing membranes. {ECO:0000250}. CC -!- PTM: Medin has a ragged N-terminus with minor species starting at Pro- CC 264 and Gly-273. CC -!- MISCELLANEOUS: [Isoform 2]: It is unsure whether Met-1 or an upstream CC Met is the initiator as the upstream Met corresponds to polymorphism CC rs1879326. {ECO:0000305}. 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; U58516; AAC50549.1; -; mRNA. DR EMBL; AY141974; AAN08508.1; -; mRNA. DR EMBL; BT006948; AAP35594.1; -; mRNA. DR EMBL; AK312640; BAG35524.1; -; mRNA. DR EMBL; AK223182; BAD96902.1; -; mRNA. DR EMBL; AK222735; BAD96455.1; -; mRNA. DR EMBL; BX537974; CAD97938.1; -; mRNA. DR EMBL; AC067805; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471101; EAX02026.1; -; Genomic_DNA. DR EMBL; BC003610; AAH03610.1; -; mRNA. DR EMBL; S56151; AAB19771.1; -; mRNA. DR CCDS; CCDS10347.1; -. [Q08431-1] DR CCDS; CCDS45345.1; -. [Q08431-3] DR CCDS; CCDS81918.1; -. [Q08431-4] DR CCDS; CCDS92057.1; -. [Q08431-2] DR PIR; A47285; A47285. DR RefSeq; NP_001108086.1; NM_001114614.2. [Q08431-3] DR RefSeq; NP_001297248.1; NM_001310319.1. [Q08431-4] DR RefSeq; NP_001297249.1; NM_001310320.1. DR RefSeq; NP_001297250.1; NM_001310321.1. [Q08431-2] DR RefSeq; NP_005919.2; NM_005928.3. [Q08431-1] DR AlphaFoldDB; Q08431; -. DR SMR; Q08431; -. DR BioGRID; 110398; 88. DR CORUM; Q08431; -. DR IntAct; Q08431; 9. DR STRING; 9606.ENSP00000268150; -. DR ChEMBL; CHEMBL3713343; -. DR GlyConnect; 1437; 32 N-Linked glycans (3 sites). DR GlyCosmos; Q08431; 5 sites, 34 glycans. DR GlyGen; Q08431; 7 sites, 34 N-linked glycans (3 sites), 1 O-linked glycan (1 site). DR iPTMnet; Q08431; -. DR PhosphoSitePlus; Q08431; -. DR SwissPalm; Q08431; -. DR BioMuta; MFGE8; -. DR DMDM; 2506380; -. DR EPD; Q08431; -. DR jPOST; Q08431; -. DR MassIVE; Q08431; -. DR MaxQB; Q08431; -. DR PaxDb; 9606-ENSP00000268150; -. DR PeptideAtlas; Q08431; -. DR ProteomicsDB; 25082; -. DR ProteomicsDB; 58610; -. [Q08431-1] DR ProteomicsDB; 58611; -. [Q08431-2] DR ProteomicsDB; 58612; -. [Q08431-3] DR Pumba; Q08431; -. DR ABCD; Q08431; 2 sequenced antibodies. DR Antibodypedia; 651; 761 antibodies from 36 providers. DR DNASU; 4240; -. DR Ensembl; ENST00000268150.13; ENSP00000268150.8; ENSG00000140545.16. [Q08431-1] DR Ensembl; ENST00000268151.11; ENSP00000268151.7; ENSG00000140545.16. [Q08431-3] DR Ensembl; ENST00000542878.5; ENSP00000444332.1; ENSG00000140545.16. [Q08431-4] DR Ensembl; ENST00000566497.5; ENSP00000456281.1; ENSG00000140545.16. [Q08431-1] DR Ensembl; ENST00000695566.1; ENSP00000512026.1; ENSG00000140545.16. [Q08431-2] DR GeneID; 4240; -. DR KEGG; hsa:4240; -. DR MANE-Select; ENST00000268150.13; ENSP00000268150.8; NM_005928.4; NP_005919.2. DR UCSC; uc002bng.5; human. [Q08431-1] DR AGR; HGNC:7036; -. DR CTD; 4240; -. DR DisGeNET; 4240; -. DR GeneCards; MFGE8; -. DR HGNC; HGNC:7036; MFGE8. DR HPA; ENSG00000140545; Low tissue specificity. DR MIM; 602281; gene. DR neXtProt; NX_Q08431; -. DR OpenTargets; ENSG00000140545; -. DR PharmGKB; PA30772; -. DR VEuPathDB; HostDB:ENSG00000140545; -. DR eggNOG; ENOG502QVK3; Eukaryota. DR GeneTree; ENSGT00940000156049; -. DR HOGENOM; CLU_030066_0_1_1; -. DR InParanoid; Q08431; -. DR OMA; YVKTFKV; -. DR OrthoDB; 3043281at2759; -. DR PhylomeDB; Q08431; -. DR TreeFam; TF330156; -. DR PathwayCommons; Q08431; -. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation. DR Reactome; R-HSA-977225; Amyloid fiber formation. DR SignaLink; Q08431; -. DR SIGNOR; Q08431; -. DR BioGRID-ORCS; 4240; 13 hits in 1160 CRISPR screens. DR ChiTaRS; MFGE8; human. DR GeneWiki; MFGE8; -. DR GenomeRNAi; 4240; -. DR Pharos; Q08431; Tbio. DR PRO; PR:Q08431; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q08431; Protein. DR Bgee; ENSG00000140545; Expressed in descending thoracic aorta and 176 other cell types or tissues. DR ExpressionAtlas; Q08431; baseline and differential. DR GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005178; F:integrin binding; IEA:Ensembl. DR GO; GO:0001786; F:phosphatidylserine binding; IPI:ARUK-UCL. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0043277; P:apoptotic cell clearance; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW. DR CDD; cd00054; EGF_CA; 1. DR CDD; cd00057; FA58C; 2. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2. DR Gene3D; 2.10.25.10; Laminin; 1. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000421; FA58C. DR InterPro; IPR008979; Galactose-bd-like_sf. DR PANTHER; PTHR46806:SF10; EGF-LIKE REPEAT AND DISCOIDIN I-LIKE DOMAIN-CONTAINING PROTEIN 3 PRECURSOR; 1. DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00008; EGF; 1. DR Pfam; PF00754; F5_F8_type_C; 2. DR SMART; SM00181; EGF; 1. DR SMART; SM00231; FA58C; 2. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 2. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS01285; FA58C_1; 2. DR PROSITE; PS01286; FA58C_2; 2. DR PROSITE; PS50022; FA58C_3; 2. DR Genevisible; Q08431; HS. PE 1: Evidence at protein level; KW Alternative splicing; Amyloid; Angiogenesis; Cell adhesion; KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; KW EGF-like domain; Fertilization; Glycoprotein; Membrane; Phosphoprotein; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..23 FT CHAIN 24..387 FT /note="Lactadherin" FT /id="PRO_0000007650" FT CHAIN 202..387 FT /note="Lactadherin short form" FT /id="PRO_0000007651" FT CHAIN 268..317 FT /note="Medin" FT /id="PRO_0000007652" FT DOMAIN 24..67 FT /note="EGF-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 70..225 FT /note="F5/8 type C 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT DOMAIN 230..387 FT /note="F5/8 type C 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT MOTIF 46..48 FT /note="Cell attachment site" FT MOD_RES 42 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT CARBOHYD 228 FT /note="N-linked (GlcNAc...) asparagine; atypical" FT /evidence="ECO:0000269|PubMed:18780401" FT CARBOHYD 238 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401" FT CARBOHYD 325 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401" FT CARBOHYD 329 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401" FT CARBOHYD 350 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401" FT DISULFID 27..38 FT /evidence="ECO:0000250" FT DISULFID 32..55 FT /evidence="ECO:0000250" FT DISULFID 57..66 FT /evidence="ECO:0000250" FT DISULFID 70..225 FT /evidence="ECO:0000250" FT DISULFID 212..216 FT /evidence="ECO:0000250" FT DISULFID 230..387 FT /evidence="ECO:0000250" FT VAR_SEQ 1..112 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_039108" FT VAR_SEQ 25..69 FT /note="DICSKNPCHNGGLCEEISQEVRGDVFPSYTCTCLKGYAGNHCETK -> E FT (in isoform 4)" FT /id="VSP_059818" FT VAR_SEQ 291..342 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_039953" FT VARIANT 3 FT /note="R -> S (in dbSNP:rs4945)" FT /id="VAR_029794" FT VARIANT 76 FT /note="L -> M (in dbSNP:rs1878326)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:8639264, ECO:0000269|Ref.2, FT ECO:0000269|Ref.3, ECO:0000269|Ref.8" FT /id="VAR_024263" FT CONFLICT 268 FT /note="R -> W (in Ref. 6; CAD97938)" FT /evidence="ECO:0000305" FT CONFLICT 352 FT /note="S -> T (in Ref. 6; CAD97938)" FT /evidence="ECO:0000305" SQ SEQUENCE 387 AA; 43105 MW; 9EA357581933789D CRC64; MPRPRLLAAL CGALLCAPSL LVALDICSKN PCHNGGLCEE ISQEVRGDVF PSYTCTCLKG YAGNHCETKC VEPLGLENGN IANSQIAASS VRVTFLGLQH WVPELARLNR AGMVNAWTPS SNDDNPWIQV NLLRRMWVTG VVTQGASRLA SHEYLKAFKV AYSLNGHEFD FIHDVNKKHK EFVGNWNKNA VHVNLFETPV EAQYVRLYPT SCHTACTLRF ELLGCELNGC ANPLGLKNNS IPDKQITASS SYKTWGLHLF SWNPSYARLD KQGNFNAWVA GSYGNDQWLQ VDLGSSKEVT GIITQGARNF GSVQFVASYK VAYSNDSANW TEYQDPRTGS SKIFPGNWDN HSHKKNLFET PILARYVRIL PVAWHNRIAL RLELLGC //