ID EMID1_HUMAN Reviewed; 441 AA. AC Q96A84; B0QYK6; Q6ICG1; Q86SS7; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-NOV-2024, entry version 157. DE RecName: Full=EMI domain-containing protein 1; DE AltName: Full=Emilin and multimerin domain-containing protein 1; DE Short=Emu1; DE Flags: Precursor; GN Name=EMID1; Synonyms=EMU1; 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] (ISOFORMS 1 AND 2). RX PubMed=12221002; DOI=10.1006/dbio.2002.0764; RA Leimeister C., Steidl C., Schumacher N., Erhard S., Gessler M.; RT "Developmental expression and biochemical characterization of Emu family RT members."; RL Dev. Biol. 249:204-218(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). 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 3), AND VARIANT GLY-107. 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). CC -!- SUBUNIT: Homo- or heteromers. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96A84-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96A84-2; Sequence=VSP_008445; CC Name=3; CC IsoId=Q96A84-3; Sequence=VSP_011824; CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice CC site. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing acceptor splice CC site. {ECO:0000305}. 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; AJ416090; CAC94777.1; -; mRNA. DR EMBL; CH471095; EAW59776.1; -; Genomic_DNA. DR EMBL; AL031186; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z95116; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC046358; AAH46358.1; -; mRNA. DR EMBL; CR456407; CAG30293.1; -; mRNA. DR CCDS; CCDS33630.1; -. [Q96A84-3] DR RefSeq; NP_001254824.1; NM_001267895.1. [Q96A84-1] DR RefSeq; NP_597712.2; NM_133455.3. [Q96A84-3] DR AlphaFoldDB; Q96A84; -. DR BioGRID; 126183; 38. DR IntAct; Q96A84; 29. DR STRING; 9606.ENSP00000335481; -. DR GlyCosmos; Q96A84; 2 sites, No reported glycans. DR GlyGen; Q96A84; 2 sites. DR iPTMnet; Q96A84; -. DR PhosphoSitePlus; Q96A84; -. DR BioMuta; EMID1; -. DR DMDM; 37537826; -. DR MassIVE; Q96A84; -. DR PaxDb; 9606-ENSP00000335481; -. DR PeptideAtlas; Q96A84; -. DR ProteomicsDB; 75935; -. [Q96A84-1] DR ProteomicsDB; 75936; -. [Q96A84-2] DR ProteomicsDB; 75937; -. [Q96A84-3] DR Antibodypedia; 248; 89 antibodies from 21 providers. DR DNASU; 129080; -. DR Ensembl; ENST00000334018.11; ENSP00000335481.6; ENSG00000186998.16. [Q96A84-3] DR GeneID; 129080; -. DR KEGG; hsa:129080; -. DR MANE-Select; ENST00000334018.11; ENSP00000335481.6; NM_133455.4; NP_597712.2. [Q96A84-3] DR UCSC; uc003aem.5; human. [Q96A84-1] DR AGR; HGNC:18036; -. DR CTD; 129080; -. DR DisGeNET; 129080; -. DR GeneCards; EMID1; -. DR HGNC; HGNC:18036; EMID1. DR HPA; ENSG00000186998; Tissue enhanced (brain, lymphoid tissue). DR MIM; 608926; gene. DR neXtProt; NX_Q96A84; -. DR OpenTargets; ENSG00000186998; -. DR PharmGKB; PA134921314; -. DR VEuPathDB; HostDB:ENSG00000186998; -. DR eggNOG; ENOG502QSR5; Eukaryota. DR GeneTree; ENSGT00940000161542; -. DR HOGENOM; CLU_045268_0_0_1; -. DR InParanoid; Q96A84; -. DR OMA; CEEXVAV; -. DR OrthoDB; 3062338at2759; -. DR PhylomeDB; Q96A84; -. DR TreeFam; TF336589; -. DR PathwayCommons; Q96A84; -. DR SignaLink; Q96A84; -. DR BioGRID-ORCS; 129080; 15 hits in 1156 CRISPR screens. DR ChiTaRS; EMID1; human. DR GenomeRNAi; 129080; -. DR Pharos; Q96A84; Tbio. DR PRO; PR:Q96A84; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q96A84; protein. DR Bgee; ENSG00000186998; Expressed in ventricular zone and 134 other cell types or tissues. DR ExpressionAtlas; Q96A84; baseline and differential. DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR InterPro; IPR008160; Collagen. DR InterPro; IPR050392; Collagen/C1q_domain. DR InterPro; IPR011489; EMI_domain. DR PANTHER; PTHR15427:SF23; EMI DOMAIN-CONTAINING PROTEIN 1; 1. DR PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1. DR Pfam; PF01391; Collagen; 3. DR Pfam; PF07546; EMI; 1. DR PROSITE; PS51041; EMI; 1. PE 1: Evidence at protein level; KW Alternative splicing; Collagen; Disulfide bond; Extracellular matrix; KW Glycoprotein; Proteomics identification; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..441 FT /note="EMI domain-containing protein 1" FT /id="PRO_0000007823" FT DOMAIN 33..106 FT /note="EMI" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384" FT DOMAIN 179..368 FT /note="Collagen-like" FT REGION 162..371 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 405..441 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 164..183 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 243..265 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 273..290 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 291..324 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 51 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 136 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 37..96 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384" FT DISULFID 62..68 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384" FT DISULFID 95..104 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384" FT VAR_SEQ 72..73 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12221002" FT /id="VSP_008445" FT VAR_SEQ 106 FT /note="E -> EVA (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15461802, FT ECO:0000303|PubMed:15489334" FT /id="VSP_011824" FT VARIANT 107 FT /note="A -> G (in dbSNP:rs743920)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_019803" SQ SEQUENCE 441 AA; 45292 MW; 676D491C4083E18E CRC64; MGGPRAWALL CLGLLLPGGG AAWSIGAAPF SGRRNWCSYV VTRTISCHVQ NGTYLQRVLQ NCPWPMSCPG SSYRTVVRPT YKVMYKIVTA REWRCCPGHS GVSCEEASSA SLEPMWSGST MRRMALRPTA FSGCLNCSKV SELTERLKVL EAKMTMLTVI EQPVPPTPAT PEDPAPLWGP PPAQGSPGDG GLQDQVGAWG LPGPTGPKGD AGSRGPMGMR GPPGPQGPPG SPGRAGAVGT PGERGPPGPP GPPGPPGPPA PVGPPHARIS QHGDPLLSNT FTETNNHWPQ GPTGPPGPPG PMGPPGPPGP TGVPGSPGHI GPPGPTGPKG ISGHPGEKGE RGLRGEPGPQ GSAGQRGEPG PKGDPGEKSH WGEGLHQLRE ALKILAERVL ILETMIGLYE PELGSGAGPA GTGTPSLLRG KRGGHATNYR IVAPRSRDER G //