EMIL1_MOUSE
ID EMIL1_MOUSE Reviewed; 1017 AA.
AC Q99K41;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=EMILIN-1;
DE AltName: Full=Elastin microfibril interface-located protein 1;
DE Short=Elastin microfibril interfacer 1;
DE Flags: Precursor;
GN Name=Emilin1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=12475644; DOI=10.1016/s0945-053x(02)00072-0;
RA Braghetta P., Ferrari A., de Gemmis P., Zanetti M., Volpin D., Bonaldo P.,
RA Bressan G.M.;
RT "Expression of the EMILIN-1 gene during mouse development.";
RL Matrix Biol. 21:603-609(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH EFEMP2.
RX PubMed=28717224; DOI=10.1038/s41598-017-05835-7;
RA Schiavinato A., Keene D.R., Imhof T., Doliana R., Sasaki T., Sengle G.;
RT "Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of
RT osteoblasts.";
RL Sci. Rep. 7:5526-5526(2017).
CC -!- FUNCTION: May be responsible for anchoring smooth muscle cells to
CC elastic fibers, and may be involved not only in the formation of the
CC elastic fiber, but also in the processes that regulate vessel assembly.
CC Has cell adhesive capacity (By similarity). May have a function in
CC placenta formation and initial organogenesis and a later role in
CC interstitial connective tissue. {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer associated through a moderately stable interaction
CC of the C-terminal globular C1q domains, allowing the nucleation of the
CC triple helix and then a further quaternary assembly to higher-order
CC polymers via intermolecular disulfide bonds. Interacts with EMILIN2 (By
CC similarity). Interacts with EFEMP2; this interaction promotes the
CC incorporation of EFEMP2 into the extracellular matrix
CC (PubMed:28717224). {ECO:0000250, ECO:0000269|PubMed:28717224}.
CC -!- INTERACTION:
CC Q99K41; P07200: TGFB1; Xeno; NbExp=2; IntAct=EBI-906561, EBI-907660;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q9Y6C2}. Note=Found mainly at the
CC interface between amorphous elastin and microfibrils.
CC {ECO:0000250|UniProtKB:Q9Y6C2}.
CC -!- DEVELOPMENTAL STAGE: Detectable in morula and blastocyst. First
CC expressed in ectoplacental cone in embryos of 6.5 days and in
CC extraembryonic visceral endoderm at 7.5 days. Expressed also in the
CC allantois. Expression in the ectoplacental cone-derived secondary
CC trophoblast giant cells and spongiotrophoblast is strong up to 11.5
CC days and then declines. In the embryo, high levels are initially
CC expressed in blood vessels, perineural mesenchyme and somites at 8.5
CC days. Later on, intense expression is identified in the mesenchymal
CC component of organs anlage (ie lung and liver) and different
CC mesenchymal condensations (ie limb bud and branchial arches). At late
CC gestation expression is widely distributed in interstitial connective
CC tissue and smooth muscle cell-rich tissues.
CC {ECO:0000269|PubMed:12475644}.
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DR EMBL; AK029337; BAC26403.1; -; mRNA.
DR EMBL; BC005481; AAH05481.1; -; mRNA.
DR CCDS; CCDS19167.1; -.
DR RefSeq; NP_598679.1; NM_133918.2.
DR AlphaFoldDB; Q99K41; -.
DR SMR; Q99K41; -.
DR BioGRID; 221560; 1.
DR ComplexPortal; CPX-437; EMILIN-1 complex.
DR IntAct; Q99K41; 3.
DR STRING; 10090.ENSMUSP00000031055; -.
DR GlyGen; Q99K41; 7 sites.
DR iPTMnet; Q99K41; -.
DR PhosphoSitePlus; Q99K41; -.
DR EPD; Q99K41; -.
DR MaxQB; Q99K41; -.
DR PaxDb; Q99K41; -.
DR PeptideAtlas; Q99K41; -.
DR PRIDE; Q99K41; -.
DR ProteomicsDB; 275861; -.
DR Antibodypedia; 1001; 201 antibodies from 25 providers.
DR Ensembl; ENSMUST00000031055; ENSMUSP00000031055; ENSMUSG00000029163.
DR GeneID; 100952; -.
DR KEGG; mmu:100952; -.
DR UCSC; uc008wwm.1; mouse.
DR CTD; 11117; -.
DR MGI; MGI:1926189; Emilin1.
DR VEuPathDB; HostDB:ENSMUSG00000029163; -.
DR eggNOG; ENOG502RIZH; Eukaryota.
DR GeneTree; ENSGT01030000234633; -.
DR HOGENOM; CLU_319805_0_0_1; -.
DR InParanoid; Q99K41; -.
DR OMA; MAPSTFW; -.
