Q12805 (FBLN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
EGF-containing fibulin-like extracellular matrix protein 1

Alternative name(s):
Extracellular protein S1-5
Fibrillin-like protein
Fibulin-3
Short name=FIBL-3

Gene names

Name:	EFEMP1
Synonyms:	FBLN3, FBNL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth. Ref.10 Ref.12 Ref.13
Subunit structure	Interacts with ECM1. Interacts with TIMP3. Ref.9 Ref.11
Subcellular location	Secreted › extracellular space By similarity. Secreted › extracellular space › extracellular matrix By similarity. Note: Localizes to the lamina propria underneath the olfactory epithelium By similarity. Ref.13
Tissue specificity	In the eye, associated with photoreceptor outer and inner segment regions, the nerve fiber layer, outer nuclear layer and inner and outer plexiform layers of the retina. Ref.8 Ref.13
Involvement in disease	Doyne honeycomb retinal dystrophy (DHRD) [MIM:126600]: Autosomal dominant disease characterized by yellow-white deposits known as drusen that accumulate beneath the retinal pigment epithelium. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.14 Ref.15 Ref.16
Miscellaneous	Up-regulated in malignant gliomas. May increase glioma cell adhesiveness and invasive properties.
Sequence similarities	Belongs to the fibulin family. Contains 6 EGF-like domains.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	EGF-like domain Repeat Signal
Ligand	Calcium
Molecular function	Growth factor
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of chondrocyte differentiation Inferred from direct assay Ref.13. Source: UniProtKB peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.10. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from direct assay Ref.13. Source: UniProtKB visual perception Traceable author statement Ref.14. Source: ProtInc
Cellular_component	extracellular space Inferred from direct assay Ref.13. Source: UniProtKB proteinaceous extracellular matrix Traceable author statement Ref.14. Source: ProtInc
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro epidermal growth factor receptor binding Inferred from direct assay Ref.10. Source: UniProtKB epidermal growth factor-activated receptor activity Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARAF	P10398	3	EBI-536772,EBI-365961
ATN1	P54259	3	EBI-536772,EBI-945980

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q12805-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q12805-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: Missing.

Isoform 3 (identifier: Q12805-3)

The sequence of this isoform differs from the canonical sequence as follows:
     58-58: Missing.

Isoform 4 (identifier: Q12805-4)

The sequence of this isoform differs from the canonical sequence as follows:
     106-106: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Chain	18 – 493	476	EGF-containing fibulin-like extracellular matrix protein 1		PRO_0000007570
Regions
	Domain	26 – 71	46	EGF-like 1; atypical
	Domain	173 – 213	41	EGF-like 2; calcium-binding Potential
	Domain	214 – 253	40	EGF-like 3; calcium-binding Potential
	Domain	254 – 293	40	EGF-like 4; calcium-binding Potential
	Domain	294 – 333	40	EGF-like 5; calcium-binding Potential
	Domain	334 – 378	45	EGF-like 6; calcium-binding Potential
	Region	259 – 493	235	Mediates interaction with TIMP3
Amino acid modifications
	Glycosylation	249	1	N-linked (GlcNAc...) Potential
	Disulfide bond	177 ↔ 190		By similarity
	Disulfide bond	184 ↔ 199		By similarity
	Disulfide bond	201 ↔ 212		By similarity
	Disulfide bond	218 ↔ 228		By similarity
	Disulfide bond	224 ↔ 237		By similarity
	Disulfide bond	239 ↔ 252		By similarity
	Disulfide bond	258 ↔ 268		By similarity
	Disulfide bond	264 ↔ 277		By similarity
	Disulfide bond	279 ↔ 292		By similarity
	Disulfide bond	298 ↔ 309		By similarity
	Disulfide bond	305 ↔ 318		By similarity
	Disulfide bond	320 ↔ 332		By similarity
	Disulfide bond	338 ↔ 350		By similarity
	Disulfide bond	344 ↔ 359		By similarity
	Disulfide bond	365 ↔ 377		By similarity
Natural variations
	Alternative sequence	1 – 8	8	Missing in isoform 2.		VSP_001392
	Alternative sequence	58	1	Missing in isoform 3.		VSP_001393
	Alternative sequence	106	1	Missing in isoform 4.		VSP_001394
	Natural variant	220	1	I → F. Ref.14		VAR_009512
	Natural variant	345	1	R → W in DHRD; misfolded, accumulates in cells due to inefficient secretion; induces the formation of deposits between Bruch's membrane and the retinal pigment epithelium where it accumulates. Ref.8 Ref.14 Ref.15 Ref.16		VAR_009513

