MMRN1_HUMAN
ID MMRN1_HUMAN Reviewed; 1228 AA.
AC Q13201; Q4W5L1; Q6P3T8; Q6ZUL9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Multimerin-1;
DE AltName: Full=EMILIN-4;
DE AltName: Full=Elastin microfibril interface located protein 4;
DE Short=Elastin microfibril interfacer 4;
DE AltName: Full=Endothelial cell multimerin;
DE Contains:
DE RecName: Full=Platelet glycoprotein Ia*;
DE Contains:
DE RecName: Full=155 kDa platelet multimerin;
DE Short=p-155;
DE Short=p155;
DE Flags: Precursor;
GN Name=MMRN1; Synonyms=ECM, EMILIN4, GPIA*, MMRN;
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), PROTEIN SEQUENCE OF 368-376,
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Endothelial cell;
RX PubMed=7629143; DOI=10.1074/jbc.270.31.18246;
RA Hayward C.P.M., Hassell J.A., Denomme G.A., Rachubinski R.A., Brown C.,
RA Kelton J.G.;
RT "The cDNA sequence of human endothelial cell multimerin. A unique protein
RT with RGDS, coiled-coil, and epidermal growth factor-like domains and a
RT carboxyl terminus similar to the globular domain of complement C1q and
RT collagens type VIII and X.";
RL J. Biol. Chem. 270:18246-18251(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-964.
RC TISSUE=PNS;
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 [6]
RP PROTEIN SEQUENCE OF 184-198 AND 318-326.
RX PubMed=9798985;
RA Polgar J., Magnenat E., Wells T.N.C., Clemetson K.J.;
RT "Platelet glycoprotein Ia* is the processed form of multimerin -- isolation
RT and determination of N-terminal sequences of stored and released forms.";
RL Thromb. Haemost. 80:645-648(1998).
RN [7]
RP PROTEIN SEQUENCE OF 461-467.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=8514871; DOI=10.1172/jci116502;
RA Hayward C.P.M., Bainton D.F., Smith J.W., Horsewood P., Stead R.H.,
RA Podor T.J., Warkentin T.E., Kelton J.G.;
RT "Multimerin is found in the alpha-granules of resting platelets and is
RT synthesized by a megakaryocytic cell line.";
RL J. Clin. Invest. 91:2630-2639(1993).
RN [9]
RP SUBUNIT.
RX PubMed=10613677;
RA Hayward C.P.M.;
RT "Platelet multimerin and its proteolytic processing.";
RL Thromb. Haemost. 82:1779-1780(1999).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-114; ASN-120; ASN-136; ASN-618
RP AND ASN-729.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP FUNCTION.
RX PubMed=16363244; DOI=10.1160/th05-02-0140;
RA Adam F., Zheng S., Joshi N., Kelton D.S., Sandhu A., Suehiro Y.,
RA Jeimy S.B., Santos A.V., Masse J.-M., Kelton J.G., Cramer E.M.,
RA Hayward C.P.M.;
RT "Analyses of cellular multimerin 1 receptors: in vitro evidence of binding
RT mediated by alphaIIbbeta3 and alphavbeta3.";
RL Thromb. Haemost. 94:1004-1011(2005).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-114.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [13]
RP FUNCTION, AND INTERACTION WITH FACTOR V.
RX PubMed=19132231; DOI=10.1160/th08-05-0307;
RA Jeimy S.B., Fuller N., Tasneem S., Segers K., Stafford A.R., Weitz J.I.,
RA Camire R.M., Nicolaes G.A.F., Hayward C.P.M.;
RT "Multimerin 1 binds factor V and activated factor V with high affinity and
RT inhibits thrombin generation.";
RL Thromb. Haemost. 100:1058-1067(2008).
RN [14]
RP DISEASE.