DR OrthoDB; 1205089at2759; -.
DR PhylomeDB; Q99K41; -.
DR TreeFam; TF331033; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR BioGRID-ORCS; 100952; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Emilin1; mouse.
DR PRO; PR:Q99K41; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99K41; protein.
DR Bgee; ENSMUSG00000029163; Expressed in ectoplacental cone and 153 other tissues.
DR Genevisible; Q99K41; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:1990971; C:EMILIN complex; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0034668; C:integrin alpha4-beta1 complex; ISO:MGI.
DR GO; GO:0030023; F:extracellular matrix constituent conferring elasticity; IMP:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0098640; F:integrin binding involved in cell-matrix adhesion; ISO:MGI.
DR GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:ComplexPortal.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0048251; P:elastic fiber assembly; IMP:BHF-UCL.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0050866; P:negative regulation of cell activation; IMP:BHF-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IMP:BHF-UCL.
DR GO; GO:1904027; P:negative regulation of collagen fibril organization; IMP:BHF-UCL.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:1905522; P:negative regulation of macrophage migration; IMP:BHF-UCL.
DR GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:ComplexPortal.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; ISO:MGI.
DR GO; GO:1901203; P:positive regulation of extracellular matrix assembly; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; IC:ComplexPortal.
DR GO; GO:0008217; P:regulation of blood pressure; IDA:ComplexPortal.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:ComplexPortal.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF07546; EMI; 1.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Coiled coil; Collagen; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:Q9Y6C2"
FT CHAIN 22..1017
FT /note="EMILIN-1"
FT /id="PRO_0000007816"
FT DOMAIN 56..133
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 815..865
FT /note="Collagen-like"
FT DOMAIN 867..1014
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 134..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 171..211
FT /evidence="ECO:0000255"
FT COILED 237..266
FT /evidence="ECO:0000255"
FT COILED 310..374
FT /evidence="ECO:0000255"
FT COILED 519..573
FT /evidence="ECO:0000255"
FT COILED 676..697
FT /evidence="ECO:0000255"
FT COILED 789..809
FT /evidence="ECO:0000255"
FT COMPBIAS 819..841
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 795
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 87..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 122..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
SQ SEQUENCE 1017 AA; 107585 MW; 2EF903204DB9C88F CRC64;
MAPRALWSCY LCCLLTIATE AASYPPRGYS LYTGGTGALS PGGPQAQNSP RPASRHRNWC
AYVVTRTVSC VLEDGVETIV KPDYQPCGWG QPHCSRSIMY RSFLRPRYRV AYKTVTDMEW
RCCQGYGGDD CGEGPASVLG PAPSTPLPRP RPVRPNLSGS SAGSHLSGLG GEGPVESEKV
QQLERQVKSL TKELQGLRGV LQGMNGRLAE DVQRAVDTVF NGRQQPADAA ARPGVHETLS
EIQQQLQLLD NRVSTHDQEL GHLNNHHNGG PGGGGRASGP VPVPSGPSEE LLRQLERQLQ
ESCSVCLTGL DGFRQQQQED RERLRTLEKL MSSMEERQQQ LVGPAMARRP PQECCPPELG
RRVSELERRL DVVTGSLTVL SGRRGSELGG AAGQGGHPPG YTSLASRLSR LEDRFNSTLG
PSEEQEKNWP GGPGRLGHWL PAAPGRLEKL EGLLANVSRE LGGRMDLLEE QVAGAVRTCG
QICSGAPGEQ DSRVNEILSA LERRVLDSEG RLQLVGSGLH EAEAAGEAQQ AVLEGLQGLL
SRLRERMDAQ EETAAEILLR LNLTAAQLSQ LEGLLQARGD EGCGACGGVQ EELGRLRDGV
ERCSCPLLPP RGPGAGPGVG GPSRGPLDGF SVFGGSSGSA LQALQGELSE VILTFSSLND
SLHELQTTVE GQGADLADLG ATKDSIISEI NRLQQEATEH VTESEERFRG LEEGQAQAGQ
CPSLEGRLGR LEGVCERLDT VAGGLQGLRE GLSRHVAGLW AAVRESNSTS LTQAALLEKL
LGGQAGLGRR LGALNNSLLL LEDRLQQLSL KDFTGPSGKA GPPGPPGLQG PSGPAGPPGP
PGKDGQQGAI GPPGPQGEQG AEGAPAAPVP RVAFSAALSL PRSEPGTVPF DRVLLNDGGY
YDPETGVFTA PLAGRYLLSA VLTGHRHEKV EAVLSRSNLG VARIDSGGYE PEGLENKPVA
ESQPSPGALG VFSLILPLQV GDTVCIDLVM GQLAHSEEPL TIFSGALLYE DTELEQV
