ID   EMIL3_HUMAN             Reviewed;         766 AA.
AC   Q9NT22; Q495S5; Q495S6; Q495S7; Q76KT4;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-NOV-2004, sequence version 2.
DT   23-FEB-2022, entry version 142.
DE   RecName: Full=EMILIN-3;
DE   AltName: Full=EMILIN-5;
DE   AltName: Full=Elastin microfibril interface-located protein 3;
DE            Short=Elastin microfibril interfacer 3;
DE   AltName: Full=Elastin microfibril interface-located protein 5;
DE            Short=Elastin microfibril interfacer 5;
DE   Flags: Precursor;
GN   Name=EMILIN3; Synonyms=C20orf130, EMILIN5;
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).
RC   TISSUE=Mesenchymal stem cell;
RX   PubMed=14706625; DOI=10.1016/j.bbrc.2003.11.181;
RA   Doi M., Nagano A., Nakamura Y.;
RT   "Molecular cloning and characterization of a novel gene, EMILIN-5, and its
RT   possible involvement in skeletal development.";
RL   Biochem. Biophys. Res. Commun. 313:888-893(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   ASN-532.
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 304-766 (ISOFORM 1).
RC   TISSUE=Testis;
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).
CC   -!- INTERACTION:
CC       Q9NT22; O75934: BCAS2; NbExp=3; IntAct=EBI-3197883, EBI-1050106;
CC       Q9NT22; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-3197883, EBI-10961624;
CC       Q9NT22; Q9NT22: EMILIN3; NbExp=3; IntAct=EBI-3197883, EBI-3197883;
CC       Q9NT22; Q9NVF7: FBXO28; NbExp=6; IntAct=EBI-3197883, EBI-740282;
CC       Q9NT22; Q9H8Y8: GORASP2; NbExp=5; IntAct=EBI-3197883, EBI-739467;
CC       Q9NT22; Q9Y316: MEMO1; NbExp=3; IntAct=EBI-3197883, EBI-1104564;
CC       Q9NT22; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-3197883, EBI-741158;
CC       Q9NT22; O00560: SDCBP; NbExp=3; IntAct=EBI-3197883, EBI-727004;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NT22-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NT22-2; Sequence=VSP_055481;
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DR   EMBL; AB089149; BAD11034.1; -; mRNA.
DR   EMBL; AL031667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC101043; AAI01044.1; -; mRNA.
DR   EMBL; BC101044; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC101045; AAI01046.1; -; mRNA.
DR   EMBL; BC101046; AAI01047.1; -; mRNA.
DR   EMBL; AL137580; CAB70822.1; -; mRNA.
DR   CCDS; CCDS13316.1; -. [Q9NT22-1]
DR   PIR; T46290; T46290.
DR   RefSeq; NP_443078.1; NM_052846.1. [Q9NT22-1]
DR   BioGRID; 124673; 54.
DR   IntAct; Q9NT22; 15.
DR   STRING; 9606.ENSP00000332806; -.
DR   GlyGen; Q9NT22; 6 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NT22; -.
DR   PhosphoSitePlus; Q9NT22; -.
DR   BioMuta; EMILIN3; -.
DR   DMDM; 55584183; -.
DR   EPD; Q9NT22; -.
DR   MassIVE; Q9NT22; -.
DR   PaxDb; Q9NT22; -.
DR   PeptideAtlas; Q9NT22; -.
DR   PRIDE; Q9NT22; -.
DR   ProteomicsDB; 82600; -. [Q9NT22-1]
DR   Antibodypedia; 57328; 82 antibodies from 18 providers.
DR   DNASU; 90187; -.
DR   Ensembl; ENST00000332312; ENSP00000332806; ENSG00000183798.
DR   GeneID; 90187; -.
DR   KEGG; hsa:90187; -.
DR   MANE-Select; ENST00000332312.4; ENSP00000332806.3; NM_052846.2; NP_443078.1.
DR   UCSC; uc002xjy.2; human. [Q9NT22-1]
DR   CTD; 90187; -.
DR   DisGeNET; 90187; -.
DR   GeneCards; EMILIN3; -.
DR   HGNC; HGNC:16123; EMILIN3.
