GenomeNet

Database: UniProt
Entry: Q12805
LinkDB: Q12805
Original site: Q12805 
ID   FBLN3_HUMAN             Reviewed;         493 AA.
AC   Q12805; A8K3I4; B4DW75; D6W5D2; Q541U7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   10-APR-2019, entry version 194.
DE   RecName: Full=EGF-containing fibulin-like extracellular matrix protein 1;
DE   AltName: Full=Extracellular protein S1-5;
DE   AltName: Full=Fibrillin-like protein;
DE   AltName: Full=Fibulin-3;
DE            Short=FIBL-3;
DE   Flags: Precursor;
GN   Name=EFEMP1; Synonyms=FBLN3, FBNL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND POSSIBLE ALTERNATIVE SPLICING.
RC   TISSUE=Skin;
RX   PubMed=7799918; DOI=10.1128/MCB.15.1.120;
RA   Lecka-Czernik B., Lumpkin C.K. Jr., Goldstein S.;
RT   "An overexpressed gene transcript in senescent and quiescent human
RT   fibroblasts encoding a novel protein in the epidermal growth factor-
RT   like repeat family stimulates DNA synthesis.";
RL   Mol. Cell. Biol. 15:120-128(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8812496; DOI=10.1006/geno.1996.0402;
RA   Ikegawa S., Toda T., Okui K., Nakamura Y.;
RT   "Structure and chromosomal assignment of the human S1-5 gene (FBNL)
RT   that is highly homologous to fibrillin.";
RL   Genomics 35:590-592(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10601734; DOI=10.1016/S0945-053X(99)00038-4;
RA   Giltay R., Timpl R., Kostka G.;
RT   "Sequence, recombinant expression and tissue localization of two novel
RT   extracellular matrix proteins, fibulin-3 and fibulin-4.";
RL   Matrix Biol. 18:469-480(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11262647; DOI=10.1076/opge.22.1.27.2239;
RA   Sauer C.G., White K., Kellner U., Rudolph G., Jurklies B.,
RA   Pauleikhoff D., Weber B.H.;
RT   "EFEMP1 is not associated with sporadic early onset drusen.";
RL   Ophthalmic Genet. 22:27-34(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC   TISSUE=Synovium;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   TISSUE SPECIFICITY, AND CHARACTERIZATION OF VARIANT DHRD TRP-345.
RX   PubMed=12242346; DOI=10.1073/pnas.202491599;
RA   Marmorstein L.Y., Munier F.L., Arsenijevic Y., Schorderet D.F.,
RA   McLaughlin P.J., Chung D., Traboulsi E., Marmorstein A.D.;
RT   "Aberrant accumulation of EFEMP1 underlies drusen formation in
RT   Malattia Leventinese and age-related macular degeneration.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13067-13072(2002).
RN   [10]
RP   INTERACTION WITH TIMP3.
RX   PubMed=15123717; DOI=10.1074/jbc.M403026200;
RA   Klenotic P.A., Munier F.L., Marmorstein L.Y., Anand-Apte B.;
RT   "Tissue inhibitor of metalloproteinases-3 (TIMP-3) is a binding
RT   partner of epithelial growth factor-containing fibulin-like
RT   extracellular matrix protein 1 (EFEMP1). Implications for macular
RT   degenerations.";
RL   J. Biol. Chem. 279:30469-30473(2004).
RN   [11]
RP   FUNCTION IN EGFR ACTIVATION.
RX   PubMed=19804359; DOI=10.1515/BC.2009.140;
RA   Camaj P., Seeliger H., Ischenko I., Krebs S., Blum H., De Toni E.N.,
RA   Faktorova D., Jauch K.W., Bruns C.J.;
RT   "EFEMP1 binds the EGF receptor and activates MAPK and Akt pathways in
RT   pancreatic carcinoma cells.";
RL   Biol. Chem. 390:1293-1302(2009).
RN   [12]
RP   INTERACTION WITH ECM1.
