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Protein

EMILIN-1

Gene

Emilin1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

GO - Molecular functioni

  1. extracellular matrix constituent conferring elasticity Source: MGI
  2. identical protein binding Source: MGI

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. extracellular matrix organization Source: MGI
  3. positive regulation of cell-substrate adhesion Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_332220. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
EMILIN-1
Alternative name(s):
Elastin microfibril interface-located protein 1
Short name:
Elastin microfibril interfacer 1
Gene namesi
Name:Emilin1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1926189. Emilin1.

Subcellular locationi

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

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. extracellular matrix Source: UniProtKB
  3. extracellular region Source: Reactome
  4. extracellular vesicular exosome Source: MGI
  5. proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 1017994EMILIN-1PRO_0000007816Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi60 ↔ 123PROSITE-ProRule annotation
Disulfide bondi87 ↔ 94PROSITE-ProRule annotation
Disulfide bondi122 ↔ 131PROSITE-ProRule annotation
Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi456 – 4561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi562 – 5621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi659 – 6591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi767 – 7671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi795 – 7951N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ99K41.
PaxDbiQ99K41.
PRIDEiQ99K41.

PTM databases

PhosphoSiteiQ99K41.

Expressioni

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ99K41.
CleanExiMM_EMILIN1.
GenevestigatoriQ99K41.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
TGFB1P072002EBI-906561,EBI-907660From a different organism.

Protein-protein interaction databases

BioGridi221560. 1 interaction.
IntActiQ99K41. 5 interactions.
MINTiMINT-4094392.

Structurei

3D structure databases

ProteinModelPortaliQ99K41.
SMRiQ99K41. Positions 868-1016.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 13378EMIPROSITE-ProRule annotationAdd
BLAST
Domaini815 – 86551Collagen-likeAdd
BLAST
Domaini867 – 1014148C1qPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili171 – 21141Sequence AnalysisAdd
BLAST
Coiled coili237 – 26630Sequence AnalysisAdd
BLAST
Coiled coili310 – 37465Sequence AnalysisAdd
BLAST
Coiled coili519 – 57355Sequence AnalysisAdd
BLAST
Coiled coili676 – 69722Sequence AnalysisAdd
BLAST
Coiled coili789 – 80921Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi269 – 2757Poly-Gly

Sequence similaritiesi

Contains 1 C1q domain.PROSITE-ProRule annotation
Contains 1 collagen-like domain.Curated
Contains 1 EMI domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Collagen, Signal

