EMIL1_HUMAN
ID EMIL1_HUMAN Reviewed; 1016 AA.
AC Q9Y6C2; A0A0C4DFX3; A5PL03; H0Y7A0; Q53SY9; Q96G58; Q96IH6; Q9UG76;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=EMILIN-1;
DE AltName: Full=Elastin microfibril interface-located protein 1;
DE Short=Elastin microfibril interfacer 1;
DE Flags: Precursor;
GN Name=EMILIN1; Synonyms=EMI;
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).
RX PubMed=10358019; DOI=10.1074/jbc.274.24.16773;
RA Doliana R., Mongiat M., Bucciotti F., Giacomello E., Deutzmann R.,
RA Volpin D., Bressan G.M., Colombatti A.;
RT "EMILIN, a component of the elastic fiber and a new member of the C1q/tumor
RT necrosis factor superfamily of proteins.";
RL J. Biol. Chem. 274:16773-16781(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=10625608; DOI=10.1074/jbc.275.2.785;
RA Doliana R., Canton A., Bucciotti F., Mongiat M., Bonaldo P., Colombatti A.;
RT "Structure, chromosomal localization, and promoter analysis of the human
RT elastin microfibril interface located protein (EMILIN) gene.";
RL J. Biol. Chem. 275:785-792(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-149.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-1016 (ISOFORM 1).
RC TISSUE=Uterus;
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 TISSUE SPECIFICITY.
RX PubMed=11278945; DOI=10.1074/jbc.m011591200;
RA Doliana R., Bot S., Mungiguerra G., Canton A., Cilli S.P., Colombatti A.;
RT "Isolation and characterization of EMILIN-2, a new component of the growing
RT EMILINs family and a member of the EMI domain-containing superfamily.";
RL J. Biol. Chem. 276:12003-12011(2001).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-455.
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 [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415; ASN-455; ASN-766 AND
RP ASN-794.
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP STRUCTURE BY NMR OF 867-1016, AND SUBUNIT.
RX PubMed=19023665; DOI=10.1007/s10858-008-9290-y;
RA Verdone G., Corazza A., Colebrooke S.A., Cicero D., Eliseo T., Boyd J.,
RA Doliana R., Fogolari F., Viglino P., Colombatti A., Campbell I.D.,
RA Esposito G.;
RT "NMR-based homology model for the solution structure of the C-terminal
RT globular domain of EMILIN1.";
RL J. Biomol. NMR 43:79-96(2009).
RN [12]
RP VARIANT THR-22, CHARACTERIZATION OF VARIANT THR-22, SUBCELLULAR LOCATION,
RP AND SIGNAL SEQUENCE CLEAVAGE SITE.
RX PubMed=26462740; DOI=10.1002/humu.22920;
RA Capuano A., Bucciotti F., Farwell K.D., Tippin Davis B., Mroske C.,
RA Hulick P.J., Weissman S.M., Gao Q., Spessotto P., Colombatti A.,
RA Doliana R.;
RT "Diagnostic exome sequencing identifies a novel gene, EMILIN1, associated
RT with autosomal-dominant hereditary connective tissue disease.";
RL Hum. Mutat. 37:84-97(2016).
CC -!- FUNCTION: May be responsible for anchoring smooth muscle cells to
CC elastic fibers, and may be involved not only in the formation of the
CC elastic fiber, but also in the processes that regulate vessel assembly.
CC Has cell adhesive capacity.
CC -!- SUBUNIT: Homotrimer associated through a moderately stable interaction
CC of the C-terminal globular C1q domains, allowing the nucleation of the
CC triple helix and then a further quaternary assembly to higher-order
CC polymers via intermolecular disulfide bonds. Interacts with EMILIN2.
CC Interacts with EFEMP2; this interaction promotes the incorporation of
CC EFEMP2 into the extracellular matrix (By similarity).
CC {ECO:0000250|UniProtKB:Q99K41, ECO:0000269|PubMed:19023665}.
