Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Vitamin K-dependent gamma-carboxylase (EC 4.1.1.90) (Gamma-glutamyl carboxylase) (Peptidyl-glutamate 4-carboxylase) (Vitamin K gamma glutamyl carboxylase)

 VKGC_HUMAN              Reviewed;         758 AA.
P38435; B4DMC5; E9PEE1; Q14415; Q6GU45;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 2.
20-JUN-2018, entry version 167.
RecName: Full=Vitamin K-dependent gamma-carboxylase;
EC=4.1.1.90 {ECO:0000269|PubMed:17073445};
AltName: Full=Gamma-glutamyl carboxylase;
AltName: Full=Peptidyl-glutamate 4-carboxylase;
AltName: Full=Vitamin K gamma glutamyl carboxylase;
Name=GGCX; Synonyms=GC;
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), AND VARIANT GLN-325.
PubMed=1749935; DOI=10.1126/science.1749935;
Wu S.-M., Cheung W.-F., Frazier D., Stafford D.W.;
"Cloning and expression of the cDNA for human gamma-glutamyl
carboxylase.";
Science 254:1634-1636(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9166845;
Wu S.-M., Stafford D.W., Frazier L.D., Fu Y.Y., High K.A., Chu K.,
Sanchez-Vega B., Solera J.;
"Genomic sequence and transcription start site for the human gamma-
glutamyl carboxylase.";
Blood 89:4058-4062(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Ying L., Lipsky J.J.;
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
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 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 MRNA] (ISOFORM 1).
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).
[7]
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=10910912;
Tie J., Wu S.-M., Jin D., Nicchitta C.V., Stafford D.W.;
"A topological study of the human gamma-glutamyl carboxylase.";
Blood 96:973-978(2000).
[8]
PROPEPTIDE INTERACTION, AND MONOMER.
PubMed=11570873; DOI=10.1021/bi010332w;
Presnell S.R., Tripathy A., Lentz B.R., Jin D.Y., Stafford D.W.;
"A novel fluorescence assay to study propeptide interaction with
gamma-glutamyl carboxylase.";
Biochemistry 40:11723-11733(2001).
[9]
DISULFIDE BOND.
PubMed=12963724; DOI=10.1074/jbc.M309164200;
Tie J.K., Mutucumarana V.P., Straight D.L., Carrick K.L., Pope R.M.,
Stafford D.W.;
"Determination of disulfide bond assignment of human vitamin K-
dependent gamma-glutamyl carboxylase by matrix-assisted laser
desorption/ionization time-of-flight mass spectrometry.";
J. Biol. Chem. 278:45468-45475(2003).
[10]
REVIEW.
PubMed=16011462; DOI=10.1146/annurev.nutr.25.050304.092713;
Berkner K.L.;
"The vitamin K-dependent carboxylase.";
Annu. Rev. Nutr. 25:127-149(2005).
[11]
MUTAGENESIS OF HIS-160; LYS-218; HIS-287 AND HIS-381, ACTIVE SITE,
FUNCTION, CATALYTIC ACTIVITY, PH DEPENDENCE, AND REACTION MECHANISM.
PubMed=17073445; DOI=10.1021/bi0609523;
Rishavy M.A., Hallgren K.W., Yakubenko A.V., Shtofman R.L.,
Runge K.W., Berkner K.L.;
"Bronsted analysis reveals Lys218 as the carboxylase active site base
that deprotonates vitamin K hydroquinone to initiate vitamin K-
dependent protein carboxylation.";
Biochemistry 45:13239-13248(2006).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-459 AND ASN-550.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
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).
[16]
VARIANT VKCFD1 ARG-394.
PubMed=9845520;
Brenner B., Sanchez-Vega B., Wu S.M., Lanir N., Stafford D.W.,
Solera J.;
"A missense mutation in gamma-glutamyl carboxylase gene causes
combined deficiency of all vitamin K-dependent blood coagulation
factors.";
Blood 92:4554-4559(1998).
[17]
VARIANT VKCFD1 SER-501.
PubMed=11071668;
Spronk H.M.H., Farah R.A., Buchanan G.R., Vermeer C., Soute B.A.M.;
"Novel mutation in the gamma-glutamyl carboxylase gene resulting in
congenital combined deficiency of all vitamin K-dependent blood
coagulation factors.";
Blood 96:3650-3652(2000).
