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   18-JUN-2025, entry version 160.
DE   RecName: Full=EMI domain-containing protein 1;
DE   AltName: Full=Emilin and multimerin domain-containing protein 1 {ECO:0000303|PubMed:12221002};
DE            Short=Emu1 {ECO:0000303|PubMed:12221002};
DE   Flags: Precursor;
GN   Name=EMID1; Synonyms=EMU1 {ECO:0000303|PubMed:12221002};
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).
RN   [6]
RP   GLYCOSYLATION AT THR-42.
RX   PubMed=39775168; DOI=10.1038/s41589-024-01815-x;
RA   Hao H., Yuan Y., Ito A., Eberand B.M., Tjondro H., Cielesh M., Norris N.,
RA   Moreno C.L., Maxwell J.W.C., Neely G.G., Payne R.J., Kebede M.A.,
RA   Urbauer R.J.B., Passam F.H., Larance M., Haltiwanger R.S.;
RT   "FUT10 and FUT11 are protein O-fucosyltransferases that modify protein EMI
RT   domains.";
RL   Nat. Chem. Biol. 0:0-0(2025).
CC   -!- SUBUNIT: Homo- or heteromers.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:Q91VF5}.
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   -!- PTM: O-fucosylated at Thr-42 within the EMI domain by FUT10/POFUT3 and
CC       FUT11/POFUT4. {ECO:0000269|PubMed:39775168}.
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}.
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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_001267895.2. [Q96A84-1]
DR   RefSeq; NP_597712.2; NM_133455.4. [Q96A84-3]
DR   AlphaFoldDB; Q96A84; -.
DR   BioGRID; 126183; 38.
DR   FunCoup; Q96A84; 9.
DR   IntAct; Q96A84; 29.
DR   STRING; 9606.ENSP00000335481; -.
DR   GlyCosmos; Q96A84; 2 sites, No reported glycans.
DR   GlyGen; Q96A84; 9 sites, 2 N-linked glycans (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; FVEPRWS; -.
DR   OrthoDB; 9837521at2759; -.
DR   PAN-GO; Q96A84; 0 GO annotations based on evolutionary models.
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        163..184
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..231
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..243
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..264
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..311
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        42
FT                   /note="O-linked (Fuc) threonine"
FT                   /evidence="ECO:0000269|PubMed:39775168"
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
//