CC -!- INTERACTION:
CC Q9Y6C2; Q00994: BEX3; NbExp=3; IntAct=EBI-744586, EBI-741753;
CC Q9Y6C2; Q5H9J7: BEX5; NbExp=4; IntAct=EBI-744586, EBI-10243741;
CC Q9Y6C2; Q9Y6C2: EMILIN1; NbExp=4; IntAct=EBI-744586, EBI-744586;
CC Q9Y6C2; Q8IY31: IFT20; NbExp=6; IntAct=EBI-744586, EBI-744203;
CC Q9Y6C2; Q6ISS4: LAIR2; NbExp=3; IntAct=EBI-744586, EBI-10250491;
CC Q9Y6C2; Q96PC5: MIA2; NbExp=3; IntAct=EBI-744586, EBI-1050253;
CC Q9Y6C2; Q96QG7: MTMR9; NbExp=10; IntAct=EBI-744586, EBI-744593;
CC Q9Y6C2; Q13287: NMI; NbExp=4; IntAct=EBI-744586, EBI-372942;
CC Q9Y6C2; Q5JTB6: PLAC9; NbExp=5; IntAct=EBI-744586, EBI-3923605;
CC Q9Y6C2; Q8N443: RIBC1; NbExp=3; IntAct=EBI-744586, EBI-10265323;
CC Q9Y6C2; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-744586, EBI-529518;
CC Q9Y6C2; Q53FD0: ZC2HC1C; NbExp=3; IntAct=EBI-744586, EBI-740767;
CC Q9Y6C2-2; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-11748557, EBI-742038;
CC Q9Y6C2-2; P02649: APOE; NbExp=3; IntAct=EBI-11748557, EBI-1222467;
CC Q9Y6C2-2; Q00994: BEX3; NbExp=6; IntAct=EBI-11748557, EBI-741753;
CC Q9Y6C2-2; Q12934-2: BFSP1; NbExp=3; IntAct=EBI-11748557, EBI-12123320;
CC Q9Y6C2-2; Q53HL2: CDCA8; NbExp=3; IntAct=EBI-11748557, EBI-979174;
CC Q9Y6C2-2; Q7L2Z9: CENPQ; NbExp=3; IntAct=EBI-11748557, EBI-2350265;
CC Q9Y6C2-2; A0A0S2Z604: COG7; NbExp=3; IntAct=EBI-11748557, EBI-16430119;
CC Q9Y6C2-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-11748557, EBI-742054;
CC Q9Y6C2-2; Q01658: DR1; NbExp=3; IntAct=EBI-11748557, EBI-750300;
CC Q9Y6C2-2; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-11748557, EBI-21603100;
CC Q9Y6C2-2; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-11748557, EBI-11748557;
CC Q9Y6C2-2; Q9NVF7: FBXO28; NbExp=3; IntAct=EBI-11748557, EBI-740282;
CC Q9Y6C2-2; Q9P2W3: GNG13; NbExp=3; IntAct=EBI-11748557, EBI-11427343;
CC Q9Y6C2-2; P42858: HTT; NbExp=3; IntAct=EBI-11748557, EBI-466029;
CC Q9Y6C2-2; Q8IY31-3: IFT20; NbExp=5; IntAct=EBI-11748557, EBI-9091197;
CC Q9Y6C2-2; Q6ISS4: LAIR2; NbExp=3; IntAct=EBI-11748557, EBI-10250491;
CC Q9Y6C2-2; Q96QG7: MTMR9; NbExp=3; IntAct=EBI-11748557, EBI-744593;
CC Q9Y6C2-2; P35240-4: NF2; NbExp=3; IntAct=EBI-11748557, EBI-1014514;
CC Q9Y6C2-2; Q5JTB6: PLAC9; NbExp=7; IntAct=EBI-11748557, EBI-3923605;
CC Q9Y6C2-2; P54646: PRKAA2; NbExp=3; IntAct=EBI-11748557, EBI-1383852;
CC Q9Y6C2-2; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-11748557, EBI-14093916;
CC Q9Y6C2-2; Q8N443: RIBC1; NbExp=6; IntAct=EBI-11748557, EBI-10265323;
CC Q9Y6C2-2; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-11748557, EBI-12004298;
CC Q9Y6C2-2; Q9NYJ8: TAB2; NbExp=3; IntAct=EBI-11748557, EBI-358708;
CC Q9Y6C2-2; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-11748557, EBI-529518;
CC Q9Y6C2-2; Q99598: TSNAX; NbExp=3; IntAct=EBI-11748557, EBI-742638;
CC Q9Y6C2-2; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-11748557, EBI-14104088;
CC Q9Y6C2-2; Q8N720: ZNF655; NbExp=3; IntAct=EBI-11748557, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:26462740}. Note=Found mainly at the
CC interface between amorphous elastin and microfibrils.
