EMIL3_HUMAN
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 03-AUG-2022, entry version 144.
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 AlphaFoldDB; Q9NT22; -.
DR BioGRID; 124673; 65.
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; 79 antibodies from 17 providers.
DR DNASU; 90187; -.
DR Ensembl; ENST00000332312.4; ENSP00000332806.3; ENSG00000183798.5. [Q9NT22-1]
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; 12 hits in 1057 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 corpus epididymis and 123 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
