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EGF-containing fibulin-like extracellular matrix protein 2 (Fibulin-4) (FIBL-4) (Protein UPH1)

 FBLN4_HUMAN             Reviewed;         443 AA.
O95967; A8K7R4; B3KM31; B3KQT1; O75967;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 3.
20-DEC-2017, entry version 183.
RecName: Full=EGF-containing fibulin-like extracellular matrix protein 2;
AltName: Full=Fibulin-4;
Short=FIBL-4;
AltName: Full=Protein UPH1;
Flags: Precursor;
Name=EFEMP2; Synonyms=FBLN4; ORFNames=UNQ200/PRO226;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-259.
TISSUE=Melanoma;
PubMed=10601734; DOI=10.1016/S0945-053X(99)00038-4;
Giltay R., Timpl R., Kostka G.;
"Sequence, recombinant expression and tissue localization of two novel
extracellular matrix proteins, fibulin-3 and fibulin-4.";
Matrix Biol. 18:469-480(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-259.
Zemel R., Shaul Y.;
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-259.
PubMed=10982184; DOI=10.1007/s004390051011;
Katsanis N., Venable S., Smith J.R., Lupski J.R.;
"Isolation of a paralog of the Doyne honeycomb retinal dystrophy gene
from the multiple retinopathy critical region on 11q13.";
Hum. Genet. 106:66-72(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-259.
TISSUE=Embryo, and Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-259.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-259.
TISSUE=Placenta;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-259.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH FBN1.
PubMed=17255108; DOI=10.1074/jbc.M608204200;
El-Hallous E., Sasaki T., Hubmacher D., Getie M., Tiedemann K.,
Brinckmann J., Baetge B., Davis E.C., Reinhardt D.P.;
"Fibrillin-1 interactions with fibulins depend on the first hybrid
domain and provide an adaptor function to tropoelastin.";
J. Biol. Chem. 282:8935-8946(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
STRUCTURE BY NMR OF 54-123, AND DISULFIDE BONDS.
Northeast structural genomics consortium (NESG);
"Solution NMR structure of the EGF-like 1 domain of human fibulin-4.";
Submitted (JUL-2009) to the PDB data bank.
[12]
VARIANT ARCL1B LYS-57.
PubMed=16685658; DOI=10.1086/504304;
Hucthagowder V., Sausgruber N., Kim K.H., Angle B., Marmorstein L.Y.,
Urban Z.;
"Fibulin-4: a novel gene for an autosomal recessive cutis laxa
syndrome.";
Am. J. Hum. Genet. 78:1075-1080(2006).
[13]
VARIANT ARCL1B CYS-279.
PubMed=17937443; DOI=10.1002/ajmg.a.31980;
Dasouki M., Markova D., Garola R., Sasaki T., Charbonneau N.L.,
Sakai L.Y., Chu M.L.;
"Compound heterozygous mutations in fibulin-4 causing neonatal lethal
pulmonary artery occlusion, aortic aneurysm, arachnodactyly, and mild
cutis laxa.";
Am. J. Med. Genet. A 143:2635-2641(2007).
[14]
VARIANT ARCL1B TYR-267.
PubMed=19664000; DOI=10.1111/j.1399-0004.2009.01204.x;
Hoyer J., Kraus C., Hammersen G., Geppert J.P., Rauch A.;
"Lethal cutis laxa with contractural arachnodactyly, overgrowth and
soft tissue bleeding due to a novel homozygous fibulin-4 gene
mutation.";
Clin. Genet. 76:276-281(2009).
-!- SUBUNIT: Interacts with FBN1 (via N-terminal domain)
(PubMed:17255108). {ECO:0000269|PubMed:17255108}.