CC {ECO:0000303|PubMed:10625608}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y6C2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6C2-2; Sequence=VSP_055478, VSP_055479, VSP_055480;
CC -!- TISSUE SPECIFICITY: Distributed in tissues where resilience and elastic
CC recoil are prominent. Highest levels in the adult small intestine,
CC aorta, lung, uterus, and appendix and in the fetal spleen, kidney,
CC lung, and heart; intermediate expression was detected in adult liver,
CC ovary, colon, stomach, lymph node and spleen; adult heart, bladder,
CC prostate, adrenal gland, mammary gland, placenta and kidney showed low
CC expression whereas a series of other adult tissues, including skeletal
CC muscle and different regions of adult brain show no expression.
CC {ECO:0000269|PubMed:11278945}.
CC -!- MISCELLANEOUS: Its deposition precedes the appearance of elastin and is
CC simultaneous with that of fibrillin 1.
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DR EMBL; AF088916; AAD42161.1; -; mRNA.
DR EMBL; AF162780; AAF25006.1; -; Genomic_DNA.
DR EMBL; AC013403; AAX93166.1; -; Genomic_DNA.
DR EMBL; KF459615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00645.1; -; Genomic_DNA.
DR EMBL; BC007530; AAH07530.1; -; mRNA.
DR EMBL; BC009947; AAH09947.2; -; mRNA.
DR EMBL; BC136279; AAI36280.1; -; mRNA.
DR EMBL; BC142688; AAI42689.1; -; mRNA.
DR EMBL; AL050138; CAB43287.2; -; mRNA.
DR CCDS; CCDS1733.1; -. [Q9Y6C2-1]
DR PIR; T08772; T08772.
DR RefSeq; NP_008977.1; NM_007046.3. [Q9Y6C2-1]
DR PDB; 2KA3; NMR; -; A/B/C=867-1016.
DR PDB; 2OII; NMR; -; A/B/C=867-1016.
DR PDBsum; 2KA3; -.
DR PDBsum; 2OII; -.
DR AlphaFoldDB; Q9Y6C2; -.
DR BMRB; Q9Y6C2; -.
DR SMR; Q9Y6C2; -.
DR BioGRID; 116292; 114.
DR ComplexPortal; CPX-421; EMILIN-1 complex.
DR CORUM; Q9Y6C2; -.
DR DIP; DIP-35733N; -.
DR IntAct; Q9Y6C2; 77.
DR MINT; Q9Y6C2; -.
DR STRING; 9606.ENSP00000369677; -.
DR GlyConnect; 1201; 6 N-Linked glycans (2 sites).
DR GlyGen; Q9Y6C2; 13 sites, 5 N-linked glycans (2 sites), 3 O-linked glycans (6 sites).
DR iPTMnet; Q9Y6C2; -.
DR PhosphoSitePlus; Q9Y6C2; -.
DR BioMuta; EMILIN1; -.
DR DMDM; 205371751; -.
DR REPRODUCTION-2DPAGE; Q9Y6C2; -.
DR EPD; Q9Y6C2; -.
DR jPOST; Q9Y6C2; -.
DR MassIVE; Q9Y6C2; -.
DR MaxQB; Q9Y6C2; -.
DR PaxDb; Q9Y6C2; -.
DR PeptideAtlas; Q9Y6C2; -.
DR PRIDE; Q9Y6C2; -.
DR ProteomicsDB; 35392; -.
DR ProteomicsDB; 76828; -.
DR ProteomicsDB; 86648; -. [Q9Y6C2-1]
DR Antibodypedia; 1001; 201 antibodies from 25 providers.
DR DNASU; 11117; -.
DR Ensembl; ENST00000380320.9; ENSP00000369677.4; ENSG00000138080.14. [Q9Y6C2-1]
DR GeneID; 11117; -.
DR KEGG; hsa:11117; -.