RX PubMed=8652809;
RA Hayward C.P.M., Rivard G.E., Kane W.H., Drouin J., Zheng S., Moore J.C.,
RA Kelton J.G.;
RT "An autosomal dominant, qualitative platelet disorder associated with
RT multimerin deficiency, abnormalities in platelet factor V, thrombospondin,
RT von Willebrand factor, and fibrinogen and an epinephrine aggregation
RT defect.";
RL Blood 87:4967-4978(1996).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-344; ASN-729; ASN-942 AND
RP ASN-1020.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP GLYCOSYLATION AT ASN-136.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
CC -!- FUNCTION: Carrier protein for platelet (but not plasma) factor V/Va.
CC Plays a role in the storage and stabilization of factor V in platelets.
CC Upon release following platelet activation, may limit platelet and
CC plasma factor Va-dependent thrombin generation. Ligand for integrin
CC alpha-IIb/beta-3 and integrin alpha-V/beta-3 on activated platelets,
CC and may function as an extracellular matrix or adhesive protein.
CC {ECO:0000269|PubMed:16363244, ECO:0000269|PubMed:19132231,
CC ECO:0000269|PubMed:7629143}.
CC -!- SUBUNIT: Multimeric. Composed of varying sized, disulfide-linked
CC multimers, the smallest of which is a homotrimer. Proteolysis of the
CC promultimerin in the N-terminal region, leads to the mature p155 form
CC that is stored in platelets. Interacts with factor V/Va.
CC {ECO:0000269|PubMed:10613677, ECO:0000269|PubMed:19132231,
CC ECO:0000269|PubMed:7629143}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13201-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13201-2; Sequence=VSP_036610, VSP_036611;
CC -!- TISSUE SPECIFICITY: Synthesized by endothelial cells and
CC megakaryocytes. Stored in platelet alpha granules and endothelial cell
CC Weibel-Palade bodies, following activation of these cells, it is
CC released and attached to megakaryocytes, platelets, endothelium and
CC subendothelium of blood vessels. Not found in plasma. Found in vascular
CC tissues such as placenta, lung, and liver. {ECO:0000269|PubMed:7629143,
CC ECO:0000269|PubMed:8514871}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Extensively N-glycosylated. {ECO:0000269|PubMed:16263699,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
CC ECO:0000269|PubMed:19159218}.
CC -!- DISEASE: Note=Deficiency in multimerin-1 due to proteolytic degradation
CC within the platelet alpha granules is associated with an autosomal
CC dominant bleeding disorder (factor V Quebec).
CC {ECO:0000269|PubMed:8652809}.
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DR EMBL; U27109; AAC52065.1; -; mRNA.
DR EMBL; AK125557; BAC86201.1; -; mRNA.
DR EMBL; AK313566; BAG36340.1; -; mRNA.
DR EMBL; AC093759; AAY40957.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX06038.1; -; Genomic_DNA.
DR EMBL; BC063848; AAH63848.1; -; mRNA.
DR CCDS; CCDS3635.1; -. [Q13201-1]
DR PIR; A57384; A57384.
DR RefSeq; NP_031377.2; NM_007351.2. [Q13201-1]
DR RefSeq; XP_016863382.1; XM_017007893.1.
DR AlphaFoldDB; Q13201; -.
DR SMR; Q13201; -.
DR BioGRID; 116577; 22.
DR ComplexPortal; CPX-445; Multimerin-1 complex.
DR ComplexPortal; CPX-460; Platelet glycoprotein Ia* complex.
DR ComplexPortal; CPX-461; 155 kDa platelet multimerin complex.
DR IntAct; Q13201; 18.
DR STRING; 9606.ENSP00000378431; -.
DR GlyConnect; 668; 27 N-Linked glycans (16 sites).
DR GlyGen; Q13201; 28 sites, 34 N-linked glycans (16 sites), 1 O-linked glycan (4 sites).
DR iPTMnet; Q13201; -.
DR PhosphoSitePlus; Q13201; -.
DR BioMuta; MMRN1; -.
DR DMDM; 143811421; -.
DR OGP; Q13201; -.
DR EPD; Q13201; -.
DR jPOST; Q13201; -.
