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Q9Y6C2 (EMIL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
EMILIN-1
Alternative name(s):
Elastin microfibril interface-located protein 1
Short name=Elastin microfibril interfacer 1
Gene names
Name:EMILIN1
Synonyms:EMI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1016 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be responsible for anchoring smooth muscle cells to elastic fibers, and may be involved not only in the formation of the elastic fiber, but also in the processes that regulate vessel assembly. Has cell adhesive capacity.

Subunit structure

Homotrimer associated through a moderately stable interaction of the C-terminal globular C1q domains, allowing the nucleation of the triple helix and then a further quaternary assembly to higher-order polymers via intermolecular disulfide bonds. Interacts with EMILIN2. Ref.10

Subcellular location

Secretedextracellular spaceextracellular matrix. Note: Found mainly at the interface between amorphous elastin and microfibrils.

Tissue specificity

Distributed in tissues where resilience and elastic recoil are prominent. Highest levels in the adult small intestine, aorta, lung, uterus, and appendix and in the fetal spleen, kidney, lung, and heart; intermediate expression was detected in adult liver, ovary, colon, stomach, lymph node and spleen; adult heart, bladder, prostate, adrenal gland, mammary gland, placenta and kidney showed low expression whereas a series of other adult tissues, including skeletal muscle and different regions of adult brain show no expression. Ref.7

Miscellaneous

Its deposition precedes the appearance of elastin and is simultaneous with that of fibrillin 1.

Sequence similarities

Contains 1 C1q domain.

Contains 1 collagen-like domain.

Contains 1 EMI domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 1016995EMILIN-1
PRO_0000007815

Regions

Domain56 – 13176EMI
Domain814 – 86451Collagen-like
Domain866 – 1013148C1q
Coiled coil216 – 25641 Potential
Coiled coil356 – 42065 Potential
Coiled coil576 – 60328 Potential
Coiled coil685 – 75268 Potential
Coiled coil835 – 85723 Potential

Amino acid modifications

Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation4151N-linked (GlcNAc...) Ref.9
Glycosylation4551N-linked (GlcNAc...) Ref.8 Ref.9
Glycosylation5611N-linked (GlcNAc...) Potential
Glycosylation6581N-linked (GlcNAc...) Potential
Glycosylation7661N-linked (GlcNAc...) Ref.9
Glycosylation7941N-linked (GlcNAc...) Ref.9
Disulfide bond60 ↔ 121 By similarity
Disulfide bond85 ↔ 92 By similarity
Disulfide bond120 ↔ 129 By similarity

Natural variations

Natural variant1491Q → R. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6
Corresponds to variant rs2736976 [ dbSNP | Ensembl ].
VAR_046095
Natural variant5361Q → R.
Corresponds to variant rs36069611 [ dbSNP | Ensembl ].
VAR_046096
Natural variant9031E → K.
Corresponds to variant rs36045790 [ dbSNP | Ensembl ].
VAR_046097

Secondary structure

........................ 1016
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y6C2 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: A447F74E17DBCBA8

FASTA1,016106,667
        10         20         30         40         50         60 
MAPRTLWSCY LCCLLTAAAG AASYPPRGFS LYTGSSGALS PGGPQAQIAP RPASRHRNWC 

        70         80         90        100        110        120 
AYVVTRTVSC VLEDGVETYV KYQPCAWGQP QCPQSIMYRR FLRPRYRVAY KTVTDMEWRC 

       130        140        150        160        170        180 
CQGYGGDDCA ESPAPALGPA SSTPRPLAQP ARPNLSGSSA GSPLSGLGGE GPGESEKVQQ 

       190        200        210        220        230        240 
LEEQVQSLTK ELQGLRGVLQ GLSGRLAEDV QRAVETAFNG RQQPADAAAR PGVHETLNEI 

       250        260        270        280        290        300 
QHQLQLLDTR VSTHDQELGH LNNHHGGSSS SGGSRAPAPA SAPPGPSEEL LRQLEQRLQE 

       310        320        330        340        350        360 
SCSVCLAGLD GFRRQQQEDR ERLRAMEKLL ASVEERQRHL AGLAVGRRPP QECCSPELGR 

       370        380        390        400        410        420 
RLAELERRLD VVAGSVTVLS GRRGTELGGA AGQGGHPPGY TSLASRLSRL EDRFNSTLGP 

       430        440        450        460        470        480 
SEEQEESWPG APGGLSHWLP AARGRLEQLG GLLANVSGEL GGRLDLLEEQ VAGAMQACGQ 

       490        500        510        520        530        540 
LCSGAPGEQD SQVSEILSAL ERRVLDSEGQ LRLVGSGLHT VEAAGEARQA TLEGLQEVVG 

       550        560        570        580        590        600 
RLQDRVDAQD ETAAEFTLRL NLTAARLGQL EGLLQAHGDE GCGACGGVQE ELGRLRDGVE 

       610        620        630        640        650        660 
RCSCPLLPPR GPGAGPGVGG PSRGPLDGFS VFGGSSGSAL QALQGELSEV ILSFSSLNDS 

       670        680        690        700        710        720 
LNELQTTVEG QGADLADLGA TKDRIISEIN RLQQEATEHA TESEERFRGL EEGQAQAGQC 