[18]
CHARACTERIZATION OF VARIANT VKCFD1 ARG-394.
PubMed=10934213; DOI=10.1074/jbc.M006808200;
Mutucumarana V.P., Stafford D.W., Stanley T.B., Jin D.-Y., Solera J.,
Brenner B., Azerad R., Wu S.-M.;
"Expression and characterization of the naturally occurring mutation
L394R in human gamma-glutamyl carboxylase.";
J. Biol. Chem. 275:32572-32577(2000).
[19]
VARIANT VKCFD1 PRO-485.
PubMed=15287948; DOI=10.1111/j.1365-2141.2004.05071.x;
Rost S., Fregin A., Koch D., Compes M., Mueller C.R., Oldenburg J.;
"Compound heterozygous mutations in the gamma-glutamyl carboxylase
gene cause combined deficiency of all vitamin K-dependent blood
coagulation factors.";
Br. J. Haematol. 126:546-549(2004).
[20]
VARIANTS PXEL-MCFD SER-299; CYS-476; HIS-476; SER-493 AND ARG-558.
PubMed=17110937; DOI=10.1038/sj.jid.5700610;
Vanakker O.M., Martin L., Gheduzzi D., Leroy B.P., Loeys B.L.,
Guerci V.I., Matthys D., Terry S.F., Coucke P.J.,
Pasquali-Ronchetti I., De Paepe A.;
"Pseudoxanthoma elasticum-like phenotype with cutis laxa and multiple
coagulation factor deficiency represents a separate genetic entity.";
J. Invest. Dermatol. 127:581-587(2007).
-!- FUNCTION: Mediates the vitamin K-dependent carboxylation of
glutamate residues to calcium-binding gamma-carboxyglutamate (Gla)
residues with the concomitant conversion of the reduced
hydroquinone form of vitamin K to vitamin K epoxide.
{ECO:0000269|PubMed:17073445}.
-!- CATALYTIC ACTIVITY: [Peptidyl]-4-carboxyglutamate + 2,3-
epoxyphylloquinone + H(2)O = [peptidyl]-glutamate + CO(2) + O(2) +
phylloquinol. {ECO:0000269|PubMed:17073445}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7. {ECO:0000269|PubMed:17073445};
-!- SUBUNIT: Monomer. May interact with CALU (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10910912}; Multi-pass membrane protein
{ECO:0000269|PubMed:10910912}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P38435-1; Sequence=Displayed;
Name=2;
IsoId=P38435-2; Sequence=VSP_046179;
Note=No experimental confirmation available.;
-!- DISEASE: Combined deficiency of vitamin K-dependent clotting
factors 1 (VKCFD1) [MIM:277450]: VKCFD leads to a bleeding
tendency that is usually reversed by oral administration of
vitamin K. {ECO:0000269|PubMed:10934213,
ECO:0000269|PubMed:11071668, ECO:0000269|PubMed:15287948,
ECO:0000269|PubMed:9845520}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Pseudoxanthoma elasticum-like disorder with multiple
coagulation factor deficiency (PXEL-MCFD) [MIM:610842]:
Characterized by hyperlaxity of the skin involving the entire
body. Important phenotypic differences with classical PXE include
much more severe skin laxity with spreading toward the trunk and
limbs with thick, leathery skin folds rather than confinement to
flexural areas, and no decrease in visual acuity. Moreover,
detailed electron microscopic analyzes revealed that alterations
of elastic fibers as well as their mineralization are slightly
different from those in classic PXE.
{ECO:0000269|PubMed:17110937}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: The vitamin K-dependent protein substrates of
carboxylase have usually a propeptide that binds to a high-
affinity site on the carboxylase. CO(2), O(2) and reduced vitamin
K are cosubstrates.
-!- SIMILARITY: Belongs to the vitamin K-dependent gamma-carboxylase
family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M81592; AAA58643.1; -; mRNA.
EMBL; U65896; AAB39832.1; -; Genomic_DNA.
EMBL; L17128; AAA91834.1; -; mRNA.
EMBL; AK297397; BAG59837.1; -; mRNA.
EMBL; AC016753; AAY24340.1; -; Genomic_DNA.
EMBL; BC013979; AAH13979.1; -; mRNA.