Phylogenomic databases

eggNOGiNOG244192.
GeneTreeiENSGT00660000095314.
HOGENOMiHOG000112364.
HOVERGENiHBG051473.
InParanoidiQ99K41.
OMAiLEGVCER.
OrthoDBiEOG74R1RX.
PhylomeDBiQ99K41.
TreeFamiTF331033.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q.
IPR008160. Collagen.
IPR011489. EMI_domain.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
PF07546. EMI. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
PS51041. EMI. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99K41-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPRALWSCY LCCLLTIATE AASYPPRGYS LYTGGTGALS PGGPQAQNSP
60 70 80 90 100
RPASRHRNWC AYVVTRTVSC VLEDGVETIV KPDYQPCGWG QPHCSRSIMY
110 120 130 140 150
RSFLRPRYRV AYKTVTDMEW RCCQGYGGDD CGEGPASVLG PAPSTPLPRP
160 170 180 190 200
RPVRPNLSGS SAGSHLSGLG GEGPVESEKV QQLERQVKSL TKELQGLRGV
210 220 230 240 250
LQGMNGRLAE DVQRAVDTVF NGRQQPADAA ARPGVHETLS EIQQQLQLLD
260 270 280 290 300
NRVSTHDQEL GHLNNHHNGG PGGGGRASGP VPVPSGPSEE LLRQLERQLQ
310 320 330 340 350
ESCSVCLTGL DGFRQQQQED RERLRTLEKL MSSMEERQQQ LVGPAMARRP
360 370 380 390 400
PQECCPPELG RRVSELERRL DVVTGSLTVL SGRRGSELGG AAGQGGHPPG
410 420 430 440 450
YTSLASRLSR LEDRFNSTLG PSEEQEKNWP GGPGRLGHWL PAAPGRLEKL
460 470 480 490 500
EGLLANVSRE LGGRMDLLEE QVAGAVRTCG QICSGAPGEQ DSRVNEILSA
510 520 530 540 550
LERRVLDSEG RLQLVGSGLH EAEAAGEAQQ AVLEGLQGLL SRLRERMDAQ
560 570 580 590 600
EETAAEILLR LNLTAAQLSQ LEGLLQARGD EGCGACGGVQ EELGRLRDGV
610 620 630 640 650
ERCSCPLLPP RGPGAGPGVG GPSRGPLDGF SVFGGSSGSA LQALQGELSE
660 670 680 690 700
VILTFSSLND SLHELQTTVE GQGADLADLG ATKDSIISEI NRLQQEATEH
710 720 730 740 750
VTESEERFRG LEEGQAQAGQ CPSLEGRLGR LEGVCERLDT VAGGLQGLRE
760 770 780 790 800
GLSRHVAGLW AAVRESNSTS LTQAALLEKL LGGQAGLGRR LGALNNSLLL
810 820 830 840 850
LEDRLQQLSL KDFTGPSGKA GPPGPPGLQG PSGPAGPPGP PGKDGQQGAI
860 870 880 890 900
GPPGPQGEQG AEGAPAAPVP RVAFSAALSL PRSEPGTVPF DRVLLNDGGY
910 920 930 940 950
YDPETGVFTA PLAGRYLLSA VLTGHRHEKV EAVLSRSNLG VARIDSGGYE
960 970 980 990 1000
PEGLENKPVA ESQPSPGALG VFSLILPLQV GDTVCIDLVM GQLAHSEEPL
1010
TIFSGALLYE DTELEQV
Length:1,017
Mass (Da):107,585
Last modified:June 1, 2001 - v1
Checksum:i2EF903204DB9C88F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029337 mRNA. Translation: BAC26403.1.
BC005481 mRNA. Translation: AAH05481.1.
CCDSiCCDS19167.1.
RefSeqiNP_598679.1. NM_133918.2.
UniGeneiMm.286375.

Genome annotation databases

EnsembliENSMUST00000031055; ENSMUSP00000031055; ENSMUSG00000029163.
GeneIDi100952.
KEGGimmu:100952.
UCSCiuc008wwm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029337 mRNA. Translation: BAC26403.1.
BC005481 mRNA. Translation: AAH05481.1.
CCDSiCCDS19167.1.
RefSeqiNP_598679.1. NM_133918.2.
UniGeneiMm.286375.

3D structure databases

ProteinModelPortaliQ99K41.
SMRiQ99K41. Positions 868-1016.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221560. 1 interaction.
IntActiQ99K41. 5 interactions.
MINTiMINT-4094392.

PTM databases

PhosphoSiteiQ99K41.

Proteomic databases

MaxQBiQ99K41.
PaxDbiQ99K41.
PRIDEiQ99K41.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031055; ENSMUSP00000031055; ENSMUSG00000029163.
GeneIDi100952.
KEGGimmu:100952.
UCSCiuc008wwm.1. mouse.

Organism-specific databases

CTDi11117.
MGIiMGI:1926189. Emilin1.

Phylogenomic databases

eggNOGiNOG244192.
GeneTreeiENSGT00660000095314.
HOGENOMiHOG000112364.
HOVERGENiHBG051473.
InParanoidiQ99K41.
OMAiLEGVCER.
OrthoDBiEOG74R1RX.
PhylomeDBiQ99K41.
TreeFamiTF331033.

Enzyme and pathway databases

ReactomeiREACT_332220. Molecules associated with elastic fibres.

Miscellaneous databases

NextBioi354704.
PROiQ99K41.
SOURCEiSearch...

Gene expression databases

BgeeiQ99K41.
CleanExiMM_EMILIN1.
GenevestigatoriQ99K41.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q.
IPR008160. Collagen.
IPR011489. EMI_domain.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
PF07546. EMI. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
PS51041. EMI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  3. Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiEMIL1_MOUSE
AccessioniPrimary (citable) accession number: Q99K41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: June 1, 2001
Last modified: April 1, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.