RX   PubMed=19275936; DOI=10.1016/j.matbio.2009.02.003;
RA   Sercu S., Lambeir A.M., Steenackers E., El Ghalbzouri A.,
RA   Geentjens K., Sasaki T., Oyama N., Merregaert J.;
RT   "ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332
RT   through its serum albumin subdomain-like 2 domain.";
RL   Matrix Biol. 28:160-169(2009).
RN   [13]
RP   FUNCTION.
RX   PubMed=19887559; DOI=10.1158/1541-7786.MCR-09-0207;
RA   Hu B., Thirtamara-Rajamani K.K., Sim H., Viapiano M.S.;
RT   "Fibulin-3 is uniquely upregulated in malignant gliomas and promotes
RT   tumor cell motility and invasion.";
RL   Mol. Cancer Res. 7:1756-1770(2009).
RN   [14]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20005202; DOI=10.1016/j.bbrc.2009.12.034;
RA   Wakabayashi T., Matsumine A., Nakazora S., Hasegawa M., Iino T.,
RA   Ota H., Sonoda H., Sudo A., Uchida A.;
RT   "Fibulin-3 negatively regulates chondrocyte differentiation.";
RL   Biochem. Biophys. Res. Commun. 391:1116-1121(2010).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22905912; DOI=10.1021/pr300539b;
RA   Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
RA   Fischer-Posovszky P., Mariman E.C., Renes J.;
RT   "Resveratrol-induced changes of the human adipocyte secretion
RT   profile.";
RL   J. Proteome Res. 11:4733-4743(2012).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [17]
RP   VARIANT DHRD TRP-345, AND VARIANT PHE-220.
RX   PubMed=10369267; DOI=10.1038/9722;
RA   Stone E.M., Lotery A.J., Munier F.L., Heon E., Piguet B., Guymer R.H.,
RA   Vandenburgh K., Cousin P., Nishimura D., Swiderski R.E., Silvestri G.,
RA   Mackey D.A., Hagerman G.S., Bird A.C., Sheffield V.C.,
RA   Schorderet D.F.;
RT   "A single EFEMP1 mutation associated with both malattia Leventinese
RT   and Doyne honeycomb retinal dystrophy.";
RL   Nat. Genet. 22:199-202(1999).
RN   [18]
RP   VARIANT DHRD TRP-345.
RX   PubMed=11384588; DOI=10.1016/S0002-9394(00)00926-0;
RA   Matsumoto M., Traboulsi E.I.;
RT   "Dominant radial drusen and Arg345Trp EFEMP1 mutation.";
RL   Am. J. Ophthalmol. 131:810-812(2001).
RN   [19]
RP   CHARACTERIZATION OF VARIANT DHRD TRP-345.
RX   PubMed=17666404; DOI=10.1093/hmg/ddm198;
RA   Fu L., Garland D., Yang Z., Shukla D., Rajendran A., Pearson E.,
RA   Stone E.M., Zhang K., Pierce E.A.;
RT   "The R345W mutation in EFEMP1 is pathogenic and causes AMD-like
RT   deposits in mice.";
RL   Hum. Mol. Genet. 16:2411-2422(2007).
CC   -!- FUNCTION: Binds EGFR, the EGF receptor, inducing EGFR
CC       autophosphorylation and the activation of downstream signaling
CC       pathways. May play a role in cell adhesion and migration. May
CC       function as a negative regulator of chondrocyte differentiation.
CC       In the olfactory epithelium, it may regulate glial cell migration,
CC       differentiation and the ability of glial cells to support neuronal
CC       neurite outgrowth. {ECO:0000269|PubMed:19804359,
CC       ECO:0000269|PubMed:19887559, ECO:0000269|PubMed:20005202}.
CC   -!- SUBUNIT: Interacts with ECM1. Interacts with TIMP3.
CC       {ECO:0000269|PubMed:15123717, ECO:0000269|PubMed:19275936}.