CCDS; CCDS1978.1; -. [P38435-1]
CCDS; CCDS46353.1; -. [P38435-2]
PIR; A39283; A39283.
RefSeq; NP_000812.2; NM_000821.6. [P38435-1]
RefSeq; NP_001135741.1; NM_001142269.3. [P38435-2]
UniGene; Hs.77719; -.
ProteinModelPortal; P38435; -.
BioGrid; 108945; 16.
IntAct; P38435; 20.
MINT; P38435; -.
STRING; 9606.ENSP00000233838; -.
ChEMBL; CHEMBL2012; -.
DrugBank; DB01125; Anisindione.
DrugBank; DB00100; Coagulation Factor IX (Recombinant).
DrugBank; DB00036; Coagulation factor VIIa Recombinant Human.
DrugBank; DB00055; Drotrecogin alfa.
DrugBank; DB00142; L-Glutamic Acid.
DrugBank; DB00170; Menadione.
DrugBank; DB01022; Phylloquinone.
iPTMnet; P38435; -.
PhosphoSitePlus; P38435; -.
BioMuta; GGCX; -.
DMDM; 84028279; -.
EPD; P38435; -.
MaxQB; P38435; -.
PaxDb; P38435; -.
PeptideAtlas; P38435; -.
PRIDE; P38435; -.
ProteomicsDB; 55296; -.
DNASU; 2677; -.
Ensembl; ENST00000233838; ENSP00000233838; ENSG00000115486. [P38435-1]
Ensembl; ENST00000430215; ENSP00000408045; ENSG00000115486. [P38435-2]
GeneID; 2677; -.
KEGG; hsa:2677; -.
UCSC; uc002sps.4; human. [P38435-1]
CTD; 2677; -.
DisGeNET; 2677; -.
EuPathDB; HostDB:ENSG00000115486.11; -.
GeneCards; GGCX; -.
HGNC; HGNC:4247; GGCX.
HPA; HPA018284; -.
MalaCards; GGCX; -.
MIM; 137167; gene.
MIM; 277450; phenotype.
MIM; 610842; phenotype.
neXtProt; NX_P38435; -.
OpenTargets; ENSG00000115486; -.
Orphanet; 91135; Body skin hyperlaxity due to vitamin K-dependent coagulation factor deficiency.
Orphanet; 98434; Hereditary combined deficiency of vitamin K-dependent clotting factors.
PharmGKB; PA28660; -.
eggNOG; ENOG410IHG2; Eukaryota.
eggNOG; ENOG410XR5Q; LUCA.
GeneTree; ENSGT00390000014909; -.
HOGENOM; HOG000007593; -.
HOVERGEN; HBG012798; -.
InParanoid; P38435; -.
KO; K10106; -.
OMA; SPSCYMY; -.
OrthoDB; EOG091G07P8; -.
PhylomeDB; P38435; -.
TreeFam; TF323879; -.
BioCyc; MetaCyc:HS03897-MONOMER; -.
BRENDA; 4.1.1.90; 2681.
Reactome; R-HSA-159740; Gamma-carboxylation of protein precursors.
ChiTaRS; GGCX; human.
GeneWiki; Gamma-glutamyl_carboxylase; -.
GenomeRNAi; 2677; -.
PRO; PR:P38435; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115486; -.
CleanEx; HS_GC; -.
CleanEx; HS_GGCX; -.
ExpressionAtlas; P38435; baseline and differential.
Genevisible; P38435; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0008488; F:gamma-glutamyl carboxylase activity; TAS:Reactome.
GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
InterPro; IPR011020; HTTM.
InterPro; IPR011051; RmlC_Cupin_sf.
InterPro; IPR007782; VKG_COase.
PANTHER; PTHR12639; PTHR12639; 1.
Pfam; PF05090; VKG_Carbox; 1.
SMART; SM00752; HTTM; 1.
SUPFAM; SSF51182; SSF51182; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome;
Disease mutation; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
Lyase; Membrane; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692}.
CHAIN 2 758 Vitamin K-dependent gamma-carboxylase.
/FTId=PRO_0000191823.
TOPO_DOM 2 60 Cytoplasmic. {ECO:0000255}.
TRANSMEM 61 81 Helical. {ECO:0000255}.
TOPO_DOM 82 113 Lumenal. {ECO:0000255}.
