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 27-MAR-2024, entry version 197. 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 HMND10 THR-22, CHARACTERIZATION OF VARIANT HMND10 THR-22, RP SUBCELLULAR LOCATION, 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). RN [13] RP VARIANT HMND10 CYS-250, INVOLVEMENT IN HMND10, TISSUE SPECIFICITY, RP SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT HMND10 CYS-250. RX PubMed=31978608; DOI=10.1016/j.nbd.2020.104757; RA Iacomino M., Doliana R., Marchese M., Capuano A., Striano P., Spessotto P., RA Bosisio G., Iodice R., Manganelli F., Lanteri P., Orsini A., Baldassari S., RA Baratto S., Fruscione F., Prada V., Broda P., Tessa A., Bertocci G., RA Schenone A., Colombatti A., Minetti C., Santorelli F.M., Zara F., RA Fiorillo C.; RT "Distal motor neuropathy associated with novel EMILIN1 mutation."; RL Neurobiol. Dis. 137:104757-104757(2020). 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, ECO:0000269|PubMed:31978608}. CC Note=Found mainly at the interface between amorphous elastin and CC microfibrils. {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 Detected in intramuscular nerve bundles, where it particularly CC localizes in the epineurium, the most external layer of dense CC connective tissue enclosing the nerve (PubMed:31978608). CC {ECO:0000269|PubMed:11278945, ECO:0000269|PubMed:31978608}. CC -!- DISEASE: Neuronopathy, distal hereditary motor, autosomal dominant 10 CC (HMND10) [MIM:620080]: A form of distal hereditary motor neuronopathy, CC a heterogeneous group of neuromuscular diseases caused by selective CC degeneration of motor neurons in the anterior horn of the spinal cord, CC without sensory deficit in the posterior horn. HMND10 is characterized CC by length-dependent motor neuropathy primarily affecting the lower CC limbs, and onset of distal muscle weakness and atrophy in early CC childhood resulting in walking difficulties and gait abnormalities. CC Some affected individuals have pyramidal signs, including CC hyperreflexia. More variable features may include mild intellectual CC disability, minor gyration defects on brain imaging, foot deformities, CC and connective tissue defects. {ECO:0000269|PubMed:26462740, CC ECO:0000269|PubMed:31978608}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Its deposition precedes the appearance of elastin and is CC simultaneous with that of fibrillin 1. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; Q9Y6C2; 13 sites, 8 glycans. DR GlyGen; Q9Y6C2; 15 sites, 5 N-linked glycans (2 sites), 4 O-linked glycans (8 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; 9606-ENSP00000369677; -. DR PeptideAtlas; Q9Y6C2; -. DR ProteomicsDB; 35392; -. DR ProteomicsDB; 76828; -. DR ProteomicsDB; 86648; -. [Q9Y6C2-1] DR Pumba; Q9Y6C2; -. DR Antibodypedia; 1001; 235 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 AGR; HGNC:19880; -. 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 MIM; 620080; phenotype. 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; EPGTIPF; -. DR OrthoDB; 5314586at2759; -. 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 1150 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 132 other cell types or 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:0060090; F:molecular adaptor activity; IMP:DisProt. 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; ISO:ComplexPortal. 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:0030336; P:negative regulation of cell migration; ISS:ComplexPortal. 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:0060392; P:negative regulation of SMAD protein signal transduction; 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:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; ISS:BHF-UCL. DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:ComplexPortal. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:ComplexPortal. DR GO; GO:0030194; P:positive regulation of blood coagulation; ISS: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:1901731; P:positive regulation of platelet aggregation; ISS:ComplexPortal. DR GO; GO:0008217; P:regulation of blood pressure; ISO:ComplexPortal. DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:ComplexPortal. 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 PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1. DR PANTHER; PTHR15427:SF1; EMILIN-1; 1. DR Pfam; PF00386; C1q; 1. DR Pfam; PF01391; Collagen; 1. DR Pfam; PF07546; EMI; 1. DR SMART; SM00110; C1Q; 1. DR SUPFAM; SSF49842; TNF-like; 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 Disease variant; Disulfide bond; Extracellular matrix; Glycoprotein; KW Neurodegeneration; Neuropathy; 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 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; uncertain significance; FT decreased secretion; accumulates in the endoplasmic FT 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 250 FT /note="R -> C (in HMND10; unable to rescue locomotor FT defects in Emilin1a zebrafish morphants; reduced FT extracellular deposition of EMILIN-1 from patient cells)" FT /evidence="ECO:0000269|PubMed:31978608" FT /id="VAR_087801" 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 //