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Multiple coagulation factor deficiency protein 2 (Neural stem cell-derived neuronal survival protein)

 MCFD2_HUMAN             Reviewed;         146 AA.
Q8NI22; A8K7W2; D6W5A9; E9PD95; Q53SS3; Q68D61; Q8N3M5;
21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
18-JUL-2018, entry version 142.
RecName: Full=Multiple coagulation factor deficiency protein 2;
AltName: Full=Neural stem cell-derived neuronal survival protein;
Flags: Precursor;
Name=MCFD2; Synonyms=SDNSF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart;
Toda H., Tashiro K., Takahashi J., Hashimoto N., Nakano I., Kobuke K.,
Tsuji M., Honjo T.;
"Isolation and characterization of SDNSF, a novel secretory molecule
with neuronal survival effect, from adult rat hippocampal stem
cells.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
INTERACTION WITH LMAN1, FUNCTION, AND VARIANTS F5F8D2 GLU-129 AND
THR-136.
PubMed=12717434; DOI=10.1038/ng1153;
Zhang B., Cunningham M.A., Nichols W.C., Bernat J.A., Seligsohn U.,
Pipe S.W., McVey J.H., Schulte-Overberg U., de Bosch N.B.,
Ruiz-Saez A., White G.C., Tuddenham E.G., Kaufman R.J., Ginsburg D.;
"Bleeding due to disruption of a cargo-specific ER-to-Golgi transport
complex.";
Nat. Genet. 34:220-225(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Melanoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Skin;
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[11]
STRUCTURE BY NMR OF 27-146, DOMAIN, CHARACTERIZATION OF VARIANTS
F5F8D2 GLU-129 AND THR-136, AND CALCIUM-BINDING.
PubMed=18590741; DOI=10.1016/j.jmb.2008.06.042;
Guy J.E., Wigren E., Svaerd M., Haerd T., Lindqvist Y.;
"New insights into multiple coagulation factor deficiency from the
solution structure of human MCFD2.";
J. Mol. Biol. 381:941-955(2008).
[12]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 58-146 IN COMPLEX WITH
LMAN1, AND SUBUNIT.
PubMed=20138881; DOI=10.1016/j.febslet.2010.02.009;
Wigren E., Bourhis J.M., Kursula I., Guy J.E., Lindqvist Y.;
"Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex
provides insight into combined deficiency of factor V and factor
VIII.";
FEBS Lett. 584:878-882(2010).
[13]
X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 27-146 IN COMPLEX WITH
LMAN1, SUBUNIT, AND CALCIUM-BINDING SITES.
PubMed=20142513; DOI=10.1073/pnas.0908526107;
Nishio M., Kamiya Y., Mizushima T., Wakatsuki S., Sasakawa H.,
Yamamoto K., Uchiyama S., Noda M., McKay A.R., Fukui K., Hauri H.P.,
Kato K.;
"Structural basis for the cooperative interplay between the two
causative gene products of combined factor V and factor VIII
deficiency.";
Proc. Natl. Acad. Sci. U.S.A. 107:4034-4039(2010).
[14]
VARIANT F5F8D2 ASN-135.
PubMed=18685427; DOI=10.1097/MBC.0b013e3283061103;
Ivaskevicius V., Windyga J., Baran B., Bykowska K., Daugela L.,
Watzka M., Seifried E., Oldenburg J.;
"The first case of combined coagulation factor V and coagulation
factor VIII deficiency in Poland due to a novel p.Tyr135Asn missense
mutation in the MCFD2 gene.";
Blood Coagul. Fibrinolysis 19:531-534(2008).
[15]
VARIANT F5F8D2 HIS-81.
PubMed=20491958; DOI=10.1111/j.1365-2516.2010.02268.x;
Abdallah H.E., Gouider E., Amor M.B., Jlizi A., Meddeb B.,
Elgaaied A.;
"Molecular analysis in two Tunisian families with combined factor V
and factor VIII deficiency.";
Haemophilia 16:801-804(2010).
-!- FUNCTION: The MCFD2-LMAN1 complex forms a specific cargo receptor
for the ER-to-Golgi transport of selected proteins. Plays a role
in the secretion of coagulation factors.
{ECO:0000269|PubMed:12717434}.
-!- SUBUNIT: Interacts in a calcium-dependent manner with LMAN1.
{ECO:0000269|PubMed:12717434, ECO:0000269|PubMed:20138881,
ECO:0000269|PubMed:20142513}.