-!- INTERACTION:
P54259:ATN1; NbExp=3; IntAct=EBI-743414, EBI-945980;
Q7Z6I8:C5orf24; NbExp=3; IntAct=EBI-743414, EBI-9995695;
Q02930-3:CREB5; NbExp=7; IntAct=EBI-743414, EBI-10192698;
P15502:ELN; NbExp=5; IntAct=EBI-743414, EBI-1222108;
Q5TZK3:FAM74A6; NbExp=5; IntAct=EBI-743414, EBI-10247271;
Q9UBX5:FBLN5; NbExp=3; IntAct=EBI-743414, EBI-947897;
P35555:FBN1; NbExp=3; IntAct=EBI-743414, EBI-2505934;
P56524:HDAC4; NbExp=3; IntAct=EBI-743414, EBI-308629;
Q96JK4-2:HHIPL1; NbExp=4; IntAct=EBI-743414, EBI-12083878;
P09022:Hoxa1 (xeno); NbExp=3; IntAct=EBI-743414, EBI-3957603;
Q8IUU6:IL16; NbExp=3; IntAct=EBI-743414, EBI-746574;
Q5TA81:LCE2C; NbExp=4; IntAct=EBI-743414, EBI-11973993;
Q5TA82:LCE2D; NbExp=3; IntAct=EBI-743414, EBI-10246750;
Q5T5A8:LCE3C; NbExp=3; IntAct=EBI-743414, EBI-10245291;
P28300:LOX; NbExp=7; IntAct=EBI-743414, EBI-3893481;
P50222:MEOX2; NbExp=3; IntAct=EBI-743414, EBI-748397;
Q7Z417:NUFIP2; NbExp=5; IntAct=EBI-743414, EBI-1210753;
O75360:PROP1; NbExp=4; IntAct=EBI-743414, EBI-9027467;
Q8WWY3:PRPF31; NbExp=5; IntAct=EBI-743414, EBI-1567797;
P43115-12:PTGER3; NbExp=3; IntAct=EBI-743414, EBI-10234038;
Q93062:RBPMS; NbExp=3; IntAct=EBI-743414, EBI-740322;
Q9BQY4:RHOXF2; NbExp=2; IntAct=EBI-743414, EBI-372094;
Q8WVD3:RNF138; NbExp=4; IntAct=EBI-743414, EBI-749039;
O43765:SGTA; NbExp=6; IntAct=EBI-743414, EBI-347996;
Q96EQ0:SGTB; NbExp=6; IntAct=EBI-743414, EBI-744081;
O75716:STK16; NbExp=5; IntAct=EBI-743414, EBI-749295;
Q9UMX0:UBQLN1; NbExp=4; IntAct=EBI-743414, EBI-741480;
Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-743414, EBI-10173939;
-!- SUBCELLULAR LOCATION: Secreted.
-!- DISEASE: Cutis laxa, autosomal recessive, 1B (ARCL1B)
[MIM:614437]: A connective tissue disorder characterized by loose,
hyperextensible skin with decreased resilience and elasticity
leading to a premature aged appearance. Face, hands, feet, joints,
and torso may be differentially affected. The clinical spectrum of
autosomal recessive cutis laxa is highly heterogeneous with
respect to organ involvement and severity. ARCL1B features include
emphysema, lethal pulmonary artery occlusion, aortic aneurysm,
cardiopulmonary insufficiency, birth fractures, arachnodactyly,
and fragility of blood vessels. {ECO:0000269|PubMed:16685658,
ECO:0000269|PubMed:17937443, ECO:0000269|PubMed:19664000}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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EMBL; AJ132819; CAA10791.2; -; mRNA.
EMBL; AF093119; AAC62108.1; -; mRNA.
EMBL; AF109121; AAF65188.1; -; mRNA.
EMBL; AK000980; BAG50843.1; -; mRNA.
EMBL; AK292079; BAF84768.1; -; mRNA.
EMBL; AY358899; AAQ89258.1; -; mRNA.
EMBL; AK075453; BAG52143.1; -; mRNA.
EMBL; AP001201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010456; AAH10456.1; -; mRNA.
CCDS; CCDS8116.1; -.
RefSeq; NP_058634.4; NM_016938.4.
UniGene; Hs.731454; -.
PDB; 2KL7; NMR; -; A=54-123.
PDBsum; 2KL7; -.
ProteinModelPortal; O95967; -.
SMR; O95967; -.
BioGrid; 119026; 51.
DIP; DIP-34518N; -.
IntAct; O95967; 132.
MINT; MINT-1439082; -.
STRING; 9606.ENSP00000309953; -.
iPTMnet; O95967; -.
PhosphoSitePlus; O95967; -.
BioMuta; EFEMP2; -.
PaxDb; O95967; -.
PeptideAtlas; O95967; -.
PRIDE; O95967; -.
DNASU; 30008; -.
Ensembl; ENST00000307998; ENSP00000309953; ENSG00000172638.
Ensembl; ENST00000531972; ENSP00000435295; ENSG00000172638.
GeneID; 30008; -.
KEGG; hsa:30008; -.
UCSC; uc001ofy.5; human.
CTD; 30008; -.
DisGeNET; 30008; -.
EuPathDB; HostDB:ENSG00000172638.12; -.
GeneCards; EFEMP2; -.
GeneReviews; EFEMP2; -.
HGNC; HGNC:3219; EFEMP2.
HPA; HPA023270; -.
MalaCards; EFEMP2; -.
MIM; 604633; gene.
MIM; 614437; phenotype.
neXtProt; NX_O95967; -.
OpenTargets; ENSG00000172638; -.
Orphanet; 90349; Autosomal recessive cutis laxa type 1.
