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Q99K41

- EMIL1_MOUSE

UniProt

Q99K41 - EMIL1_MOUSE

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Protein
EMILIN-1
Gene
Emilin1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

GO - Molecular functioni

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

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_198998. 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: 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 region Source: Reactome
  3. extracellular vesicular exosome Source: Ensembl
  4. 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 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 1017994EMILIN-1
PRO_0000007816Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

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.

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 13378EMI
Add
BLAST
Domaini815 – 86551Collagen-like
Add
BLAST
Domaini867 – 1014148C1q
Add
BLAST

Coiled coil

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

Compositional bias

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

Sequence similaritiesi

Contains 1 C1q domain.
Contains 1 EMI domain.

Keywords - Domaini

Coiled coil, Collagen, Signal

Phylogenomic databases

eggNOGiNOG244192.
GeneTreeiENSGT00660000095314.
HOGENOMiHOG000112364.
HOVERGENiHBG051473.
InParanoidiQ99K41.
OMAiQQEATEH.
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

MAPRALWSCY LCCLLTIATE AASYPPRGYS LYTGGTGALS PGGPQAQNSP     50
RPASRHRNWC AYVVTRTVSC VLEDGVETIV KPDYQPCGWG QPHCSRSIMY 100
RSFLRPRYRV AYKTVTDMEW RCCQGYGGDD CGEGPASVLG PAPSTPLPRP 150
RPVRPNLSGS SAGSHLSGLG GEGPVESEKV QQLERQVKSL TKELQGLRGV 200
LQGMNGRLAE DVQRAVDTVF NGRQQPADAA ARPGVHETLS EIQQQLQLLD 250
NRVSTHDQEL GHLNNHHNGG PGGGGRASGP VPVPSGPSEE LLRQLERQLQ 300
ESCSVCLTGL DGFRQQQQED RERLRTLEKL MSSMEERQQQ LVGPAMARRP 350
PQECCPPELG RRVSELERRL DVVTGSLTVL SGRRGSELGG AAGQGGHPPG 400
YTSLASRLSR LEDRFNSTLG PSEEQEKNWP GGPGRLGHWL PAAPGRLEKL 450
EGLLANVSRE LGGRMDLLEE QVAGAVRTCG QICSGAPGEQ DSRVNEILSA 500
LERRVLDSEG RLQLVGSGLH EAEAAGEAQQ AVLEGLQGLL SRLRERMDAQ 550
EETAAEILLR LNLTAAQLSQ LEGLLQARGD EGCGACGGVQ EELGRLRDGV 600
ERCSCPLLPP RGPGAGPGVG GPSRGPLDGF SVFGGSSGSA LQALQGELSE 650
VILTFSSLND SLHELQTTVE GQGADLADLG ATKDSIISEI NRLQQEATEH 700
VTESEERFRG LEEGQAQAGQ CPSLEGRLGR LEGVCERLDT VAGGLQGLRE 750
GLSRHVAGLW AAVRESNSTS LTQAALLEKL LGGQAGLGRR LGALNNSLLL 800
LEDRLQQLSL KDFTGPSGKA GPPGPPGLQG PSGPAGPPGP PGKDGQQGAI 850
GPPGPQGEQG AEGAPAAPVP RVAFSAALSL PRSEPGTVPF DRVLLNDGGY 900
YDPETGVFTA PLAGRYLLSA VLTGHRHEKV EAVLSRSNLG VARIDSGGYE 950
PEGLENKPVA ESQPSPGALG VFSLILPLQV GDTVCIDLVM GQLAHSEEPL 1000
TIFSGALLYE DTELEQV 1017
Length:1,017
Mass (Da):107,585
Last modified:June 1, 2001 - v1
Checksum:i2EF903204DB9C88F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK029337 mRNA. Translation: BAC26403.1 .
BC005481 mRNA. Translation: AAH05481.1 .
CCDSi CCDS19167.1.
RefSeqi NP_598679.1. NM_133918.2.
UniGenei Mm.286375.

3D structure databases

ProteinModelPortali Q99K41.
SMRi Q99K41. Positions 868-1016.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 221560. 1 interaction.
IntActi Q99K41. 5 interactions.
MINTi MINT-4094392.

PTM databases

PhosphoSitei Q99K41.

Proteomic databases

PaxDbi Q99K41.
PRIDEi Q99K41.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031055 ; ENSMUSP00000031055 ; ENSMUSG00000029163 .
GeneIDi 100952.
KEGGi mmu:100952.
UCSCi uc008wwm.1. mouse.

Organism-specific databases

CTDi 11117.
MGIi MGI:1926189. Emilin1.

Phylogenomic databases

eggNOGi NOG244192.
GeneTreei ENSGT00660000095314.
HOGENOMi HOG000112364.
HOVERGENi HBG051473.
InParanoidi Q99K41.
OMAi QQEATEH.
OrthoDBi EOG74R1RX.
PhylomeDBi Q99K41.
TreeFami TF331033.

Enzyme and pathway databases

Reactomei REACT_198998. Molecules associated with elastic fibres.

Miscellaneous databases

NextBioi 354704.
PROi Q99K41.
SOURCEi Search...

Gene expression databases

Bgeei Q99K41.
CleanExi MM_EMILIN1.
Genevestigatori Q99K41.

Family and domain databases

Gene3Di 2.60.120.40. 1 hit.
InterProi IPR001073. C1q.
IPR008160. Collagen.
IPR011489. EMI_domain.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view ]
Pfami PF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
PF07546. EMI. 1 hit.
[Graphical view ]
SUPFAMi SSF49842. SSF49842. 1 hit.
PROSITEi PS50871. C1Q. 1 hit.
PS51041. EMI. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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. 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: September 3, 2014
This is version 108 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

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