GenomeNet

Database: UniProt
Entry: Q08431
LinkDB: Q08431
Original site: Q08431 
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   13-FEB-2019, entry version 173.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RP   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
RT   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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.,
RA   Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
RA   Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
RA   Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
RA   Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
RA   Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
RA   Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
RA   Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human
RT   chromosome 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RP   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
RT   project: 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
RT   in 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.,
RA   Godovac-Zimmermann J.;
RT   "Isolation and characterization of full and truncated forms of human
RT   breast 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
RT   expressed in human milk and breast carcinomas, promotes Arg-Gly-Asp
RT   (RGD)-dependent cell adhesion.";
RL   DNA Cell Biol. 16:861-869(1997).
RN   [14]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-228; ASN-238; ASN-325;
RP   ASN-329 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
RT   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.
CC       Promotes VEGF-dependent neovascularization (By similarity).
CC       Contributes to phagocytic removal of apoptotic cells in many
CC       tissues. Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5
CC       receptors. Also binds to phosphatidylserine-enriched cell surfaces
CC       in a receptor-independent manner. Zona pellucida-binding protein
CC       which may play a role in gamete interaction. {ECO:0000250,
CC       ECO:0000269|PubMed:19204935}.
CC   -!- FUNCTION: Medin is the 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}.
CC       Secreted {ECO:0000269|PubMed:19204935}.
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         Note=It is unsure whether Met-1 or an upstream Met is the
CC         initiator as the upstream Met corresponds to polymorphism
CC         rs1879326. {ECO:0000305};
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
CC       media. 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
CC       Pro-264 and Gly-273.
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   UniGene; Hs.3745; -.
DR   UniGene; Hs.720851; -.
DR   ProteinModelPortal; Q08431; -.
DR   SMR; Q08431; -.
DR   BioGrid; 110398; 6.
DR   CORUM; Q08431; -.
DR   IntAct; Q08431; 2.
DR   STRING; 9606.ENSP00000268150; -.
DR   ChEMBL; CHEMBL3713343; -.
DR   GlyConnect; 1437; -.
DR   iPTMnet; Q08431; -.
DR   PhosphoSitePlus; Q08431; -.
DR   BioMuta; MFGE8; -.
DR   DMDM; 2506380; -.
DR   EPD; Q08431; -.
DR   jPOST; Q08431; -.
DR   PaxDb; Q08431; -.
DR   PeptideAtlas; Q08431; -.
DR   PRIDE; Q08431; -.
DR   ProteomicsDB; 58610; -.
DR   ProteomicsDB; 58611; -. [Q08431-2]
DR   ProteomicsDB; 58612; -. [Q08431-3]
DR   DNASU; 4240; -.
DR   Ensembl; ENST00000268150; ENSP00000268150; ENSG00000140545. [Q08431-1]
DR   Ensembl; ENST00000268151; ENSP00000268151; ENSG00000140545. [Q08431-3]
DR   Ensembl; ENST00000542878; ENSP00000444332; ENSG00000140545. [Q08431-4]
DR   Ensembl; ENST00000566497; ENSP00000456281; ENSG00000140545. [Q08431-1]
DR   GeneID; 4240; -.
DR   KEGG; hsa:4240; -.
DR   UCSC; uc002bng.5; human. [Q08431-1]
DR   CTD; 4240; -.
DR   DisGeNET; 4240; -.
DR   EuPathDB; HostDB:ENSG00000140545.14; -.
DR   GeneCards; MFGE8; -.
DR   H-InvDB; HIX0012558; -.
DR   HGNC; HGNC:7036; MFGE8.
DR   HPA; CAB002753; -.
DR   HPA; HPA002807; -.
DR   MIM; 602281; gene.
DR   neXtProt; NX_Q08431; -.
DR   OpenTargets; ENSG00000140545; -.
DR   PharmGKB; PA30772; -.
DR   eggNOG; ENOG410IFBC; Eukaryota.
DR   eggNOG; ENOG41114BV; LUCA.
DR   GeneTree; ENSGT00940000156049; -.
DR   HOGENOM; HOG000236278; -.
DR   HOVERGEN; HBG002385; -.
DR   InParanoid; Q08431; -.
DR   KO; K17253; -.
DR   OrthoDB; 441415at2759; -.
DR   PhylomeDB; Q08431; -.
DR   TreeFam; TF330156; -.
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   ChiTaRS; MFGE8; human.
DR   GeneWiki; MFGE8; -.
DR   GenomeRNAi; 4240; -.
DR   PRO; PR:Q08431; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   Bgee; ENSG00000140545; Expressed in 207 organ(s), highest expression level in descending thoracic aorta.
DR   ExpressionAtlas; Q08431; baseline and differential.
DR   Genevisible; Q08431; HS.
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:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
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; IEA:Ensembl.
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:0044267; P:cellular protein metabolic process; TAS:Reactome.
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:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   CDD; cd00057; FA58C; 2.
DR   Gene3D; 2.60.120.260; -; 2.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR027060; Lactadherin.
DR   PANTHER; PTHR44122:SF1; PTHR44122:SF1; 2.
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   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Fertilization; Glycoprotein; Membrane;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL        1     23
FT   CHAIN        24    387       Lactadherin.
FT                                /FTId=PRO_0000007650.
FT   CHAIN       202    387       Lactadherin short form.
FT                                /FTId=PRO_0000007651.
FT   CHAIN       268    317       Medin.
FT                                /FTId=PRO_0000007652.
FT   DOMAIN       24     67       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       70    225       F5/8 type C 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00081}.
FT   DOMAIN      230    387       F5/8 type C 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00081}.
FT   MOTIF        46     48       Cell attachment site.
FT   MOD_RES      42     42       Phosphoserine; by FAM20C.
FT                                {ECO:0000269|PubMed:26091039}.
FT   CARBOHYD    228    228       N-linked (GlcNAc...) asparagine;
FT                                atypical. {ECO:0000269|PubMed:18780401}.
FT   CARBOHYD    238    238       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:18780401}.
FT   CARBOHYD    325    325       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:18780401}.
FT   CARBOHYD    329    329       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:18780401}.
FT   CARBOHYD    350    350       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:18780401}.
FT   DISULFID     27     38       {ECO:0000250}.
FT   DISULFID     32     55       {ECO:0000250}.
FT   DISULFID     57     66       {ECO:0000250}.
FT   DISULFID     70    225       {ECO:0000250}.
FT   DISULFID    212    216       {ECO:0000250}.
FT   DISULFID    230    387       {ECO:0000250}.
FT   VAR_SEQ       1    112       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_039108.
FT   VAR_SEQ      25     69       DICSKNPCHNGGLCEEISQEVRGDVFPSYTCTCLKGYAGNH
FT                                CETK -> E (in isoform 4).
FT                                /FTId=VSP_059818.
FT   VAR_SEQ     291    342       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_039953.
FT   VARIANT       3      3       R -> S (in dbSNP:rs4945).
FT                                /FTId=VAR_029794.
FT   VARIANT      76     76       L -> M (in dbSNP:rs1878326).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:8639264,
FT                                ECO:0000269|Ref.2, ECO:0000269|Ref.3,
FT                                ECO:0000269|Ref.8}.
FT                                /FTId=VAR_024263.
FT   CONFLICT    268    268       R -> W (in Ref. 6; CAD97938).
FT                                {ECO:0000305}.
FT   CONFLICT    352    352       S -> T (in Ref. 6; CAD97938).
FT                                {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
//
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