Orphanet; 314718; Lethal arteriopathy syndrome due to fibulin-4 deficiency.
PharmGKB; PA27653; -.
eggNOG; ENOG410IR6U; Eukaryota.
eggNOG; ENOG410ZNNG; LUCA.
GeneTree; ENSGT00760000118806; -.
HOGENOM; HOG000234337; -.
HOVERGEN; HBG051560; -.
InParanoid; O95967; -.
KO; K19866; -.
OMA; QECHNLP; -.
OrthoDB; EOG091G04QP; -.
PhylomeDB; O95967; -.
TreeFam; TF317514; -.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
SIGNOR; O95967; -.
EvolutionaryTrace; O95967; -.
GeneWiki; EFEMP2; -.
GenomeRNAi; 30008; -.
PRO; PR:O95967; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000172638; -.
CleanEx; HS_EFEMP2; -.
ExpressionAtlas; O95967; baseline and differential.
Genevisible; O95967; HS.
GO; GO:0005604; C:basement membrane; TAS:ProtInc.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
GO; GO:0048251; P:elastic fiber assembly; IEA:InterPro.
InterPro; IPR026823; cEGF.
InterPro; IPR026824; Efemp2.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR037287; Fibulin_3/4/5.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
PANTHER; PTHR44074; PTHR44074; 1.
PANTHER; PTHR44074:SF3; PTHR44074:SF3; 1.
Pfam; PF12662; cEGF; 2.
Pfam; PF07645; EGF_CA; 3.
SMART; SM00181; EGF; 5.
SMART; SM00179; EGF_CA; 6.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS00010; ASX_HYDROXYL; 4.
PROSITE; PS01186; EGF_2; 4.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS01187; EGF_CA; 6.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Disease mutation;
Disulfide bond; EGF-like domain; Glycoprotein; Polymorphism;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 443 EGF-containing fibulin-like extracellular
matrix protein 2.
/FTId=PRO_0000007575.
DOMAIN 36 81 EGF-like 1; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 123 163 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 164 202 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 203 242 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 243 282 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 283 328 EGF-like 6; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
CARBOHYD 198 198 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 394 394 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 58 121 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|Ref.11}.
DISULFID 65 80 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|Ref.11}.
DISULFID 71 109 {ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000269|Ref.11}.
DISULFID 127 140 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 134 149 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 151 162 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 168 177 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 173 186 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 188 201 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 207 217 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 213 226 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 228 241 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 247 258 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 254 267 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 269 281 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 287 300 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 294 309 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 315 327 {ECO:0000255|PROSITE-ProRule:PRU00076}.
VARIANT 57 57 E -> K (in ARCL1B; dbSNP:rs119489101).
{ECO:0000269|PubMed:16685658}.
/FTId=VAR_027019.
VARIANT 259 259 I -> V (in dbSNP:rs601314).
{ECO:0000269|PubMed:10601734,
ECO:0000269|PubMed:10982184,
ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16303743,
ECO:0000269|Ref.2}.
/FTId=VAR_027020.
VARIANT 267 267 C -> Y (in ARCL1B; dbSNP:rs193302866).
{ECO:0000269|PubMed:19664000}.
/FTId=VAR_067069.
VARIANT 279 279 R -> C (in ARCL1B; dbSNP:rs119489102).
{ECO:0000269|PubMed:17937443}.
/FTId=VAR_067070.
CONFLICT 5 5 A -> T (in Ref. 1; CAA10791).
{ECO:0000305}.
CONFLICT 44 51 EWDPDSQH -> TQTAN (in Ref. 2; AAC62108).
{ECO:0000305}.
CONFLICT 46 46 D -> G (in Ref. 4; BAF84768).
{ECO:0000305}.
CONFLICT 96 96 P -> L (in Ref. 4; BAG50843).
{ECO:0000305}.
CONFLICT 103 111 AQHPNPCPP -> VNTQPLPT (in Ref. 2;
AAC62108). {ECO:0000305}.
CONFLICT 294 294 C -> W (in Ref. 2; AAC62108).
{ECO:0000305}.
CONFLICT 354 356 RSV -> AER (in Ref. 2; AAC62108).
{ECO:0000305}.
CONFLICT 355 355 S -> R (in Ref. 3; AAF65188).
{ECO:0000305}.
STRAND 68 73 {ECO:0000244|PDB:2KL7}.
STRAND 78 82 {ECO:0000244|PDB:2KL7}.
STRAND 113 116 {ECO:0000244|PDB:2KL7}.
