Q99K41 (EMIL1_MOUSE) 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1017 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 By similarity. May have a function in placenta formation and initial organogenesis and a later role in interstitial connective tissue.
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 By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix. Note: Found mainly at the interface between amorphous elastin and microfibrils.
Developmental stage	Detectable in morula and blastocyst. First expressed in ectoplacental cone in embryos of 6.5 days and in extraembryonic visceral endoderm at 7.5 days. Expressed also in the allantois. Expression in the ectoplacental cone-derived secondary trophoblast giant cells and spongiotrophoblast is strong up to 11.5 days and then declines. In the embryo, high levels are initially expressed in blood vessels, perineural mesenchyme and somites at 8.5 days. Later on, intense expression is identified in the mesenchymal component of organs anlage (ie lung and liver) and different mesenchymal condensations (ie limb bud and branchial arches). At late gestation expression is widely distributed in interstitial connective tissue and smooth muscle cell-rich tissues. Ref.3
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
Domain	Coiled coil Collagen Signal
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW extracellular matrix organization Inferred from direct assay PubMed 18757743. Source: MGI positive regulation of cell-substrate adhesion Inferred from direct assay PubMed 18757743. Source: MGI
Cellular_component	collagen Inferred from electronic annotation. Source: UniProtKB-KW proteinaceous extracellular matrix Inferred from direct assay PubMed 14701737. Source: MGI
Molecular_function	extracellular matrix constituent conferring elasticity Inferred from mutant phenotype PubMed 14701737. Source: MGI identical protein binding Inferred from direct assay PubMed 14701737. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TGFB1	P07200	2	EBI-906561,EBI-907660	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 1017	994	EMILIN-1		PRO_0000007816
Regions
	Domain	56 – 133	78	EMI
	Domain	815 – 865	51	Collagen-like
	Domain	867 – 1014	148	C1q
	Coiled coil	171 – 211	41	Potential
	Coiled coil	237 – 266	30	Potential
	Coiled coil	310 – 374	65	Potential
	Coiled coil	519 – 573	55	Potential
	Coiled coil	676 – 697	22	Potential
	Coiled coil	789 – 809	21	Potential
	Compositional bias	269 – 275	7	Poly-Gly
Amino acid modifications
	Glycosylation	156	1	N-linked (GlcNAc...) Potential
	Glycosylation	416	1	N-linked (GlcNAc...) Potential
	Glycosylation	456	1	N-linked (GlcNAc...) Potential
	Glycosylation	562	1	N-linked (GlcNAc...) Potential
	Glycosylation	659	1	N-linked (GlcNAc...) Potential
	Glycosylation	767	1	N-linked (GlcNAc...) Potential
	Glycosylation	795	1	N-linked (GlcNAc...) Potential
	Disulfide bond	60 ↔ 123		By similarity
	Disulfide bond	87 ↔ 94		By similarity
	Disulfide bond	122 ↔ 131		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q99K41 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 2EF903204DB9C88F	FASTA	1,017	107,585
	10 20 30 40 50 60 MAPRALWSCY LCCLLTIATE AASYPPRGYS LYTGGTGALS PGGPQAQNSP RPASRHRNWC 70 80 90 100 110 120 AYVVTRTVSC VLEDGVETIV KPDYQPCGWG QPHCSRSIMY RSFLRPRYRV AYKTVTDMEW 130 140 150 160 170 180 RCCQGYGGDD CGEGPASVLG PAPSTPLPRP RPVRPNLSGS SAGSHLSGLG GEGPVESEKV 190 200 210 220 230 240 QQLERQVKSL TKELQGLRGV LQGMNGRLAE DVQRAVDTVF NGRQQPADAA ARPGVHETLS 250 260 270 280 290 300 EIQQQLQLLD NRVSTHDQEL GHLNNHHNGG PGGGGRASGP VPVPSGPSEE LLRQLERQLQ 310 320 330 340 350 360 ESCSVCLTGL DGFRQQQQED RERLRTLEKL MSSMEERQQQ LVGPAMARRP PQECCPPELG 370 380 390 400 410 420 RRVSELERRL DVVTGSLTVL SGRRGSELGG AAGQGGHPPG YTSLASRLSR LEDRFNSTLG 430 440 450 460 470 480 PSEEQEKNWP GGPGRLGHWL PAAPGRLEKL EGLLANVSRE LGGRMDLLEE QVAGAVRTCG 490 500 510 520 530 540 QICSGAPGEQ DSRVNEILSA LERRVLDSEG RLQLVGSGLH EAEAAGEAQQ AVLEGLQGLL 550 560 570 580 590 600 SRLRERMDAQ EETAAEILLR LNLTAAQLSQ LEGLLQARGD EGCGACGGVQ EELGRLRDGV 610 620 630 640 650 660 ERCSCPLLPP RGPGAGPGVG GPSRGPLDGF SVFGGSSGSA LQALQGELSE VILTFSSLND 670 680 690 700 710 720 SLHELQTTVE GQGADLADLG ATKDSIISEI NRLQQEATEH VTESEERFRG LEEGQAQAGQ 730 740 750 760 770 780 CPSLEGRLGR LEGVCERLDT VAGGLQGLRE GLSRHVAGLW AAVRESNSTS LTQAALLEKL 790 800 810 820 830 840 LGGQAGLGRR LGALNNSLLL LEDRLQQLSL KDFTGPSGKA GPPGPPGLQG PSGPAGPPGP 850 860 870 880 890 900 PGKDGQQGAI GPPGPQGEQG AEGAPAAPVP RVAFSAALSL PRSEPGTVPF DRVLLNDGGY 910 920 930 940 950 960 YDPETGVFTA PLAGRYLLSA VLTGHRHEKV EAVLSRSNLG VARIDSGGYE PEGLENKPVA 970 980 990 1000 1010 ESQPSPGALG VFSLILPLQV GDTVCIDLVM GQLAHSEEPL TIFSGALLYE DTELEQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Head.
[2]	"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]. Tissue: Mammary tumor.
[3]	"Expression of the EMILIN-1 gene during mouse development." Braghetta P., Ferrari A., de Gemmis P., Zanetti M., Volpin D., Bonaldo P., Bressan G.M. Matrix Biol. 21:603-609(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK029337 mRNA. Translation: BAC26403.1. BC005481 mRNA. Translation: AAH05481.1.
IPI	IPI00115516.
RefSeq	NP_598679.1. NM_133918.2.
UniGene	Mm.286375.
3D structure databases
ProteinModelPortal	Q99K41.
SMR	Q99K41. Positions 868-1016.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99K41. 3 interactions.
PTM databases
PhosphoSite	Q99K41.
Proteomic databases
PaxDb	Q99K41.
PRIDE	Q99K41.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031055; ENSMUSP00000031055; ENSMUSG00000029163.
GeneID	100952.
KEGG	mmu:100952.
UCSC	uc008wwm.1. mouse.
Organism-specific databases
CTD	11117.
MGI	MGI:1926189. Emilin1.
Phylogenomic databases
eggNOG	NOG244192.
GeneTree	ENSGT00660000095314.
HOGENOM	HOG000112364.
HOVERGEN	HBG051473.
InParanoid	Q99K41.
OMA	NDGGYYD.
OrthoDB	EOG4S7JPW.
Gene expression databases
Bgee	Q99K41.
CleanEx	MM_EMILIN1.
Genevestigator	Q99K41.
GermOnline	ENSMUSG00000029163. Mus musculus.
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
NextBio	354704.
SOURCE	Search...

Entry information

Entry name

EMIL1_MOUSE

Accession

Primary (citable) accession number: Q99K41

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program