ID G3GXS2_CRIGR Unreviewed; 1017 AA.
AC G3GXS2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=EMILIN-1 {ECO:0000313|EMBL:EGV95861.1, ECO:0000313|RefSeq:XP_027280299.1};
DE SubName: Full=Elastin microfibril interfacer 1 {ECO:0000313|Ensembl:ENSCGRP00001020176.1};
GN Name=Emilin1 {ECO:0000313|Ensembl:ENSCGRP00001020176.1,
GN ECO:0000313|RefSeq:XP_027280299.1};
GN ORFNames=I79_002565 {ECO:0000313|EMBL:EGV95861.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV95861.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
RN [2] {ECO:0000313|EMBL:EGV95861.1}
RP NUCLEOTIDE SEQUENCE.
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary CHO-K1 cell line.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSCGRP00001020176.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [4] {ECO:0000313|RefSeq:XP_027280299.1}
RP IDENTIFICATION.
RC STRAIN=17A/GY {ECO:0000313|RefSeq:XP_027280299.1};
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_027280299.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; JH000061; EGV95861.1; -; Genomic_DNA.
DR RefSeq; XP_003497086.1; XM_003497038.3.
DR RefSeq; XP_027280299.1; XM_027424498.2.
DR STRING; 10029.G3GXS2; -.
DR PaxDb; 10029-XP_007613664-1; -.
DR Ensembl; ENSCGRT00001024420.1; ENSCGRP00001020176.1; ENSCGRG00001019405.1.
DR GeneID; 100763067; -.
DR KEGG; cge:100763067; -.
DR CTD; 11117; -.
DR eggNOG; ENOG502RIZH; Eukaryota.
DR GeneTree; ENSGT01030000234633; -.
DR OMA; EPGTIPF; -.
DR OrthoDB; 5314586at2759; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR Proteomes; UP000694386; Unplaced.
DR Proteomes; UP001108280; Chromosome 7.
DR GO; GO:1990971; C:EMILIN complex; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0034668; C:integrin alpha4-beta1 complex; IEA:Ensembl.
DR GO; GO:0030023; F:extracellular matrix constituent conferring elasticity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0098640; F:integrin binding involved in cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:Ensembl.
DR GO; GO:0003180; P:aortic valve morphogenesis; IEA:Ensembl.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0048251; P:elastic fiber assembly; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0050866; P:negative regulation of cell activation; IEA:Ensembl.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:1904027; P:negative regulation of collagen fibril organization; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:1905522; P:negative regulation of macrophage migration; IEA:Ensembl.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IEA:Ensembl.
DR GO; GO:1901203; P:positive regulation of extracellular matrix assembly; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
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 PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1.
DR PANTHER; PTHR15427:SF1; EMILIN-1; 1.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF07546; EMI; 1.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; TNF-like; 1.
DR PROSITE; PS50871; C1Q; 1.
DR PROSITE; PS51041; EMI; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1017
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041157637"
FT DOMAIN 56..133
FT /note="EMI"
FT /evidence="ECO:0000259|PROSITE:PS51041"
FT DOMAIN 867..1014
FT /note="C1q"
FT /evidence="ECO:0000259|PROSITE:PS50871"
FT REGION 133..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 533..560
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 676..703
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 419..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..848
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 107315 MW; 3D476F25E138BE12 CRC64;
MAPSTLWSCY LCYLLTVATK AASYPPRGYS LYTGGSSALS PGGPQTQNSP RPASRHRNWC
AYVVTRTVSC VLEDGVETFV KPDYQPCGWG QSQCPRSIMY RSFLRPRYRV AYKTVTDMEW
RCCQGYGGDD CGEGPASAQG PAPSTPHPRP RPVRPNLSGS SAGSHLSGLG GEGPGGSEKV
QQLEQQVQSL TKELQGLRGV LQGINGRLAE DVQRAVETAF NGRQQPADAA ARPGVHETLN
EIQHQLQLLD NRVSTHDQEL GHLNNHHNGG AGGGSRTPAP VTGPSGLSEE VLRQLERQLQ
ESCSVCLAGL DGFRQQQQED RERLRTLEKI LSSVEERQQQ LVGSAMARRP HQECCPPELG
RRLSELERRL DVVAGSVTVL SGRRGSELGG AAGQGGYPPG YTSLASRLSL LEDRFNSTLG
PSEEQEKDRP GGPGRLGHWL PDAPGRLEKL EELLANVSRE LGGRLGLLEE QVTGAVQACG
QLCSGGPGER DSQVSEILSA LERRVLDSEG QLRLVGSGLH KVGAAGEAQQ AMLEGLQGMV
GQLQERMDAQ EETAAELSLR LNLTAAQLSQ LQGLLQARGD EGCGACGGVQ EELGRLRDGV
ERCSCPLLPP RGPGAGPGVG GPSRGPLDGF SVFGGSSGSA LQALQGELSE VILTFSSLND
SLHELQTTVE GQGADLADLG ATKDSIISEI NRLQQEATEH ITESEERFRG LEEGLAQAGQ
CPSLEGRLGR LEGVCERLDA VAGGLQGLRE GLSRHVAGLW AALRESNSTS LTQAALLEKL
LGGQAGLGRR LGALNSSLLL LEDRLQQFSQ KDFTGPSGKA GPPGPPGLHG PPGPAGPPGP
PGKDGQKGPI GPPGPQGEQG VEGAPAAPVP RVAFSAALSL PRSEPGTVPF DRVLLNDGGY
YDPETGVFTA PLAGRYLLSA VLTGHRHEKV EAVLSRSNLG VARIDSGGYE PEGLENKPVA
ESQPSPGALG VFSLILPLQV GDTVCIDLVM GQLAHSEEPL TIFSGALLYE DTDLEQA
//