TRANSMEM 114 134 Helical. {ECO:0000255}.
TOPO_DOM 135 136 Cytoplasmic. {ECO:0000255}.
TRANSMEM 137 157 Helical. {ECO:0000255}.
TOPO_DOM 158 292 Lumenal. {ECO:0000255}.
TRANSMEM 293 313 Helical. {ECO:0000255}.
TOPO_DOM 314 361 Cytoplasmic. {ECO:0000255}.
TRANSMEM 362 382 Helical. {ECO:0000255}.
TOPO_DOM 383 758 Lumenal. {ECO:0000255}.
ACT_SITE 218 218 Proton acceptor.
{ECO:0000269|PubMed:17073445}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692}.
CARBOHYD 459 459 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 550 550 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 99 450 {ECO:0000269|PubMed:12963724}.
VAR_SEQ 15 71 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046179.
VARIANT 299 299 F -> S (in PXEL-MCFD; dbSNP:rs121909677).
{ECO:0000269|PubMed:17110937}.
/FTId=VAR_032979.
VARIANT 325 325 R -> Q (in dbSNP:rs699664).
{ECO:0000269|PubMed:1749935}.
/FTId=VAR_005780.
VARIANT 394 394 L -> R (in VKCFD1; affects glutamate
binding; dbSNP:rs121909675).
{ECO:0000269|PubMed:10934213,
ECO:0000269|PubMed:9845520}.
/FTId=VAR_005781.
VARIANT 476 476 R -> C (in PXEL-MCFD; dbSNP:rs121909681).
{ECO:0000269|PubMed:17110937}.
/FTId=VAR_032980.
VARIANT 476 476 R -> H (in PXEL-MCFD; dbSNP:rs121909682).
{ECO:0000269|PubMed:17110937}.
/FTId=VAR_032981.
VARIANT 485 485 R -> P (in VKCFD1; dbSNP:rs121909676).
{ECO:0000269|PubMed:15287948}.
/FTId=VAR_021826.
VARIANT 493 493 W -> S (in PXEL-MCFD; dbSNP:rs121909679).
{ECO:0000269|PubMed:17110937}.
/FTId=VAR_032982.
VARIANT 501 501 W -> S (in VKCFD1; dbSNP:rs28928872).
{ECO:0000269|PubMed:11071668}.
/FTId=VAR_015218.
VARIANT 558 558 G -> R (in PXEL-MCFD; dbSNP:rs121909678).
{ECO:0000269|PubMed:17110937}.
/FTId=VAR_032983.
MUTAGEN 160 160 H->A: No effect on activity.
{ECO:0000269|PubMed:17073445}.
MUTAGEN 218 218 K->A: No activity.
{ECO:0000269|PubMed:17073445}.
MUTAGEN 287 287 H->A: No effect on activity.
{ECO:0000269|PubMed:17073445}.
MUTAGEN 381 381 H->A: No effect on activity.
{ECO:0000269|PubMed:17073445}.
CONFLICT 400 400 D -> N (in Ref. 3; AAA91834).
{ECO:0000305}.
CONFLICT 659 659 F -> S (in Ref. 4; BAG59837).
{ECO:0000305}.
