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";
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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 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: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.
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
//