SEQUENCE 443 AA; 49405 MW; 9315CFBBAA0FD3A7 CRC64;
MLPCASCLPG SLLLWALLLL LLGSASPQDS EEPDSYTECT DGYEWDPDSQ HCRDVNECLT
IPEACKGEMK CINHYGGYLC LPRSAAVIND LHGEGPPPPV PPAQHPNPCP PGYEPDDQDS
CVDVDECAQA LHDCRPSQDC HNLPGSYQCT CPDGYRKIGP ECVDIDECRY RYCQHRCVNL
PGSFRCQCEP GFQLGPNNRS CVDVNECDMG APCEQRCFNS YGTFLCRCHQ GYELHRDGFS
CSDIDECSYS SYLCQYRCIN EPGRFSCHCP QGYQLLATRL CQDIDECESG AHQCSEAQTC
VNFHGGYRCV DTNRCVEPYI QVSENRCLCP ASNPLCREQP SSIVHRYMTI TSERSVPADV
FQIQATSVYP GAYNAFQIRA GNSQGDFYIR QINNVSAMLV LARPVTGPRE YVLDLEMVTM
NSLMSYRASS VLRLTVFVGA YTF


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EIAAB14480 EFEMP1,EGF-containing fibulin-like extracellular matrix protein 1,Extracellular protein S1-5,FBLN3,FBNL,FIBL-3,Fibrillin-like protein,Fibulin-3,Homo sapiens,Human
EIAAB14479 Efemp1,EGF-containing fibulin-like extracellular matrix protein 1,Fbln3,FIBL-3,Fibulin-3,Mouse,Mus musculus
EIAAB14478 Efemp1,EGF-containing fibulin-like extracellular matrix protein 1,Fbln3,FIBL-3,Fibulin-3,Rat,Rattus norvegicus,T16 protein
EIAAB14481 Efemp2,EGF-containing fibulin-like extracellular matrix protein 2,Fbln4,FIBL-4,Fibulin-4,Mbp1,Mouse,Mus musculus,Mutant p53-binding protein 1
5213 EGF-containing fibulin-like extracellular matrix protein 1 0.1 mg
5213 EGF-containing fibulin-like extracellular matrix protein 1 0.5 mg
EFHA2 EFEMP2 Gene EGF-containing fibulin-like extracellular matrix protein 2
CSB-EL007450RA Rat EGF-containing fibulin-like extracellular matrix protein 1(EFEMP1) ELISA kit 96T
EFHA1 EFEMP1 Gene EGF-containing fibulin-like extracellular matrix protein 1
CSB-EL007450RA Rat EGF-containing fibulin-like extracellular matrix protein 1(EFEMP1) ELISA kit SpeciesRat 96T
CSB-EL007451HU Human EGF-containing fibulin-like extracellular matrix protein 2(EFEMP2) ELISA kit 96T
CSB-EL007450MO Mouse EGF-containing fibulin-like extracellular matrix protein 1(EFEMP1) ELISA kit 96T
CSB-EL007451MO Mouse EGF-containing fibulin-like extracellular matrix protein 2(EFEMP2) ELISA kit 96T
CSB-EL007450HU Human EGF-containing fibulin-like extracellular matrix protein 1(EFEMP1) ELISA kit 96T
CSB-EL007451HU Human EGF-containing fibulin-like extracellular matrix protein 2(EFEMP2) ELISA kit SpeciesHuman 96T
CSB-EL007450HU Human EGF-containing fibulin-like extracellular matrix protein 1(EFEMP1) ELISA kit SpeciesHuman 96T
CSB-EL007450MO Mouse EGF-containing fibulin-like extracellular matrix protein 1(EFEMP1) ELISA kit SpeciesMouse 96T
CSB-EL007451MO Mouse EGF-containing fibulin-like extracellular matrix protein 2(EFEMP2) ELISA kit SpeciesMouse 96T
FBLN4_MOUSE ELISA Kit FOR EGF-containing fibulin-like extracellular matrix protein 2; organism: Mouse; gene name: Efemp2 96T
FBLN3_MOUSE ELISA Kit FOR EGF-containing fibulin-like extracellular matrix protein 1; organism: Mouse; gene name: Efemp1 96T
CSB-EL007450RA Rat EGF-containing fibulin-like extracellular matrix protein 1 (EFEMP1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
32-155 Fibulin 5(FBLN5), with 448-amino acid protein (about 50kDa), is a recently discovered multifunctional extracellular matrix protein that mediates endothelial cell adhesion through integrin ligation, re 0.1 mL
32-156 Fibulin 5(FBLN5), with 448-amino acid protein (about 50kDa), is a recently discovered multifunctional extracellular matrix protein that mediates endothelial cell adhesion through integrin ligation, re 0.1 mL
EFMP-101AP EGF-containing fibulin-like extracellular matrix protein-1 (EFEMP1) Polyclonal anbtibody Host: Rabbit Affinity purifed 200ul


 

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