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 128CA5ED140DF414	FASTA	493	54,641
	10 20 30 40 50 60 MLKALFLTML TLALVKSQDT EETITYTQCT DGYEWDPVRQ QCKDIDECDI VPDACKGGMK 70 80 90 100 110 120 CVNHYGGYLC LPKTAQIIVN NEQPQQETQP AEGTSGATTG VVAASSMATS GVLPGGGFVA 130 140 150 160 170 180 SAAAVAGPEM QTGRNNFVIR RNPADPQRIP SNPSHRIQCA AGYEQSEHNV CQDIDECTAG 190 200 210 220 230 240 THNCRADQVC INLRGSFACQ CPPGYQKRGE QCVDIDECTI PPYCHQRCVN TPGSFYCQCS 250 260 270 280 290 300 PGFQLAANNY TCVDINECDA SNQCAQQCYN ILGSFICQCN QGYELSSDRL NCEDIDECRT 310 320 330 340 350 360 SSYLCQYQCV NEPGKFSCMC PQGYQVVRSR TCQDINECET TNECREDEMC WNYHGGFRCY 370 380 390 400 410 420 PRNPCQDPYI LTPENRCVCP VSNAMCRELP QSIVYKYMSI RSDRSVPSDI FQIQATTIYA 430 440 450 460 470 480 NTINTFRIKS GNENGEFYLR QTSPVSAMLV LVKSLSGPRE HIVDLEMLTV SSIGTFRTSS 490 VLRLTIIVGP FSF
	Isoform 2 [UniParc]. Checksum: CF3DF7CCD89C58AC	FASTA	485	53,722
	10 20 30 40 50 60 MLTLALVKSQ DTEETITYTQ CTDGYEWDPV RQQCKDIDEC DIVPDACKGG MKCVNHYGGY 70 80 90 100 110 120 LCLPKTAQII VNNEQPQQET QPAEGTSGAT TGVVAASSMA TSGVLPGGGF VASAAAVAGP 130 140 150 160 170 180 EMQTGRNNFV IRRNPADPQR IPSNPSHRIQ CAAGYEQSEH NVCQDIDECT AGTHNCRADQ 190 200 210 220 230 240 VCINLRGSFA CQCPPGYQKR GEQCVDIDEC TIPPYCHQRC VNTPGSFYCQ CSPGFQLAAN 250 260 270 280 290 300 NYTCVDINEC DASNQCAQQC YNILGSFICQ CNQGYELSSD RLNCEDIDEC RTSSYLCQYQ 310 320 330 340 350 360 CVNEPGKFSC MCPQGYQVVR SRTCQDINEC ETTNECREDE MCWNYHGGFR CYPRNPCQDP 370 380 390 400 410 420 YILTPENRCV CPVSNAMCRE LPQSIVYKYM SIRSDRSVPS DIFQIQATTI YANTINTFRI 430 440 450 460 470 480 KSGNENGEFY LRQTSPVSAM LVLVKSLSGP REHIVDLEML TVSSIGTFRT SSVLRLTIIV GPFSF
	Isoform 3 [UniParc]. Checksum: FD09CF260582EA63	FASTA	492	54,583
	10 20 30 40 50 60 MLKALFLTML TLALVKSQDT EETITYTQCT DGYEWDPVRQ QCKDIDECDI VPDACKGMKC 70 80 90 100 110 120 VNHYGGYLCL PKTAQIIVNN EQPQQETQPA EGTSGATTGV VAASSMATSG VLPGGGFVAS 130 140 150 160 170 180 AAAVAGPEMQ TGRNNFVIRR NPADPQRIPS NPSHRIQCAA GYEQSEHNVC QDIDECTAGT 190 200 210 220 230 240 HNCRADQVCI NLRGSFACQC PPGYQKRGEQ CVDIDECTIP PYCHQRCVNT PGSFYCQCSP 250 260 270 280 290 300 GFQLAANNYT CVDINECDAS NQCAQQCYNI LGSFICQCNQ GYELSSDRLN CEDIDECRTS 310 320 330 340 350 360 SYLCQYQCVN EPGKFSCMCP QGYQVVRSRT CQDINECETT NECREDEMCW NYHGGFRCYP 370 380 390 400 410 420 RNPCQDPYIL TPENRCVCPV SNAMCRELPQ SIVYKYMSIR SDRSVPSDIF QIQATTIYAN 430 440 450 460 470 480 TINTFRIKSG NENGEFYLRQ TSPVSAMLVL VKSLSGPREH IVDLEMLTVS SIGTFRTSSV 490 LRLTIIVGPF SF
	Isoform 4 [UniParc]. Checksum: EF7B59437CAA3C67	FASTA	492	54,553
	10 20 30 40 50 60 MLKALFLTML TLALVKSQDT EETITYTQCT DGYEWDPVRQ QCKDIDECDI VPDACKGGMK 70 80 90 100 110 120 CVNHYGGYLC LPKTAQIIVN NEQPQQETQP AEGTSGATTG VVAASMATSG VLPGGGFVAS 130 140 150 160 170 180 AAAVAGPEMQ TGRNNFVIRR NPADPQRIPS NPSHRIQCAA GYEQSEHNVC QDIDECTAGT 190 200 210 220 230 240 HNCRADQVCI NLRGSFACQC PPGYQKRGEQ CVDIDECTIP PYCHQRCVNT PGSFYCQCSP 250 260 270 280 290 300 GFQLAANNYT CVDINECDAS NQCAQQCYNI LGSFICQCNQ GYELSSDRLN CEDIDECRTS 310 320 330 340 350 360 SYLCQYQCVN EPGKFSCMCP QGYQVVRSRT CQDINECETT NECREDEMCW NYHGGFRCYP 370 380 390 400 410 420 RNPCQDPYIL TPENRCVCPV SNAMCRELPQ SIVYKYMSIR SDRSVPSDIF QIQATTIYAN 430 440 450 460 470 480 TINTFRIKSG NENGEFYLRQ TSPVSAMLVL VKSLSGPREH IVDLEMLTVS SIGTFRTSSV 490 LRLTIIVGPF SF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An overexpressed gene transcript in senescent and quiescent human fibroblasts encoding a novel protein in the epidermal growth factor-like repeat family stimulates DNA synthesis." Lecka-Czernik B., Lumpkin C.K. Jr., Goldstein S. Mol. Cell. Biol. 15:120-128(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE ALTERNATIVE SPLICING. Tissue: Skin.