-!- INTERACTION:
P49257:LMAN1; NbExp=9; IntAct=EBI-2689785, EBI-1057738;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
compartment {ECO:0000269|PubMed:12717434}. Endoplasmic reticulum
{ECO:0000269|PubMed:12717434}. Golgi apparatus
{ECO:0000269|PubMed:12717434}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8NI22-1; Sequence=Displayed;
Name=2;
IsoId=Q8NI22-2; Sequence=VSP_043815;
Name=3;
IsoId=Q8NI22-3; Sequence=VSP_043814;
-!- DOMAIN: Essentially unstructured in the absence of calcium ions.
Requires calcium ions for folding. {ECO:0000269|PubMed:18590741}.
-!- DISEASE: Factor V and factor VIII combined deficiency 2 (F5F8D2)
[MIM:613625]: A blood coagulation disorder characterized by
bleeding symptoms similar to those in hemophilia or
parahemophilia, that are caused by single deficiency of FV or
FVIII, respectively. The most common symptoms are epistaxis,
menorrhagia, and excessive bleeding during or after trauma. Plasma
levels of coagulation factors V and VIII are in the range of 5 to
30% of normal. {ECO:0000269|PubMed:12717434,
ECO:0000269|PubMed:18590741, ECO:0000269|PubMed:18685427,
ECO:0000269|PubMed:20491958}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=CAD38756.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF475284; AAM28465.1; -; mRNA.
EMBL; AF537214; AAP23162.1; -; mRNA.
EMBL; AK292127; BAF84816.1; -; mRNA.
EMBL; AL833900; CAD38756.1; ALT_INIT; mRNA.
EMBL; CR749562; CAH18359.1; -; mRNA.
EMBL; AC016722; AAY15013.1; -; Genomic_DNA.
EMBL; AC093732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471053; EAX00230.1; -; Genomic_DNA.
EMBL; CH471053; EAX00231.1; -; Genomic_DNA.
EMBL; CH471053; EAX00232.1; -; Genomic_DNA.
EMBL; CH471053; EAX00233.1; -; Genomic_DNA.
EMBL; BC037845; AAH37845.1; -; mRNA.
EMBL; BC040357; AAH40357.1; -; mRNA.
CCDS; CCDS33192.1; -. [Q8NI22-1]
CCDS; CCDS54354.1; -. [Q8NI22-2]
CCDS; CCDS54355.1; -. [Q8NI22-3]
PIR; JS0027; JS0027.
RefSeq; NP_001164977.1; NM_001171506.2. [Q8NI22-1]
RefSeq; NP_001164978.1; NM_001171507.2. [Q8NI22-1]
RefSeq; NP_001164979.1; NM_001171508.2. [Q8NI22-1]
RefSeq; NP_001164980.1; NM_001171509.2. [Q8NI22-2]
RefSeq; NP_001164981.1; NM_001171510.2. [Q8NI22-2]
RefSeq; NP_001164982.1; NM_001171511.2. [Q8NI22-3]
RefSeq; NP_644808.1; NM_139279.5. [Q8NI22-1]
UniGene; Hs.662152; -.
PDB; 2VRG; NMR; -; A=27-146.
PDB; 3A4U; X-ray; 1.84 A; B=27-146.
PDB; 3LCP; X-ray; 2.45 A; C/D=58-146.
PDB; 3WHT; X-ray; 1.80 A; B=67-146.
PDB; 3WHU; X-ray; 2.60 A; B=67-146.
PDB; 3WNX; X-ray; 2.75 A; B=67-146.
PDB; 4YGB; X-ray; 1.60 A; B/D=67-146.
PDB; 4YGC; X-ray; 2.40 A; B/D/F/H=67-146.
PDB; 4YGD; X-ray; 2.51 A; B/D/F/H=67-146.
PDB; 4YGE; X-ray; 3.05 A; B/D/F=27-146.
PDBsum; 2VRG; -.
PDBsum; 3A4U; -.
PDBsum; 3LCP; -.
PDBsum; 3WHT; -.
PDBsum; 3WHU; -.
PDBsum; 3WNX; -.
PDBsum; 4YGB; -.
PDBsum; 4YGC; -.
PDBsum; 4YGD; -.
PDBsum; 4YGE; -.
ProteinModelPortal; Q8NI22; -.
SMR; Q8NI22; -.
BioGrid; 124712; 42.
DIP; DIP-56233N; -.
IntAct; Q8NI22; 9.
MINT; Q8NI22; -.