DR MassIVE; Q13201; -.
DR MaxQB; Q13201; -.
DR PaxDb; Q13201; -.
DR PeptideAtlas; Q13201; -.
DR PRIDE; Q13201; -.
DR ProteomicsDB; 59220; -. [Q13201-1]
DR ProteomicsDB; 59221; -. [Q13201-2]
DR Antibodypedia; 25682; 198 antibodies from 24 providers.
DR DNASU; 22915; -.
DR Ensembl; ENST00000264790.7; ENSP00000264790.2; ENSG00000138722.10. [Q13201-1]
DR Ensembl; ENST00000394980.5; ENSP00000378431.1; ENSG00000138722.10. [Q13201-1]
DR GeneID; 22915; -.
DR KEGG; hsa:22915; -.
DR MANE-Select; ENST00000264790.7; ENSP00000264790.2; NM_007351.3; NP_031377.2.
DR UCSC; uc003hst.4; human. [Q13201-1]
DR CTD; 22915; -.
DR DisGeNET; 22915; -.
DR GeneCards; MMRN1; -.
DR HGNC; HGNC:7178; MMRN1.
DR HPA; ENSG00000138722; Low tissue specificity.
DR MIM; 601456; gene.
DR neXtProt; NX_Q13201; -.
DR OpenTargets; ENSG00000138722; -.
DR PharmGKB; PA30891; -.
DR VEuPathDB; HostDB:ENSG00000138722; -.
DR eggNOG; ENOG502QTYP; Eukaryota.
DR GeneTree; ENSGT01030000234633; -.
DR InParanoid; Q13201; -.
DR OMA; NCTVKLV; -.
DR OrthoDB; 1205089at2759; -.
DR PhylomeDB; Q13201; -.
DR TreeFam; TF336041; -.
DR PathwayCommons; Q13201; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q13201; -.
DR BioGRID-ORCS; 22915; 4 hits in 1064 CRISPR screens.
DR ChiTaRS; MMRN1; human.
DR GeneWiki; MMRN1; -.
DR GenomeRNAi; 22915; -.
DR Pharos; Q13201; Tbio.
DR PRO; PR:Q13201; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q13201; protein.
DR Bgee; ENSG00000138722; Expressed in pericardium and 139 other tissues.
DR ExpressionAtlas; Q13201; baseline and differential.
DR Genevisible; Q13201; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1990972; C:multimerin complex; IPI:ComplexPortal.
DR GO; GO:0031091; C:platelet alpha granule; IDA:ComplexPortal.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:ComplexPortal.
DR GO; GO:0061045; P:negative regulation of wound healing; IDA:ComplexPortal.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; IDA:ComplexPortal.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR033188; MMRN1.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR15427:SF3; PTHR15427:SF3; 1.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07546; EMI; 1.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1228
FT /note="Multimerin-1"
FT /id="PRO_0000007821"
FT CHAIN 184..1228
FT /note="Platelet glycoprotein Ia*"
FT /id="PRO_0000367047"
FT CHAIN 318..1228
FT /note="155 kDa platelet multimerin"
FT /id="PRO_0000367048"
FT DOMAIN 207..282
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 1041..1077
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1096..1228
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 68..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 333..365
FT /evidence="ECO:0000255"
FT COILED 400..430
FT /evidence="ECO:0000255"
FT COILED 503..523
FT /evidence="ECO:0000255"
FT COILED 580..650
FT /evidence="ECO:0000255"
FT COILED 675..726