DR MANE-Select; ENST00000380320.9; ENSP00000369677.4; NM_007046.4; NP_008977.1.
DR UCSC; uc002rii.5; human. [Q9Y6C2-1]
DR CTD; 11117; -.
DR DisGeNET; 11117; -.
DR GeneCards; EMILIN1; -.
DR HGNC; HGNC:19880; EMILIN1.
DR HPA; ENSG00000138080; Low tissue specificity.
DR MalaCards; EMILIN1; -.
DR MIM; 130660; gene.
DR neXtProt; NX_Q9Y6C2; -.
DR OpenTargets; ENSG00000138080; -.
DR Orphanet; 485418; EMILIN-1-related connective tissue disease.
DR PharmGKB; PA134922135; -.
DR VEuPathDB; HostDB:ENSG00000138080; -.
DR eggNOG; ENOG502RIZH; Eukaryota.
DR GeneTree; ENSGT01030000234633; -.
DR InParanoid; Q9Y6C2; -.
DR OMA; MAPSTFW; -.
DR OrthoDB; 1205089at2759; -.
DR PhylomeDB; Q9Y6C2; -.
DR TreeFam; TF331033; -.
DR PathwayCommons; Q9Y6C2; -.
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR SignaLink; Q9Y6C2; -.
DR BioGRID-ORCS; 11117; 11 hits in 1070 CRISPR screens.
DR ChiTaRS; EMILIN1; human.
DR EvolutionaryTrace; Q9Y6C2; -.
DR GeneWiki; EMILIN1; -.
DR GenomeRNAi; 11117; -.
DR Pharos; Q9Y6C2; Tbio.
DR PRO; PR:Q9Y6C2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y6C2; protein.
DR Bgee; ENSG00000138080; Expressed in right coronary artery and 131 other tissues.
DR ExpressionAtlas; Q9Y6C2; baseline and differential.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IMP:UniProtKB.
DR GO; GO:1990971; C:EMILIN complex; IMP:CAFA.
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; IMP:UniProtKB.
DR GO; GO:0034668; C:integrin alpha4-beta1 complex; IMP:CAFA.
DR GO; GO:0030023; F:extracellular matrix constituent conferring elasticity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0098640; F:integrin binding involved in cell-matrix adhesion; IMP:CAFA.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISS:BHF-UCL.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IMP:CAFA.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:CAFA.
DR GO; GO:0048251; P:elastic fiber assembly; ISS:BHF-UCL.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:BHF-UCL.
DR GO; GO:0050866; P:negative regulation of cell activation; ISS:BHF-UCL.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; ISS:BHF-UCL.
DR GO; GO:1904027; P:negative regulation of collagen fibril organization; ISS:BHF-UCL.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:BHF-UCL.
DR GO; GO:1905522; P:negative regulation of macrophage migration; ISS:BHF-UCL.
DR GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; ISS:BHF-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IC:ComplexPortal.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IDA:ComplexPortal.
DR GO; GO:1901203; P:positive regulation of extracellular matrix assembly; ISS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF07546; EMI; 1.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Coiled coil; Collagen;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:26462740"
FT CHAIN 22..1016
FT /note="EMILIN-1"
FT /id="PRO_0000007815"
FT DOMAIN 56..131
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 814..864
FT /note="Collagen-like"
FT DOMAIN 866..1013
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 135..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 216..256
FT /evidence="ECO:0000255"
FT COILED 356..420
