Q9Y6C2 (EMIL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
EMILIN-1

Alternative name(s):
Elastin microfibril interface-located protein 1
Short name=Elastin microfibril interfacer 1

Gene names

Name:	EMILIN1
Synonyms:	EMI

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1016 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular 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.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Coiled coil Collagen Signal
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Traceable author statement Ref.1. Source: ProtInc extracellular matrix organization Inferred from electronic annotation. Source: Compara positive regulation of cell-substrate adhesion Inferred from electronic annotation. Source: Compara
Cellular_component	collagen Inferred from electronic annotation. Source: UniProtKB-KW extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB
Molecular_function	extracellular matrix constituent conferring elasticity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 1016

995

EMILIN-1

PRO_0000007815

Regions

Domain

56 – 131

76

EMI

Domain

814 – 864

51

Collagen-like

Domain

866 – 1013

148

C1q

Coiled coil

216 – 256

41

Potential

Coiled coil

356 – 420

65

Potential

Coiled coil

576 – 603

28

Potential

Coiled coil

685 – 752

68

Potential

Coiled coil

835 – 857

23

Potential

Amino acid modifications

Glycosylation

154

1

N-linked (GlcNAc...) Potential

Glycosylation

415

1

N-linked (GlcNAc...) Ref.9

Glycosylation

455

1

N-linked (GlcNAc...) Ref.8 Ref.9

Glycosylation

561

1

N-linked (GlcNAc...) Potential

Glycosylation

658

1

N-linked (GlcNAc...) Potential

Glycosylation

766

1

N-linked (GlcNAc...) Ref.9

Glycosylation

794

1

N-linked (GlcNAc...) Ref.9

Disulfide bond

60 ↔ 121

By similarity

Disulfide bond

85 ↔ 92

By similarity

Disulfide bond

120 ↔ 129

By similarity

Natural variations

Natural variant

149

1

Q → R. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6
Corresponds to variant rs2736976 [ dbSNP | Ensembl ].

VAR_046095

Natural variant

536

1

Q → R.
Corresponds to variant rs36069611 [ dbSNP | Ensembl ].

VAR_046096

Natural variant

903

1

E → K.
Corresponds to variant rs36045790 [ dbSNP | Ensembl ].

VAR_046097

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1016

Helix Strand Turn

Details...

Beta strand

872 – 876

5

Beta strand

884 – 886

3

Beta strand

891 – 897

7

Turn

902 – 905

4

Beta strand

906 – 908

3

Beta strand

913 – 919

7

Beta strand

929 – 933

5

Turn

935 – 937

3

Beta strand

942 – 946

5

Beta strand

972 – 974

3

Beta strand

982 – 986

5

Beta strand

1002 – 1009

8

Sequences

	Sequence		Length	Mass (Da)
	Q9Y6C2 [UniParc]. Last modified September 2, 2008. Version 2. Checksum: A447F74E17DBCBA8	FASTA	1,016	106,667
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.

IPI

IPI00013079.

PIR

T08772.

RefSeq

NP_008977.1. NM_007046.3.

UniGene

Hs.63348.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KA3	NMR	-	A/B/C	867-1016	[»]
2OII	NMR	-	A/B/C	867-1016	[»]

ProteinModelPortal

Q9Y6C2.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35733N.

IntAct

Q9Y6C2. 6 interactions.

MINT

MINT-133181.

STRING

9606.ENSP00000369677.

PTM databases

PhosphoSite

Q9Y6C2.

Polymorphism databases

DMDM

205371751.

2D gel databases

REPRODUCTION-2DPAGE

Q9Y6C2.

Proteomic databases

PaxDb

Q9Y6C2.

PRIDE

Q9Y6C2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000380320; ENSP00000369677; ENSG00000138080.

GeneID

11117.

KEGG

hsa:11117.

UCSC

uc002rii.4. human.

Organism-specific databases

CTD

11117.

GeneCards

GC02P027301.

HGNC

HGNC:19880. EMILIN1.

HPA

HPA002822.

MIM

130660. gene.

neXtProt

NX_Q9Y6C2.

PharmGKB

PA134922135.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG244192.

HOGENOM

HOG000112364.

HOVERGEN

HBG051473.

InParanoid

Q9Y6C2.

OMA

NDGGYYD.

OrthoDB

EOG4S7JPW.

PhylomeDB

Q9Y6C2.

Enzyme and pathway databases

Reactome

REACT_118779. Extracellular matrix organization.

Gene expression databases

Bgee

Q9Y6C2.

CleanEx

HS_EMILIN1.

Genevestigator

Q9Y6C2.

GermOnline

ENSG00000138080. Homo sapiens.

Family and domain databases

Gene3D

2.60.120.40. 1 hit.

InterPro

IPR001073. C1q.
IPR008160. Collagen.
IPR011489. EMI_domain.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]

Pfam

PF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
PF07546. EMI. 1 hit.
[Graphical view]

SUPFAM

SSF49842. TNF_like. 1 hit.

PROSITE

PS50871. C1Q. 1 hit.
PS51041. EMI. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

EMILIN1. human.

EvolutionaryTrace

Q9Y6C2.

GenomeRNAi

11117.

NextBio

42252.

SOURCE

Search...

Entry information

Entry name

EMIL1_HUMAN

Accession

Primary (citable) accession number: Q9Y6C2
Secondary accession number(s): A5PL03 , Q53SY9, Q96G58, Q9UG76

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	September 2, 2008
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.