[2]	"Structure and chromosomal assignment of the human S1-5 gene (FBNL) that is highly homologous to fibrillin." Ikegawa S., Toda T., Okui K., Nakamura Y. Genomics 35:590-592(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Sequence, recombinant expression and tissue localization of two novel extracellular matrix proteins, fibulin-3 and fibulin-4." Giltay R., Timpl R., Kostka G. Matrix Biol. 18:469-480(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"EFEMP1 is not associated with sporadic early onset drusen." Sauer C.G., White K., Kellner U., Rudolph G., Jurklies B., Pauleikhoff D., Weber B.H. Ophthalmic Genet. 22:27-34(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[8]	"Aberrant accumulation of EFEMP1 underlies drusen formation in Malattia Leventinese and age-related macular degeneration." Marmorstein L.Y., Munier F.L., Arsenijevic Y., Schorderet D.F., McLaughlin P.J., Chung D., Traboulsi E., Marmorstein A.D. Proc. Natl. Acad. Sci. U.S.A. 99:13067-13072(2002) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT DHRD TRP-345.
[9]	"Tissue inhibitor of metalloproteinases-3 (TIMP-3) is a binding partner of epithelial growth factor-containing fibulin-like extracellular matrix protein 1 (EFEMP1). Implications for macular degenerations." Klenotic P.A., Munier F.L., Marmorstein L.Y., Anand-Apte B. J. Biol. Chem. 279:30469-30473(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TIMP3.
[10]	"EFEMP1 binds the EGF receptor and activates MAPK and Akt pathways in pancreatic carcinoma cells." Camaj P., Seeliger H., Ischenko I., Krebs S., Blum H., De Toni E.N., Faktorova D., Jauch K.W., Bruns C.J. Biol. Chem. 390:1293-1302(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN EGFR ACTIVATION.
[11]	"ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332 through its serum albumin subdomain-like 2 domain." Sercu S., Lambeir A.M., Steenackers E., El Ghalbzouri A., Geentjens K., Sasaki T., Oyama N., Merregaert J. Matrix Biol. 28:160-169(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ECM1.
[12]	"Fibulin-3 is uniquely upregulated in malignant gliomas and promotes tumor cell motility and invasion." Hu B., Thirtamara-Rajamani K.K., Sim H., Viapiano M.S. Mol. Cancer Res. 7:1756-1770(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Fibulin-3 negatively regulates chondrocyte differentiation." Wakabayashi T., Matsumine A., Nakazora S., Hasegawa M., Iino T., Ota H., Sonoda H., Sudo A., Uchida A. Biochem. Biophys. Res. Commun. 391:1116-1121(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[14]	"A single EFEMP1 mutation associated with both malattia Leventinese and Doyne honeycomb retinal dystrophy." Stone E.M., Lotery A.J., Munier F.L., Heon E., Piguet B., Guymer R.H., Vandenburgh K., Cousin P., Nishimura D., Swiderski R.E., Silvestri G., Mackey D.A., Hagerman G.S., Bird A.C., Sheffield V.C., Schorderet D.F. Nat. Genet. 22:199-202(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DHRD TRP-345, VARIANT PHE-220.
[15]	"Dominant radial drusen and Arg345Trp EFEMP1 mutation." Matsumoto M., Traboulsi E.I. Am. J. Ophthalmol. 131:810-812(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DHRD TRP-345.
[16]	"The R345W mutation in EFEMP1 is pathogenic and causes AMD-like deposits in mice." Fu L., Garland D., Yang Z., Shukla D., Rajendran A., Pearson E., Stone E.M., Zhang K., Pierce E.A. Hum. Mol. Genet. 16:2411-2422(2007) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT DHRD TRP-345.
+	Additional computationally mapped references.