SEQUENCE 758 AA; 87561 MW; 720D5B08E9B558C8 CRC64;
MAVSAGSART SPSSDKVQKD KAELISGPRQ DSRIGKLLGF EWTDLSSWRR LVTLLNRPTD
PASLAVFRFL FGFLMVLDIP QERGLSSLDR KYLDGLDVCR FPLLDALRPL PLDWMYLVYT
IMFLGALGMM LGLCYRISCV LFLLPYWYVF LLDKTSWNNH SYLYGLLAFQ LTFMDANHYW
SVDGLLNAHR RNAHVPLWNY AVLRGQIFIV YFIAGVKKLD ADWVEGYSME YLSRHWLFSP
FKLLLSEELT SLLVVHWGGL LLDLSAGFLL FFDVSRSIGL FFVSYFHCMN SQLFSIGMFS
YVMLASSPLF CSPEWPRKLV SYCPRRLQQL LPLKAAPQPS VSCVYKRSRG KSGQKPGLRH
QLGAAFTLLY LLEQLFLPYS HFLTQGYNNW TNGLYGYSWD MMVHSRSHQH VKITYRDGRT
GELGYLNPGV FTQSRRWKDH ADMLKQYATC LSRLLPKYNV TEPQIYFDIW VSINDRFQQR
IFDPRVDIVQ AAWSPFQRTS WVQPLLMDLS PWRAKLQEIK SSLDNHTEVV FIADFPGLHL
ENFVSEDLGN TSIQLLQGEV TVELVAEQKN QTLREGEKMQ LPAGEYHKVY TTSPSPSCYM
YVYVNTTELA LEQDLAYLQE LKEKVENGSE TGPLPPELQP LLEGEVKGGP EPTPLVQTFL
RRQQRLQEIE RRRNTPFHER FFRFLLRKLY VFRRSFLMTC ISLRNLILGR PSLEQLAQEV
TYANLRPFEA VGELNPSNTD SSHSNPPESN PDPVHSEF


Related products :

Catalog number Product name Quantity
EIAAB45818 Gamma-glutamyl carboxylase,GC,GGCX,Homo sapiens,Human,Peptidyl-glutamate 4-carboxylase,Vitamin K gamma glutamyl carboxylase,Vitamin K-dependent gamma-carboxylase
EIAAB45819 Gamma-glutamyl carboxylase,Ggcx,Peptidyl-glutamate 4-carboxylase,Rat,Rattus norvegicus,Vitamin K gamma glutamyl carboxylase,Vitamin K-dependent gamma-carboxylase
EIAAB45820 Gamma-glutamyl carboxylase,Ggcx,Mouse,Mus musculus,Peptidyl-glutamate 4-carboxylase,Vitamin K gamma glutamyl carboxylase,Vitamin K-dependent gamma-carboxylase
EIAAB45817 Bos taurus,Bovine,Gamma-glutamyl carboxylase,GC,GGCX,Peptidyl-glutamate 4-carboxylase,Vitamin K gamma glutamyl carboxylase,Vitamin K-dependent gamma-carboxylase
CSB-EL009388RA Rat Vitamin K-dependent gamma-carboxylase(GGCX) ELISA kit 96T
GGN GGCX Gene gamma-glutamyl carboxylase
CSB-EL009388RA Rat Vitamin K-dependent gamma-carboxylase(GGCX) ELISA kit SpeciesRat 96T
CSB-EL009388HU Human Vitamin K-dependent gamma-carboxylase(GGCX) ELISA kit 96T
CSB-EL009388MO Mouse Vitamin K-dependent gamma-carboxylase(GGCX) ELISA kit 96T
CSB-EL009388BO Bovine Vitamin K-dependent gamma-carboxylase(GGCX) ELISA kit 96T
201-20-2240 GGCX{gamma-glutamyl carboxylase}rabbit.pAb 0.2ml
VKGC_RAT ELISA Kit FOR Vitamin K-dependent gamma-carboxylase; organism: Rat; gene name: Ggcx 96T
CSB-EL009388SH Sheep Vitamin K-dependent gamma-carboxylase(GGCX) ELISA kit SpeciesSheep 96T
CSB-EL009388MO Mouse Vitamin K-dependent gamma-carboxylase(GGCX) ELISA kit SpeciesMouse 96T
CSB-EL009388BO Bovine Vitamin K-dependent gamma-carboxylase(GGCX) ELISA kit SpeciesBovine 96T
CSB-EL009388HU Human Vitamin K-dependent gamma-carboxylase(GGCX) ELISA kit SpeciesHuman 96T
E1386121 Sheep gamma-Glutamyl Carboxylase (GGCX) ELISA Kit 1
GS-0849a gamma-glutamyl carboxylase primary antibody, Host: Rabbit 200ul
CSB-EL009388RA Rat gamma-glutamyl carboxylase (GGCX) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL009388HU Human gamma-glutamyl carboxylase (GGCX) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL009388SH Sheep gamma-glutamyl carboxylase (GGCX) ELISA kit, Species Sheep, Sample Type serum, plasma 96T
CSB-EL009388MO Mouse gamma-glutamyl carboxylase (GGCX) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL009388BO Bovine gamma-glutamyl carboxylase (GGCX) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-PA009388GA01HU Rabbit anti-human gamma-glutamyl carboxylase polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-PA009388GA01HU Rabbit anti-human gamma-glutamyl carboxylase polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur