MFGM_HUMAN
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 03-AUG-2022, entry version 194.
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}.
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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 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; 76.
DR CORUM; Q08431; -.
DR IntAct; Q08431; 8.
DR STRING; 9606.ENSP00000268150; -.
DR ChEMBL; CHEMBL3713343; -.
DR GlyConnect; 1437; 32 N-Linked glycans (3 sites).
DR GlyGen; Q08431; 6 sites, 30 N-linked glycans (3 sites).
DR iPTMnet; Q08431; -.
DR PhosphoSitePlus; Q08431; -.
DR BioMuta; MFGE8; -.
DR DMDM; 2506380; -.
DR EPD; Q08431; -.
DR jPOST; Q08431; -.
DR MassIVE; Q08431; -.
DR MaxQB; Q08431; -.
DR PaxDb; Q08431; -.
DR PeptideAtlas; Q08431; -.
DR PRIDE; Q08431; -.
DR ProteomicsDB; 25082; -.
DR ProteomicsDB; 58610; -. [Q08431-1]
DR ProteomicsDB; 58611; -. [Q08431-2]
DR ProteomicsDB; 58612; -. [Q08431-3]
DR ABCD; Q08431; 2 sequenced antibodies.
DR Antibodypedia; 651; 640 antibodies from 36 providers.
DR DNASU; 4240; -.
DR Ensembl; ENST00000268150.13; ENSP00000268150.8; ENSG00000140545.15. [Q08431-1]
DR Ensembl; ENST00000268151.11; ENSP00000268151.7; ENSG00000140545.15. [Q08431-3]
DR Ensembl; ENST00000542878.5; ENSP00000444332.1; ENSG00000140545.15. [Q08431-4]
DR Ensembl; ENST00000566497.5; ENSP00000456281.1; ENSG00000140545.15. [Q08431-1]
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 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; 441415at2759; -.
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; 12 hits in 1082 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 174 other tissues.
DR ExpressionAtlas; Q08431; baseline and differential.
DR Genevisible; Q08431; HS.
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:0019897; C:extrinsic component of plasma membrane; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0008429; F:phosphatidylethanolamine 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:0006911; P:phagocytosis, engulfment; IEA:Ensembl.
DR GO; GO:0006910; P:phagocytosis, recognition; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR CDD; cd00057; FA58C; 2.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; SSF49785; SSF49785; 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.
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