STRING; 9606.ENSP00000317271; -.
DrugBank; DB00025; Antihemophilic Factor (Recombinant).
iPTMnet; Q8NI22; -.
PhosphoSitePlus; Q8NI22; -.
BioMuta; MCFD2; -.
DMDM; 49036425; -.
EPD; Q8NI22; -.
MaxQB; Q8NI22; -.
PaxDb; Q8NI22; -.
PeptideAtlas; Q8NI22; -.
PRIDE; Q8NI22; -.
ProteomicsDB; 73813; -.
ProteomicsDB; 73814; -. [Q8NI22-2]
ProteomicsDB; 73815; -. [Q8NI22-3]
TopDownProteomics; Q8NI22-1; -. [Q8NI22-1]
DNASU; 90411; -.
Ensembl; ENST00000319466; ENSP00000317271; ENSG00000180398. [Q8NI22-1]
Ensembl; ENST00000409105; ENSP00000386651; ENSG00000180398. [Q8NI22-1]
Ensembl; ENST00000409147; ENSP00000387082; ENSG00000180398. [Q8NI22-2]
Ensembl; ENST00000409207; ENSP00000386386; ENSG00000180398. [Q8NI22-1]
Ensembl; ENST00000409218; ENSP00000386261; ENSG00000180398. [Q8NI22-1]
Ensembl; ENST00000409800; ENSP00000387202; ENSG00000180398. [Q8NI22-2]
Ensembl; ENST00000409913; ENSP00000386941; ENSG00000180398. [Q8NI22-2]
Ensembl; ENST00000409973; ENSP00000386279; ENSG00000180398. [Q8NI22-1]
Ensembl; ENST00000412438; ENSP00000402717; ENSG00000180398. [Q8NI22-1]
Ensembl; ENST00000444761; ENSP00000394647; ENSG00000180398. [Q8NI22-3]
GeneID; 90411; -.
KEGG; hsa:90411; -.
UCSC; uc002rvk.4; human. [Q8NI22-1]
CTD; 90411; -.
DisGeNET; 90411; -.
EuPathDB; HostDB:ENSG00000180398.11; -.
GeneCards; MCFD2; -.
HGNC; HGNC:18451; MCFD2.
HPA; CAB022410; -.
HPA; HPA034593; -.
MalaCards; MCFD2; -.
MIM; 607788; gene.
MIM; 613625; phenotype.
neXtProt; NX_Q8NI22; -.
OpenTargets; ENSG00000180398; -.
Orphanet; 35909; Combined deficiency of factor V and factor VIII.
PharmGKB; PA134925788; -.
eggNOG; KOG4065; Eukaryota.
eggNOG; ENOG41124J6; LUCA.
GeneTree; ENSGT00390000003130; -.
HOGENOM; HOG000113497; -.
HOVERGEN; HBG060762; -.
InParanoid; Q8NI22; -.
KO; K20364; -.
OMA; ISHVHKE; -.
OrthoDB; EOG091G0ZJA; -.
PhylomeDB; Q8NI22; -.
TreeFam; TF315801; -.
Reactome; R-HSA-204005; COPII-mediated vesicle transport.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-948021; Transport to the Golgi and subsequent modification.
ChiTaRS; MCFD2; human.
EvolutionaryTrace; Q8NI22; -.
GeneWiki; MCFD2; -.
GenomeRNAi; 90411; -.
PRO; PR:Q8NI22; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000180398; -.
CleanEx; HS_MCFD2; -.
ExpressionAtlas; Q8NI22; baseline and differential.
Genevisible; Q8NI22; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13499; EF-hand_7; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Complete proteome;
Disease mutation; Endoplasmic reticulum; ER-Golgi transport;
Golgi apparatus; Metal-binding; Phosphoprotein; Protein transport;
Reference proteome; Repeat; Signal; Transport.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 146 Multiple coagulation factor deficiency
protein 2.
/FTId=PRO_0000004159.
DOMAIN 68 103 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 116 146 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 81 92 1.
CA_BIND 129 140 2.
MOD_RES 106 106 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K5B3}.
VAR_SEQ 1 52 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_043815.
VAR_SEQ 1 50 MTMRSLLRTPFLCGLLWAFCAPGARAEEPAASFSQPGSMGL
DKNTVHDQE -> MLSVCSCRTSSGMRSQWPSARQRSSSLS
TFR (in isoform 3). {ECO:0000305}.
/FTId=VSP_043814.