FT /evidence="ECO:0000255"
FT COILED 576..603
FT /evidence="ECO:0000255"
FT COILED 685..752
FT /evidence="ECO:0000255"
FT COILED 835..857
FT /evidence="ECO:0000255"
FT COMPBIAS 262..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16263699,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 794
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 60..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 85..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 120..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT VAR_SEQ 1..674
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055478"
FT VAR_SEQ 675
FT /note="L -> M (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055479"
FT VAR_SEQ 813
FT /note="T -> TGEGTK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055480"
FT VARIANT 22
FT /note="A -> T (found in a patient with connective tissue
FT disorder and peripheral neuropathy; unknown pathological
FT significance; decreased secretion; accumulates in the
FT endoplasmic reticulum; dbSNP:rs753862645)"
FT /evidence="ECO:0000269|PubMed:26462740"
FT /id="VAR_077591"
FT VARIANT 149
FT /note="R -> Q (in dbSNP:rs2736976)"
FT /evidence="ECO:0000269|PubMed:15815621"
FT /id="VAR_046095"
FT VARIANT 536
FT /note="Q -> R (in dbSNP:rs36069611)"
FT /id="VAR_046096"
FT VARIANT 903
FT /note="E -> K (in dbSNP:rs36045790)"
FT /id="VAR_046097"
FT STRAND 872..876
FT /evidence="ECO:0007829|PDB:2KA3"
FT STRAND 884..886
FT /evidence="ECO:0007829|PDB:2KA3"
FT STRAND 891..897
FT /evidence="ECO:0007829|PDB:2KA3"
FT TURN 902..905
FT /evidence="ECO:0007829|PDB:2KA3"
FT STRAND 906..908
FT /evidence="ECO:0007829|PDB:2KA3"
FT STRAND 913..919
FT /evidence="ECO:0007829|PDB:2KA3"
FT STRAND 929..933
FT /evidence="ECO:0007829|PDB:2KA3"
FT TURN 935..937
FT /evidence="ECO:0007829|PDB:2KA3"
FT STRAND 942..946
FT /evidence="ECO:0007829|PDB:2KA3"
FT STRAND 972..974
FT /evidence="ECO:0007829|PDB:2OII"
FT STRAND 982..986
FT /evidence="ECO:0007829|PDB:2KA3"
FT STRAND 1002..1009
FT /evidence="ECO:0007829|PDB:2KA3"
SQ SEQUENCE 1016 AA; 106695 MW; 6CF330238DD0EE26 CRC64;
MAPRTLWSCY LCCLLTAAAG AASYPPRGFS LYTGSSGALS PGGPQAQIAP RPASRHRNWC
AYVVTRTVSC VLEDGVETYV KYQPCAWGQP QCPQSIMYRR FLRPRYRVAY KTVTDMEWRC
CQGYGGDDCA ESPAPALGPA SSTPRPLARP ARPNLSGSSA GSPLSGLGGE GPGESEKVQQ
LEEQVQSLTK ELQGLRGVLQ GLSGRLAEDV QRAVETAFNG RQQPADAAAR PGVHETLNEI
QHQLQLLDTR VSTHDQELGH LNNHHGGSSS SGGSRAPAPA SAPPGPSEEL LRQLEQRLQE
SCSVCLAGLD GFRRQQQEDR ERLRAMEKLL ASVEERQRHL AGLAVGRRPP QECCSPELGR
RLAELERRLD VVAGSVTVLS GRRGTELGGA AGQGGHPPGY TSLASRLSRL EDRFNSTLGP
SEEQEESWPG APGGLSHWLP AARGRLEQLG GLLANVSGEL GGRLDLLEEQ VAGAMQACGQ
LCSGAPGEQD SQVSEILSAL ERRVLDSEGQ LRLVGSGLHT VEAAGEARQA TLEGLQEVVG
RLQDRVDAQD ETAAEFTLRL NLTAARLGQL EGLLQAHGDE GCGACGGVQE ELGRLRDGVE
RCSCPLLPPR GPGAGPGVGG PSRGPLDGFS VFGGSSGSAL QALQGELSEV ILSFSSLNDS
LNELQTTVEG QGADLADLGA TKDRIISEIN RLQQEATEHA TESEERFRGL EEGQAQAGQC
PSLEGRLGRL EGVCERLDTV AGGLQGLREG LSRHVAGLWA GLRETNTTSQ MQAALLEKLV
GGQAGLGRRL GALNSSLQLL EDRLHQLSLK DLTGPAGEAG PPGPPGLQGP PGPAGPPGSP
GKDGQEGPIG PPGPQGEQGV EGAPAAPVPQ VAFSAALSLP RSEPGTVPFD RVLLNDGGYY
DPETGVFTAP LAGRYLLSAV LTGHRHEKVE AVLSRSNQGV ARVDSGGYEP EGLENKPVAE
SQPSPGTLGV FSLILPLQAG DTVCVDLVMG QLAHSEEPLT IFSGALLYGD PELEHA