CC   -!- INTERACTION:
CC       Q9WMX2:- (xeno); NbExp=2; IntAct=EBI-536772, EBI-6863748;
CC       P10398:ARAF; NbExp=3; IntAct=EBI-536772, EBI-365961;
CC       P54259:ATN1; NbExp=3; IntAct=EBI-536772, EBI-945980;
CC       P46379:BAG6; NbExp=3; IntAct=EBI-536772, EBI-347552;
CC       P53673:CRYBA4; NbExp=3; IntAct=EBI-536772, EBI-7519711;
CC       P50222:MEOX2; NbExp=3; IntAct=EBI-536772, EBI-748397;
CC       Q6FHY5:MEOX2; NbExp=5; IntAct=EBI-536772, EBI-16439278;
CC       Q9NPQ8-4:RIC8A; NbExp=3; IntAct=EBI-536772, EBI-9091816;
CC       O43765:SGTA; NbExp=12; IntAct=EBI-536772, EBI-347996;
CC       Q12933:TRAF2; NbExp=11; IntAct=EBI-536772, EBI-355744;
CC       Q86UY0:TXNDC5; NbExp=3; IntAct=EBI-536772, EBI-2825190;
CC       Q9UHD9:UBQLN2; NbExp=4; IntAct=EBI-536772, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC       Secreted, extracellular space, extracellular matrix {ECO:0000250}.
CC       Note=Localizes to the lamina propria underneath the olfactory
CC       epithelium. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Experimental confirmation may be lacking for some
CC         isoforms.;
CC       Name=1;
CC         IsoId=Q12805-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q12805-2; Sequence=VSP_001392;
CC       Name=3;
CC         IsoId=Q12805-3; Sequence=VSP_001393;
CC       Name=4;
CC         IsoId=Q12805-4; Sequence=VSP_001394;
CC       Name=5;
CC         IsoId=Q12805-5; Sequence=VSP_054372, VSP_054373;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: In the eye, associated with photoreceptor
CC       outer and inner segment regions, the nerve fiber layer, outer
CC       nuclear layer and inner and outer plexiform layers of the retina.
CC       {ECO:0000269|PubMed:12242346, ECO:0000269|PubMed:20005202}.
CC   -!- DISEASE: Doyne honeycomb retinal dystrophy (DHRD) [MIM:126600]:
CC       Autosomal dominant disease characterized by yellow-white deposits
CC       known as drusen that accumulate beneath the retinal pigment
CC       epithelium. {ECO:0000269|PubMed:10369267,
CC       ECO:0000269|PubMed:11384588, ECO:0000269|PubMed:12242346,
CC       ECO:0000269|PubMed:17666404}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: Up-regulated in malignant gliomas. May increase
CC       glioma cell adhesiveness and invasive properties.
CC   -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Mutations of the EFEMP1 gene; Note=Retina
CC       International's Scientific Newsletter;
CC       URL="http://www.retina-international.org/files/sci-news/efempmut.htm";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/EFEMP1ID49818ch2p16.html";
DR   EMBL; U03877; AAA65590.1; -; mRNA.
DR   EMBL; AY004330; AAK11491.1; -; Genomic_DNA.
DR   EMBL; AY004321; AAK11491.1; JOINED; Genomic_DNA.
DR   EMBL; AY004322; AAK11491.1; JOINED; Genomic_DNA.
DR   EMBL; AY004325; AAK11491.1; JOINED; Genomic_DNA.
DR   EMBL; AY004324; AAK11491.1; JOINED; Genomic_DNA.
DR   EMBL; AY004323; AAK11491.1; JOINED; Genomic_DNA.
DR   EMBL; AY004326; AAK11491.1; JOINED; Genomic_DNA.
DR   EMBL; AY004328; AAK11491.1; JOINED; Genomic_DNA.
DR   EMBL; AY004329; AAK11491.1; JOINED; Genomic_DNA.
DR   EMBL; AY004327; AAK11491.1; JOINED; Genomic_DNA.
DR   EMBL; AK290599; BAF83288.1; -; mRNA.
DR   EMBL; AK301402; BAG62937.1; -; mRNA.
DR   EMBL; AC010895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC096549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471053; EAX00080.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAX00081.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAX00082.1; -; Genomic_DNA.
DR   EMBL; BC014410; AAH14410.1; -; mRNA.
DR   EMBL; BC098561; AAH98561.1; -; mRNA.
DR   CCDS; CCDS1857.1; -. [Q12805-1]
DR   PIR; I38449; I38449.
DR   RefSeq; NP_001034437.1; NM_001039348.2. [Q12805-1]
DR   RefSeq; NP_001034438.1; NM_001039349.2. [Q12805-1]
DR   UniGene; Hs.732348; -.
DR   UniGene; Hs.76224; -.
DR   ProteinModelPortal; Q12805; -.
DR   SMR; Q12805; -.
DR   BioGrid; 108496; 59.
DR   IntAct; Q12805; 61.
DR   MINT; Q12805; -.
DR   STRING; 9606.ENSP00000378058; -.
DR   iPTMnet; Q12805; -.
DR   PhosphoSitePlus; Q12805; -.
DR   SwissPalm; Q12805; -.
DR   BioMuta; EFEMP1; -.
DR   DMDM; 9973182; -.
DR   EPD; Q12805; -.
DR   jPOST; Q12805; -.
DR   MaxQB; Q12805; -.
DR   PaxDb; Q12805; -.
DR   PeptideAtlas; Q12805; -.
DR   PRIDE; Q12805; -.
DR   ProteomicsDB; 58959; -.
DR   ProteomicsDB; 58960; -. [Q12805-2]
DR   ProteomicsDB; 58961; -. [Q12805-3]
DR   ProteomicsDB; 58962; -. [Q12805-4]
DR   DNASU; 2202; -.
DR   Ensembl; ENST00000355426; ENSP00000347596; ENSG00000115380. [Q12805-1]
DR   Ensembl; ENST00000394555; ENSP00000378058; ENSG00000115380. [Q12805-1]
DR   GeneID; 2202; -.
DR   KEGG; hsa:2202; -.
DR   UCSC; uc002rzi.4; human. [Q12805-1]
DR   CTD; 2202; -.
DR   DisGeNET; 2202; -.
DR   EuPathDB; HostDB:ENSG00000115380.19; -.
DR   GeneCards; EFEMP1; -.
DR   HGNC; HGNC:3218; EFEMP1.
DR   HPA; CAB016368; -.
DR   HPA; HPA049806; -.
DR   HPA; HPA070841; -.
DR   HPA; HPA071588; -.
DR   MalaCards; EFEMP1; -.
DR   MIM; 126600; phenotype.
DR   MIM; 601548; gene.
DR   neXtProt; NX_Q12805; -.
DR   OpenTargets; ENSG00000115380; -.
DR   Orphanet; 75376; Familial drusen.
DR   PharmGKB; PA27652; -.
DR   eggNOG; ENOG410IR77; Eukaryota.
DR   eggNOG; ENOG410YCRW; LUCA.
DR   GeneTree; ENSGT00940000157837; -.
DR   HOGENOM; HOG000234337; -.
DR   HOVERGEN; HBG051560; -.
DR   InParanoid; Q12805; -.
DR   KO; K18262; -.
DR   OMA; PCQDPYV; -.
DR   OrthoDB; 1174178at2759; -.
DR   PhylomeDB; Q12805; -.
DR   TreeFam; TF317514; -.
DR   Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR   ChiTaRS; EFEMP1; human.
DR   GeneWiki; EFEMP1; -.
DR   GenomeRNAi; 2202; -.
DR   PRO; PR:Q12805; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000115380; Expressed in 226 organ(s), highest expression level in thoracic aorta.
DR   ExpressionAtlas; Q12805; baseline and differential.
DR   Genevisible; Q12805; HS.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
DR   GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:UniProtKB.