Web resources

Mutations of the EFEMP1 gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	U03877 mRNA. Translation: AAA65590.1. AY004330 , AY004321, AY004322, AY004325, AY004324, AY004323, AY004326, AY004328, AY004329, AY004327 Genomic DNA. Translation: AAK11491.1. AK290599 mRNA. Translation: BAF83288.1. CH471053 Genomic DNA. Translation: EAX00080.1. CH471053 Genomic DNA. Translation: EAX00081.1. CH471053 Genomic DNA. Translation: EAX00082.1. BC014410 mRNA. Translation: AAH14410.1. BC098561 mRNA. Translation: AAH98561.1.
IPI	IPI00029658. IPI00220813. IPI00220814. IPI00220815.
PIR	I38449.
RefSeq	NP_001034437.1. NM_001039348.2. NP_001034438.1. NM_001039349.2.
UniGene	Hs.732348. Hs.76224.
3D structure databases
ProteinModelPortal	Q12805.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q12805. 20 interactions.
MINT	MINT-1466511.
STRING	9606.ENSP00000347596.
PTM databases
PhosphoSite	Q12805.
Polymorphism databases
DMDM	9973182.
Proteomic databases
PaxDb	Q12805.
PRIDE	Q12805.
Protocols and materials databases
DNASU	2202.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000355426; ENSP00000347596; ENSG00000115380. ENST00000394554; ENSP00000378057; ENSG00000115380. ENST00000394555; ENSP00000378058; ENSG00000115380.
GeneID	2202.
KEGG	hsa:2202.
UCSC	uc002rzi.3. human.
Organism-specific databases
CTD	2202.
GeneCards	GC02M056093.
HGNC	HGNC:3218. EFEMP1.
MIM	126600. phenotype. 601548. gene.
neXtProt	NX_Q12805.
Orphanet	75376. Familial drusen.
PharmGKB	PA27652.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG250502.
HOGENOM	HOG000234337.
HOVERGEN	HBG051560.
InParanoid	Q12805.
OMA	VQTGRNN.
OrthoDB	EOG4PNXGR.
PhylomeDB	Q12805.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	Q12805.
Bgee	Q12805.
CleanEx	HS_EFEMP1.
Genevestigator	Q12805.
GermOnline	ENSG00000115380. Homo sapiens.
Family and domain databases
InterPro	IPR026823. cEGF. IPR026824. Efemp1/Efemp2. IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. [Graphical view]
PANTHER	PTHR24048:SF2. PTHR24048:SF2. 1 hit.
Pfam	PF12662. cEGF. 3 hits. PF07645. EGF_CA. 2 hits. [Graphical view]
SMART	SM00179. EGF_CA. 4 hits. [Graphical view]
PROSITE	PS00010. ASX_HYDROXYL. 4 hits. PS00022. EGF_1. False negative. PS01186. EGF_2. 4 hits. PS50026. EGF_3. 4 hits. PS01187. EGF_CA. 6 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EFEMP1. human.
GenomeRNAi	2202.
NextBio	8899.
SOURCE	Search...

Entry information

Entry name

FBLN3_HUMAN

Accession

Primary (citable) accession number: Q12805
Secondary accession number(s): A8K3I4, D6W5D2, Q541U7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.