       730        740        750        760        770        780 
PSLEGRLGRL EGVCERLDTV AGGLQGLREG LSRHVAGLWA GLRETNTTSQ MQAALLEKLV 

       790        800        810        820        830        840 
GGQAGLGRRL GALNSSLQLL EDRLHQLSLK DLTGPAGEAG PPGPPGLQGP PGPAGPPGSP 

       850        860        870        880        890        900 
GKDGQEGPIG PPGPQGEQGV EGAPAAPVPQ VAFSAALSLP RSEPGTVPFD RVLLNDGGYY 

       910        920        930        940        950        960 
DPETGVFTAP LAGRYLLSAV LTGHRHEKVE AVLSRSNQGV ARVDSGGYEP EGLENKPVAE 

       970        980        990       1000       1010 
SQPSPGTLGV FSLILPLQAG DTVCVDLVMG QLAHSEEPLT IFSGALLYGD PELEHA 

« Hide

References

« Hide 'large scale' references
[1]"EMILIN, a component of the elastic fiber and a new member of the C1q/tumor necrosis factor superfamily of proteins."
Doliana R., Mongiat M., Bucciotti F., Giacomello E., Deutzmann R., Volpin D., Bressan G.M., Colombatti A.
J. Biol. Chem. 274:16773-16781(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-149.
[2]"Structure, chromosomal localization, and promoter analysis of the human elastin microfibril interface located protein (EMILIN) gene."
Doliana R., Canton A., Bucciotti F., Mongiat M., Bonaldo P., Colombatti A.
J. Biol. Chem. 275:785-792(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-149.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-149.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-149.
Tissue: Brain.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-1016, VARIANT ARG-149.
Tissue: Uterus.
[7]"Isolation and characterization of EMILIN-2, a new component of the growing EMILINs family and a member of the EMI domain-containing superfamily."
Doliana R., Bot S., Mungiguerra G., Canton A., Cilli S.P., Colombatti A.
J. Biol. Chem. 276:12003-12011(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
Lewandrowski U., Moebius J., Walter U., Sickmann A.
Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-455.
Tissue: Platelet.
[9]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415; ASN-455; ASN-766 AND ASN-794.
Tissue: Liver.
[10]"NMR-based homology model for the solution structure of the C-terminal globular domain of EMILIN1."
Verdone G., Corazza A., Colebrooke S.A., Cicero D., Eliseo T., Boyd J., Doliana R., Fogolari F., Viglino P., Colombatti A., Campbell I.D., Esposito G.
J. Biomol. NMR 43:79-96(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 867-1016, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF088916 mRNA. Translation: AAD42161.1.
AF162780 Genomic DNA. Translation: AAF25006.1.
AC013403 Genomic DNA. Translation: AAX93166.1.
CH471053 Genomic DNA. Translation: EAX00645.1.
BC009947 mRNA. Translation: AAH09947.2.
BC136279 mRNA. Translation: AAI36280.1.
BC142688 mRNA. Translation: AAI42689.1.
AL050138 mRNA. Translation: CAB43287.2.
PIRT08772.
RefSeqNP_008977.1. NM_007046.3.
UniGeneHs.63348.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KA3NMR-A/B/C867-1016[»]
2OIINMR-A/B/C867-1016[»]
ProteinModelPortalQ9Y6C2.
SMRQ9Y6C2. Positions 867-1016.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116292. 10 interactions.
DIPDIP-35733N.
IntActQ9Y6C2. 9 interactions.
MINTMINT-133181.
STRING9606.ENSP00000369677.

PTM databases

PhosphoSiteQ9Y6C2.

Polymorphism databases

DMDM205371751.

2D gel databases

REPRODUCTION-2DPAGEQ9Y6C2.

Proteomic databases

PaxDbQ9Y6C2.
PRIDEQ9Y6C2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380320; ENSP00000369677; ENSG00000138080.
GeneID11117.
KEGGhsa:11117.
UCSCuc002rii.4. human.

Organism-specific databases

CTD11117.
GeneCardsGC02P027301.
HGNCHGNC:19880. EMILIN1.
HPAHPA002822.
MIM130660. gene.
neXtProtNX_Q9Y6C2.
PharmGKBPA134922135.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG244192.
HOGENOMHOG000112364.
HOVERGENHBG051473.
InParanoidQ9Y6C2.
OMAQQEATEH.
OrthoDBEOG74R1RX.
PhylomeDBQ9Y6C2.
TreeFamTF331033.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

BgeeQ9Y6C2.
CleanExHS_EMILIN1.
GenevestigatorQ9Y6C2.

Family and domain databases

Gene3D2.60.120.40. 1 hit.
InterProIPR001073. C1q.
IPR008160. Collagen.
IPR011489. EMI_domain.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamPF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
PF07546. EMI. 1 hit.
[Graphical view]
SUPFAMSSF49842. SSF49842. 1 hit.
PROSITEPS50871. C1Q. 1 hit.
PS51041. EMI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEMILIN1. human.
EvolutionaryTraceQ9Y6C2.
GeneWikiEMILIN1.
GenomeRNAi11117.
NextBio42252.
PROQ9Y6C2.
SOURCESearch...

Entry information

Entry nameEMIL1_HUMAN
AccessionPrimary (citable) accession number: Q9Y6C2
Secondary accession number(s): A5PL03 expand/collapse secondary AC list , Q53SY9, Q96G58, Q9UG76
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM