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 27-MAR-2024, entry version 223. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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-like RT 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) that is RT 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., Pauleikhoff D., RA 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., 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., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., 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., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 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., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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 project: RT 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 Malattia RT 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 partner of RT epithelial growth factor-containing fibulin-like extracellular matrix RT protein 1 (EFEMP1). Implications for macular 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., Geentjens K., RA Sasaki T., Oyama N., Merregaert J.; RT "ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332 through RT 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 tumor RT 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., Ota H., RA 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., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT 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., Schorderet D.F.; RT "A single EFEMP1 mutation associated with both malattia Leventinese and RT 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 deposits in RT 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 function CC as a negative regulator of chondrocyte differentiation. In the CC 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 Q12805; Q9NYG5-2: ANAPC11; NbExp=3; IntAct=EBI-536772, EBI-12224467; CC Q12805; P10398: ARAF; NbExp=3; IntAct=EBI-536772, EBI-365961; CC Q12805; P54259: ATN1; NbExp=3; IntAct=EBI-536772, EBI-945980; CC Q12805; O95429: BAG4; NbExp=3; IntAct=EBI-536772, EBI-2949658; CC Q12805; Q9UL15: BAG5; NbExp=3; IntAct=EBI-536772, EBI-356517; CC Q12805; P46379: BAG6; NbExp=4; IntAct=EBI-536772, EBI-347552; CC Q12805; Q16740: CLPP; NbExp=3; IntAct=EBI-536772, EBI-1056029; CC Q12805; P53673: CRYBA4; NbExp=3; IntAct=EBI-536772, EBI-7519711; CC Q12805; A8MQ03: CYSRT1; NbExp=5; IntAct=EBI-536772, EBI-3867333; CC Q12805; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-536772, EBI-1752811; CC Q12805; P49639: HOXA1; NbExp=4; IntAct=EBI-536772, EBI-740785; CC Q12805; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-536772, EBI-3918847; CC Q12805; P42858: HTT; NbExp=3; IntAct=EBI-536772, EBI-466029; CC Q12805; P24592: IGFBP6; NbExp=3; IntAct=EBI-536772, EBI-947015; CC Q12805; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-536772, EBI-12196745; CC Q12805; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-536772, EBI-18395721; CC Q12805; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-536772, EBI-12111050; CC Q12805; Q5T751: LCE1C; NbExp=3; IntAct=EBI-536772, EBI-12224199; CC Q12805; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-536772, EBI-11973993; CC Q12805; Q5TA76: LCE3A; NbExp=3; IntAct=EBI-536772, EBI-9394625; CC Q12805; Q9BYE3: LCE3D; NbExp=3; IntAct=EBI-536772, EBI-6658837; CC Q12805; P50222: MEOX2; NbExp=3; IntAct=EBI-536772, EBI-748397; CC Q12805; Q6FHY5: MEOX2; NbExp=6; IntAct=EBI-536772, EBI-16439278; CC Q12805; Q13064: MKRN3; NbExp=3; IntAct=EBI-536772, EBI-2340269; CC Q12805; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-536772, EBI-10699187; CC Q12805; Q92570: NR4A3; NbExp=3; IntAct=EBI-536772, EBI-13644623; CC Q12805; P32242: OTX1; NbExp=3; IntAct=EBI-536772, EBI-740446; CC Q12805; Q9NPQ8-4: RIC8A; NbExp=3; IntAct=EBI-536772, EBI-9091816; CC Q12805; O43765: SGTA; NbExp=14; IntAct=EBI-536772, EBI-347996; CC Q12805; P03973: SLPI; NbExp=3; IntAct=EBI-536772, EBI-355293; CC Q12805; Q12933: TRAF2; NbExp=12; IntAct=EBI-536772, EBI-355744; CC Q12805; Q86UY0: TXNDC5; NbExp=3; IntAct=EBI-536772, EBI-2825190; CC Q12805; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-536772, EBI-947187; CC Q12805; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-536772, EBI-6863748; 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 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 -!- TISSUE SPECIFICITY: In the eye, associated with photoreceptor outer and CC inner segment regions, the nerve fiber layer, outer nuclear layer and CC 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 known CC as drusen that accumulate beneath the retinal pigment epithelium. CC {ECO:0000269|PubMed:10369267, ECO:0000269|PubMed:11384588, CC ECO:0000269|PubMed:12242346, ECO:0000269|PubMed:17666404}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: Up-regulated in malignant gliomas. May increase glioma CC 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="https://www.retina-international.org/files/sci-news/efempmut.htm"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/49818/EFEMP1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; Q12805; -. DR BioGRID; 108496; 118. DR IntAct; Q12805; 99. DR MINT; Q12805; -. DR STRING; 9606.ENSP00000378058; -. DR GlyCosmos; Q12805; 8 sites, 5 glycans. DR GlyGen; Q12805; 10 sites, 7 O-linked glycans (9 sites). DR iPTMnet; Q12805; -. DR PhosphoSitePlus; Q12805; -. DR SwissPalm; Q12805; -. DR BioMuta; EFEMP1; -. DR DMDM; 9973182; -. DR EPD; Q12805; -. DR jPOST; Q12805; -. DR MassIVE; Q12805; -. DR MaxQB; Q12805; -. DR PaxDb; 9606-ENSP00000378058; -. DR PeptideAtlas; Q12805; -. DR ProteomicsDB; 5317; -. DR ProteomicsDB; 58959; -. [Q12805-1] DR ProteomicsDB; 58960; -. [Q12805-2] DR ProteomicsDB; 58961; -. [Q12805-3] DR ProteomicsDB; 58962; -. [Q12805-4] DR Pumba; Q12805; -. DR ABCD; Q12805; 1 sequenced antibody. DR Antibodypedia; 30453; 426 antibodies from 36 providers. DR DNASU; 2202; -. DR Ensembl; ENST00000355426.8; ENSP00000347596.3; ENSG00000115380.20. [Q12805-1] DR Ensembl; ENST00000394555.6; ENSP00000378058.2; ENSG00000115380.20. [Q12805-1] DR GeneID; 2202; -. DR KEGG; hsa:2202; -. DR MANE-Select; ENST00000355426.8; ENSP00000347596.3; NM_001039348.3; NP_001034437.1. DR UCSC; uc002rzi.4; human. [Q12805-1] DR AGR; HGNC:3218; -. DR CTD; 2202; -. DR DisGeNET; 2202; -. DR GeneCards; EFEMP1; -. DR HGNC; HGNC:3218; EFEMP1. DR HPA; ENSG00000115380; Low tissue specificity. DR MalaCards; EFEMP1; -. DR MIM; 126600; phenotype. DR MIM; 601548; gene. DR neXtProt; NX_Q12805; -. DR OpenTargets; ENSG00000115380; -. DR Orphanet; 75376; Familial drusen. DR Orphanet; 98977; Juvenile glaucoma. DR PharmGKB; PA27652; -. DR VEuPathDB; HostDB:ENSG00000115380; -. DR eggNOG; KOG1217; Eukaryota. DR GeneTree; ENSGT00940000157837; -. DR HOGENOM; CLU_004826_0_1_1; -. DR InParanoid; Q12805; -. DR OMA; ERCICRS; -. DR OrthoDB; 19806at2759; -. DR PhylomeDB; Q12805; -. DR TreeFam; TF317514; -. DR PathwayCommons; Q12805; -. DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres. DR SignaLink; Q12805; -. DR BioGRID-ORCS; 2202; 15 hits in 1144 CRISPR screens. DR ChiTaRS; EFEMP1; human. DR GeneWiki; EFEMP1; -. DR GenomeRNAi; 2202; -. DR Pharos; Q12805; Tbio. DR PRO; PR:Q12805; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q12805; Protein. DR Bgee; ENSG00000115380; Expressed in right coronary artery and 206 other cell types or tissues. DR ExpressionAtlas; Q12805; baseline and differential. 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:0005006; F:epidermal growth factor receptor activity; IDA:UniProtKB. DR GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:UniProtKB. 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 DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR CDD; cd00054; EGF_CA; 4. DR Gene3D; 2.10.25.10; Laminin; 5. DR InterPro; IPR026823; cEGF. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR PANTHER; PTHR24034:SF102; EGF-CONTAINING FIBULIN-LIKE EXTRACELLULAR MATRIX PROTEIN 1; 1. DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF12662; cEGF; 3. DR Pfam; PF07645; EGF_CA; 2. DR SMART; SM00181; EGF; 5. DR SMART; SM00179; EGF_CA; 6. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF57184; Growth factor receptor domain; 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. DR Genevisible; Q12805; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Disease variant; Disulfide bond; KW EGF-like domain; Extracellular matrix; Glycoprotein; Growth factor; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT CHAIN 18..493 FT /note="EGF-containing fibulin-like extracellular matrix FT protein 1" FT /id="PRO_0000007570" FT DOMAIN 26..71 FT /note="EGF-like 1; atypical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 173..213 FT /note="EGF-like 2; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 214..253 FT /note="EGF-like 3; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 254..293 FT /note="EGF-like 4; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 294..333 FT /note="EGF-like 5; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 334..378 FT /note="EGF-like 6; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REGION 259..493 FT /note="Mediates interaction with TIMP3" FT /evidence="ECO:0000269|PubMed:15123717" FT CARBOHYD 249 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 177..190 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 184..199 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 201..212 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 218..228 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 224..237 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 239..252 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 258..268 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 264..277 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 279..292 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 298..309 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 305..318 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 320..332 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 338..350 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 344..359 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 365..377 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT VAR_SEQ 1..58 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054372" FT VAR_SEQ 1..8 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_001392" FT VAR_SEQ 58 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_001393" FT VAR_SEQ 106 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_001394" FT VAR_SEQ 214..293 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054373" FT VARIANT 220 FT /note="I -> F (in dbSNP:rs748965004)" FT /evidence="ECO:0000269|PubMed:10369267" FT /id="VAR_009512" FT VARIANT 345 FT /note="R -> W (in DHRD; misfolded, accumulates in cells due FT to inefficient secretion; induces the formation of deposits FT between Bruch's membrane and the retinal pigment epithelium FT where it accumulates; dbSNP:rs121434491)" FT /evidence="ECO:0000269|PubMed:10369267, FT ECO:0000269|PubMed:11384588, ECO:0000269|PubMed:12242346, FT ECO:0000269|PubMed:17666404" FT /id="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 //