ID G1L552_AILME Unreviewed; 1011 AA.
AC G1L552;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Ketohexokinase {ECO:0000313|Ensembl:ENSAMEP00000002012.2};
GN Name=EMILIN1 {ECO:0000313|Ensembl:ENSAMEP00000002012.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000002012.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000002012.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000002012.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; G1L552; -.
DR STRING; 9646.ENSAMEP00000002012; -.
DR Ensembl; ENSAMET00000002093.2; ENSAMEP00000002012.2; ENSAMEG00000001899.2.
DR eggNOG; ENOG502RIZH; Eukaryota.
DR GeneTree; ENSGT01030000234633; -.
DR HOGENOM; CLU_319805_0_0_1; -.
DR InParanoid; G1L552; -.
DR TreeFam; TF331033; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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 Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1011
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030170552"
FT DOMAIN 56..133
FT /note="EMI"
FT /evidence="ECO:0000259|PROSITE:PS51041"
FT DOMAIN 861..1008
FT /note="C1q"
FT /evidence="ECO:0000259|PROSITE:PS50871"
FT REGION 131..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 304..331
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 670..697
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 813..833
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1011 AA; 106183 MW; D3170DACCD00E8A3 CRC64;
MAPSTLWSCC FCCLLTTAVG AASYPPRGYS LYTGGGGALS PGEPQAQSAP RPASRHRNWC
AYVVTRTVSC VLEDGVETFV KADYQPCGWG QPQCPRSIMY RSLLRPRYRV AYKTVTDMEW
RCCQGYGGDD CAEGPAPTTP RPRPRPVRPN LSGSSAGSHL SGLGGEGPGD SEKVQQLEEQ
VQSLTKELQG LRGVLQGLSG RLAEDVQRAV ETAFNGRQPP ADAAARPGVH ETLSEIQQQL
QLLDNRVSTH DQELGHLNNH HTGGGGGGGR ALDPAPAPPG HGEELLRELE QRLQESCSVC
LAGLEGFRRQ QQEDRERLRA LEKLLASVEE RQRQLPGPAM GRRPLQECCP PELGRRLAEL
ERRLDVVAGS VTVLSGRRGT ELGGAAGQGG HPPGYTSLAS RLSRLEDQFN STLGPSEKQE
EGWPGHPGGL GHWLPAARGQ LEKLEGLLAN VSGVLGGRLD LLEEQVAGAV QACGQLCSGA
PGEQDSQVSE ILSALERRVL DSEGQLRLVG SGLHKVGAAG EAQRTALEEL QGVVGQLQGR
VDAQDETITE FALQLNLTAT RLGQLEGLLQ ARGDEGCGAC GGVQEELGRL RDGVERCSCP
LLPPRGPGAG PGVGGPSRGP LDGFSVFGGS SGSALQALQG ELSEVILTFS SLNDSLHELQ
TTVEGQGADL ADLGATKDRI ISEINRLQQE ATEHATESEE RFRGLEEGQA QAGQCPSLEG
RLGRLEGVCE RLDTVAGGLQ GLREGLSRHV AGLWAGLRET NSTSQTQAAL LEKLLGGQAG
LGRRLGALNS SVLLLEDQLH QLSLKDLTGP AGEAGPPGPP GIQGPPGPAG PPGLPGKDGQ
KGPIGPPGPQ GEQGVEGAPA APVPRVAFSA ALSLPRSEPG TVPFDRVLLN DGGYYDPETG
VFTAPLAGRY LLSAVLTGHR HEKVEAVLSR SNLGVARIDS GGYEPEGLEN KPVAESQPSP
GALGVFSLIL PLQAGDTVCI DLVMGQLAHS EEPLTIFSGA LLYGDLELEQ V
//
