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   07-OCT-2020, entry version 180.
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       {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; 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; 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; 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; 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   BMRB; Q9Y6C2; -.
DR   SMR; Q9Y6C2; -.
DR   BioGRID; 116292; 72.
DR   ComplexPortal; CPX-421; EMILIN-1 complex.
DR   CORUM; Q9Y6C2; -.
DR   DIP; DIP-35733N; -.
DR   IntAct; Q9Y6C2; 72.
DR   MINT; Q9Y6C2; -.
DR   STRING; 9606.ENSP00000369677; -.
DR   GlyConnect; 1201; 6 N-Linked glycans (2 sites).
DR   GlyGen; Q9Y6C2; 12 sites, 2 O-linked glycans (5 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   PaxDb; Q9Y6C2; -.
DR   PeptideAtlas; Q9Y6C2; -.
DR   PRIDE; Q9Y6C2; -.
DR   ProteomicsDB; 35392; -.
DR   ProteomicsDB; 76828; -.
DR   ProteomicsDB; 86648; -. [Q9Y6C2-1]
DR   Antibodypedia; 1001; 184 antibodies.
DR   Ensembl; ENST00000380320; ENSP00000369677; ENSG00000138080. [Q9Y6C2-1]
DR   GeneID; 11117; -.
DR   KEGG; hsa:11117; -.
DR   UCSC; uc002rii.5; human. [Q9Y6C2-1]
DR   CTD; 11117; -.
DR   DisGeNET; 11117; -.
DR   EuPathDB; HostDB:ENSG00000138080.13; -.
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   eggNOG; ENOG502RIZH; Eukaryota.
DR   GeneTree; ENSGT00950000182813; -.
DR   InParanoid; Q9Y6C2; -.
DR   OMA; RLEDQFN; -.
DR   OrthoDB; 1205089at2759; -.
DR   PhylomeDB; Q9Y6C2; -.
DR   TreeFam; TF331033; -.
DR   PathwayCommons; Q9Y6C2; -.
DR   Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR   BioGRID-ORCS; 11117; 5 hits in 872 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 ovary and 182 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: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:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
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   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; Polymorphism;
KW   Reference proteome; 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   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   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:0000244|PDB:2KA3"
FT   STRAND          884..886
FT                   /evidence="ECO:0000244|PDB:2KA3"
FT   STRAND          891..897
FT                   /evidence="ECO:0000244|PDB:2KA3"
FT   TURN            902..905
FT                   /evidence="ECO:0000244|PDB:2KA3"
FT   STRAND          906..908
FT                   /evidence="ECO:0000244|PDB:2KA3"
FT   STRAND          913..919
FT                   /evidence="ECO:0000244|PDB:2KA3"
FT   STRAND          929..933
FT                   /evidence="ECO:0000244|PDB:2KA3"
FT   TURN            935..937
FT                   /evidence="ECO:0000244|PDB:2KA3"
FT   STRAND          942..946
FT                   /evidence="ECO:0000244|PDB:2KA3"
FT   STRAND          972..974
FT                   /evidence="ECO:0000244|PDB:2OII"
FT   STRAND          982..986
FT                   /evidence="ECO:0000244|PDB:2KA3"
FT   STRAND          1002..1009
FT                   /evidence="ECO:0000244|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
//