DR   HPA; ENSG00000183798; Tissue enriched (epididymis).
DR   MIM; 608929; gene.
DR   neXtProt; NX_Q9NT22; -.
DR   OpenTargets; ENSG00000183798; -.
DR   PharmGKB; PA164741521; -.
DR   VEuPathDB; HostDB:ENSG00000183798; -.
DR   eggNOG; ENOG502QV8J; Eukaryota.
DR   GeneTree; ENSGT01030000234633; -.
DR   HOGENOM; CLU_011705_1_0_1; -.
DR   InParanoid; Q9NT22; -.
DR   OMA; FMTIVGE; -.
DR   OrthoDB; 1205089at2759; -.
DR   PhylomeDB; Q9NT22; -.
DR   TreeFam; TF331033; -.
DR   PathwayCommons; Q9NT22; -.
DR   Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR   SignaLink; Q9NT22; -.
DR   BioGRID-ORCS; 90187; 9 hits in 1028 CRISPR screens.
DR   GenomeRNAi; 90187; -.
DR   Pharos; Q9NT22; Tbio.
DR   PRO; PR:Q9NT22; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9NT22; protein.
DR   Bgee; ENSG00000183798; Expressed in caput epididymis and 168 other tissues.
DR   Genevisible; Q9NT22; HS.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0030023; F:extracellular matrix constituent conferring elasticity; ISS:BHF-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   InterPro; IPR011489; EMI_domain.
DR   Pfam; PF07546; EMI; 1.
DR   PROSITE; PS51041; EMI; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..766
FT                   /note="EMILIN-3"
FT                   /id="PRO_0000007819"
FT   DOMAIN          55..131
FT                   /note="EMI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT   REGION          132..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          467..491
FT                   /evidence="ECO:0000255"
FT   COILED          615..663
FT                   /evidence="ECO:0000255"
FT   COILED          726..761
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        151..165
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        562
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        616
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        732
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        59..121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT   DISULFID        86..92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT   DISULFID        120..129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT   VAR_SEQ         1..394
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055481"
FT   VARIANT         532
FT                   /note="S -> N (in dbSNP:rs2235592)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_053075"
SQ   SEQUENCE   766 AA;  82647 MW;  72B9BFC6DCD15DC5 CRC64;
     MGRRRLLVWL CAVAALLSGA QARGTPLLAR PAPPGASRYS LYTTGWRPRL RPGPHKALCA
     YVVHRNVTCI LQEGAESYVK AEYRQCRWGP KCPGTVTYRT VLRPKYKVGY KTVTDLAWRC
     CPGFTGKRCP EHLTDHGAAS PQLEPEPQIP SGQLDPGPRP PSYSRAAPSP HGRKGPGLFG
     ERLERLEGDV QRLAQTYGTL SGLVASHEDP NRMTGGPRAP AVPVGFGVIP EGLVGPGDRA
     RGPLTPPLDE ILSKVTEVSN TLQTKVQLLD KVHGLALGHE AHLQRLREAP PSPLTSLALL
     EEYVDRRLHR LWGSLLDGFE QKLQGVQSEC DLRVQEVRRQ CEEGQAASRR LHQSLDGREL
     ALRQELSQLG SQLQGLSVSG RGSCCGQLAL INARMDGLER ALQAVTETQR GPGAPAGDEL
     TRLSAAMLEG GVDGLLEGLE TLNGTEGGAR GCCLRLDMGG WGVGGFGTML EERVQSLEER
     LATLAGELSH DSASPGRSAR PLVQTELAVL EQRLVSLETS CTPSTTSAIL DSLVAEVKAW
     QSRSEALLRQ VASHAALLQQ LNGTVAEVQG QLAEGTGSSL QGEITLLKVN LNSVSKSLTG
     LSDSVSQYSD AFLAANTSLD ERERKVEAEV QAIQEQVSSQ GSRLQAGHRQ VLNLRGELEQ
     LKAGVAKVAS GLSRCQDTAQ KLQHTVGHFD QRVAQVEGAC RRLGLLAAGL DSLPTEPLRP
     REGLWSHVDQ LNRTLAQHTQ DIARLRDDLL DCQAQLAEQV RPGQAN
//