DR   GO; GO:0005006; F:epidermal growth factor-activated receptor activity; IDA:UniProtKB.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0043010; P:camera-type eye development; IEP:UniProtKB.
DR   GO; GO:0048048; P:embryonic eye morphogenesis; IEP:UniProtKB.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IDA:UniProtKB.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0048050; P:post-embryonic eye morphogenesis; IEP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR032973; EFEMP1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR037287; Fibulin_3/4/5.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   PANTHER; PTHR44074; PTHR44074; 1.
DR   PANTHER; PTHR44074:SF2; PTHR44074:SF2; 1.
DR   Pfam; PF12662; cEGF; 2.
DR   Pfam; PF07645; EGF_CA; 3.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00179; EGF_CA; 6.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 4.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 6.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Complete proteome; Disease mutation;
KW   Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Growth factor; Polymorphism; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   CHAIN        18    493       EGF-containing fibulin-like extracellular
FT                                matrix protein 1.
FT                                /FTId=PRO_0000007570.
FT   DOMAIN       26     71       EGF-like 1; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      173    213       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      214    253       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      254    293       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      294    333       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      334    378       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REGION      259    493       Mediates interaction with TIMP3.
FT                                {ECO:0000269|PubMed:15123717}.
FT   CARBOHYD    249    249       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    177    190       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    184    199       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    201    212       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    218    228       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    224    237       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    239    252       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    258    268       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    264    277       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    279    292       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    298    309       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    305    318       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    320    332       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    338    350       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    344    359       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    365    377       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ       1     58       Missing (in isoform 5).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054372.
FT   VAR_SEQ       1      8       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_001392.
FT   VAR_SEQ      58     58       Missing (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_001393.
FT   VAR_SEQ     106    106       Missing (in isoform 4). {ECO:0000305}.
FT                                /FTId=VSP_001394.
FT   VAR_SEQ     214    293       Missing (in isoform 5).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054373.
FT   VARIANT     220    220       I -> F (in dbSNP:rs748965004).
FT                                {ECO:0000269|PubMed:10369267}.
FT                                /FTId=VAR_009512.
FT   VARIANT     345    345       R -> W (in DHRD; misfolded, accumulates
FT                                in cells due to inefficient secretion;
FT                                induces the formation of deposits between
FT                                Bruch's membrane and the retinal pigment
FT                                epithelium where it accumulates;
FT                                dbSNP:rs121434491).
FT                                {ECO:0000269|PubMed:10369267,
FT                                ECO:0000269|PubMed:11384588,
FT                                ECO:0000269|PubMed:12242346,
FT                                ECO:0000269|PubMed:17666404}.
FT                                /FTId=VAR_009513.
SQ   SEQUENCE   493 AA;  54641 MW;  128CA5ED140DF414 CRC64;
     MLKALFLTML TLALVKSQDT EETITYTQCT DGYEWDPVRQ QCKDIDECDI VPDACKGGMK
     CVNHYGGYLC LPKTAQIIVN NEQPQQETQP AEGTSGATTG VVAASSMATS GVLPGGGFVA
     SAAAVAGPEM QTGRNNFVIR RNPADPQRIP SNPSHRIQCA AGYEQSEHNV CQDIDECTAG
     THNCRADQVC INLRGSFACQ CPPGYQKRGE QCVDIDECTI PPYCHQRCVN TPGSFYCQCS
     PGFQLAANNY TCVDINECDA SNQCAQQCYN ILGSFICQCN QGYELSSDRL NCEDIDECRT
     SSYLCQYQCV NEPGKFSCMC PQGYQVVRSR TCQDINECET TNECREDEMC WNYHGGFRCY
     PRNPCQDPYI LTPENRCVCP VSNAMCRELP QSIVYKYMSI RSDRSVPSDI FQIQATTIYA
     NTINTFRIKS GNENGEFYLR QTSPVSAMLV LVKSLSGPRE HIVDLEMLTV SSIGTFRTSS
     VLRLTIIVGP FSF
//
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