VARIANT 81 81 D -> H (in F5F8D2; dbSNP:rs78289603).
{ECO:0000269|PubMed:20491958}.
/FTId=VAR_072245.
VARIANT 129 129 D -> E (in F5F8D2; interferes with
protein folding; dbSNP:rs137852913).
{ECO:0000269|PubMed:12717434,
ECO:0000269|PubMed:18590741}.
/FTId=VAR_019076.
VARIANT 135 135 Y -> N (in F5F8D2; dbSNP:rs748641905).
{ECO:0000269|PubMed:18685427}.
/FTId=VAR_072246.
VARIANT 136 136 I -> T (in F5F8D2; interferes with
protein folding; dbSNP:rs137852914).
{ECO:0000269|PubMed:12717434,
ECO:0000269|PubMed:18590741}.
/FTId=VAR_019077.
HELIX 70 78 {ECO:0000244|PDB:4YGB}.
STRAND 85 89 {ECO:0000244|PDB:4YGB}.
HELIX 90 97 {ECO:0000244|PDB:4YGB}.
STRAND 106 108 {ECO:0000244|PDB:2VRG}.
HELIX 114 128 {ECO:0000244|PDB:4YGB}.
STRAND 133 137 {ECO:0000244|PDB:4YGB}.
HELIX 138 142 {ECO:0000244|PDB:4YGB}.
SEQUENCE 146 AA; 16390 MW; EF3F3B28E5C7A8A8 CRC64;
MTMRSLLRTP FLCGLLWAFC APGARAEEPA ASFSQPGSMG LDKNTVHDQE HIMEHLEGVI
NKPEAEMSPQ ELQLHYFKMH DYDGNNLLDG LELSTAITHV HKEEGSEQAP LMSEDELINI
IDGVLRDDDK NNDGYIDYAE FAKSLQ


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CSB-EL013582RA Rat Multiple coagulation factor deficiency protein 2(MCFD2) ELISA kit 96T
orb81213 Human Multiple Coagulation Factor Deficiency 2 protein Proteins 5
EM645 Multiple coagulation factor deficiency protein 2 homolog Elisa Kit 96T
CSB-EL013582RA Rat Multiple coagulation factor deficiency protein 2(MCFD2) ELISA kit SpeciesRat 96T
CSB-EL013582HU Human Multiple coagulation factor deficiency protein 2(MCFD2) ELISA kit 96T
CSB-EL013582MO Mouse Multiple coagulation factor deficiency protein 2(MCFD2) ELISA kit 96T
CSB-EL013582HU Human Multiple coagulation factor deficiency protein 2(MCFD2) ELISA kit SpeciesHuman 96T
CSB-EL013582MO Mouse Multiple coagulation factor deficiency protein 2(MCFD2) ELISA kit SpeciesMouse 96T
MCFD2_RAT ELISA Kit FOR Multiple coagulation factor deficiency protein 2 homolog; organism: Rat; gene name: Mcfd2 96T
MCFD2_MOUSE ELISA Kit FOR Multiple coagulation factor deficiency protein 2 homolog; organism: Mouse; gene name: Mcfd2 96T
orb81213 Human Multiple Coagulation Factor Deficiency 2 protein MCFD2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (27-146 a.a.) and having mo 5
PRO-769 Recombinant Human Multiple Coagulation Factor Deficiency 2 1mg
PRO-769 Recombinant Human Multiple Coagulation Factor Deficiency 2 5µg
PRO-769 Recombinant Human Multiple Coagulation Factor Deficiency 2 25µg
pro-769 Recombinant Human Multiple Coagulation Factor Deficiency 2 1mg
pro-769 Recombinant Human Multiple Coagulation Factor Deficiency 2 5
pro-769 Recombinant Human Multiple Coagulation Factor Deficiency 2 25
RPR-769 Recombinant Human Multiple Coagulation Factor Deficiency 2 5
pro-769 Recombinant Human Multiple Coagulation Factor Deficiency 2 MCFD2 5
OETPRO769 Multiple Coagulation Factor Deficiency 2 Human Recombinant 5
7-05577 Recombinant Human Multiple Coagulation Factor Deficiency 2 1mg
MCHR2 MCFD2 Gene multiple coagulation factor deficiency 2
pro-769 Recombinant Human Multiple Coagulation Factor Deficiency 2 MCFD2 1mg
pro-769 Recombinant Human Multiple Coagulation Factor Deficiency 2 MCFD2 25


 

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