FT /evidence="ECO:0000255"
FT COILED 819..869
FT /evidence="ECO:0000255"
FT MOTIF 186..188
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 183..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16263699,
FT ECO:0000269|PubMed:16335952"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 981
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1020
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 1075
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 211..272
FT /evidence="ECO:0000250"
FT DISULFID 238..245
FT /evidence="ECO:0000250"
FT DISULFID 271..280
FT /evidence="ECO:0000250"
FT DISULFID 1045..1056
FT /evidence="ECO:0000250"
FT DISULFID 1050..1065
FT /evidence="ECO:0000250"
FT DISULFID 1067..1076
FT /evidence="ECO:0000250"
FT VAR_SEQ 71..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036610"
FT VAR_SEQ 377..1039
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036611"
FT VARIANT 58
FT /note="T -> A (in dbSNP:rs1442138)"
FT /id="VAR_031471"
FT VARIANT 805
FT /note="T -> A (in dbSNP:rs3756065)"
FT /id="VAR_031472"
FT VARIANT 883
FT /note="G -> D (in dbSNP:rs12646270)"
FT /id="VAR_031473"
FT VARIANT 964
FT /note="T -> R (in dbSNP:rs17855885)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031474"
FT CONFLICT 217
FT /note="R -> K (in Ref. 2; BAC86201)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="I -> T (in Ref. 1; AAC52065)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="L -> S (in Ref. 1; AAC52065)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1228 AA; 138110 MW; 270BCFBE85AA2F8F CRC64;
MKGARLFVLL SSLWSGGIGL NNSKHSWTIP EDGNSQKTMP SASVPPNKIQ SLQILPTTRV
MSAEIATTPE ARTSEDSLLK STLPPSETSA PAEGVRNQTL TSTEKAEGVV KLQNLTLPTN
ASIKFNPGAE SVVLSNSTLK FLQSFARKSN EQATSLNTVG GTGGIGGVGG TGGVGNRAPR
ETYLSRGDSS SSQRTDYQKS NFETTRGKNW CAYVHTRLSP TVILDNQVTY VPGGKGPCGW
TGGSCPQRSQ KISNPVYRMQ HKIVTSLDWR CCPGYSGPKC QLRAQEQQSL IHTNQAESHT
AVGRGVAEQQ QQQGCGDPEV MQKMTDQVNY QAMKLTLLQK KIDNISLTVN DVRNTYSSLE
GKVSEDKSRE FQSLLKGLKS KSINVLIRDI VREQFKIFQN DMQETVAQLF KTVSSLSEDL
ESTRQIIQKV NESVVSIAAQ QKFVLVQENR PTLTDIVELR NHIVNVRQEM TLTCEKPIKE
LEVKQTHLEG ALEQEHSRSI LYYESLNKTL SKLKEVHEQL LSTEQVSDQK NAPAAESVSN
NVTEYMSTLH ENIKKQSLMM LQMFEDLHIQ ESKINNLTVS LEMEKESLRG ECEDMLSKCR
NDFKFQLKDT EENLHVLNQT LAEVLFPMDN KMDKMSEQLN DLTYDMEILQ PLLEQGASLR
QTMTYEQPKE AIVIRKKIEN LTSAVNSLNF IIKELTKRHN LLRNEVQGRD DALERRINEY
ALEMEDGLNK TMTIINNAID FIQDNYALKE TLSTIKDNSE IHHKCTSDME TILTFIPQFH
RLNDSIQTLV NDNQRYNFVL QVAKTLAGIP RDEKLNQSNF QKMYQMFNET TSQVRKYQQN
MSHLEEKLLL TTKISKNFET RLQDIESKVT QTLIPYYISV KKGSVVTNER DQALQLQVLN
SRFKALEAKS IHLSINFFSL NKTLHEVLTM CHNASTSVSE LNATIPKWIK HSLPDIQLLQ
KGLTEFVEPI IQIKTQAALS NLTCCIDRSL PGSLANVVKS QKQVKSLPKK INALKKPTVN
LTTVLIGRTQ RNTDNIIYPE EYSSCSRHPC QNGGTCINGR TSFTCACRHP FTGDNCTIKL
VEENALAPDF SKGSYRYAPM VAFFASHTYG MTIPGPILFN NLDVNYGASY TPRTGKFRIP
YLGVYVFKYT IESFSAHISG FLVVDGIDKL AFESENINSE IHCDRVLTGD ALLELNYGQE
VWLRLAKGTI PAKFPPVTTF SGYLLYRT
