Overview
| Uniprot ID | P38435 |
|---|
| Protein Name | Vitamin K-dependent gamma-carboxylase |
|---|
| Gene Name | GGCX |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 21 |
SDKVQKDKAELISGP |
Function
Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant epoxidation of vitamin K hydroquinone to vitamin K epoxide (PubMed:17073445, PubMed:39880952, PubMed:39880037). Couples epoxidation and carboxylation in the same active site (PubMed:39880952, PubMed:39880037). Catalyzes gamma-carboxylation of blood coagulation factors (F2, F7, F9 and F10) and anticoagulants such as PROC, which are essential for thrombosis(PubMed:17073445, PubMed:39880037). Catalyzes gamma-carboxylation of osteocalcin/BGLAP, which is essential for bone metabolism (PubMed:17073445, PubMed:39880952). Catalyzes gamma-carboxylation of matrix Gla protein (MGP) and other transmembrane gamma-Gla proteins such as PRRG2, which are essential for calcium homeostasis and haemostasis (PubMed:17073445, PubMed:39880037)
Protein Sequence
10
MAVSAGSART
20
SPSSDKVQKD
30
KAELISGPRQ
40
DSRIGKLLGF
50
EWTDLSSWRR
60
LVTLLNRPTD
70
PASLAVFRFL
80
FGFLMVLDIP
90
QERGLSSLDR
100
KYLDGLDVCR
110
FPLLDALRPL
120
PLDWMYLVYT
130
IMFLGALGMM
140
LGLCYRISCV
150
LFLLPYWYVF
160
LLDKTSWNNH
170
SYLYGLLAFQ
180
LTFMDANHYW
190
SVDGLLNAHR
200
RNAHVPLWNY
210
AVLRGQIFIV
220
YFIAGVKKLD
230
ADWVEGYSME
240
YLSRHWLFSP
250
FKLLLSEELT
260
SLLVVHWGGL
270
LLDLSAGFLL
280
FFDVSRSIGL
290
FFVSYFHCMN
300
SQLFSIGMFS
310
YVMLASSPLF
320
CSPEWPRKLV
330
SYCPRRLQQL
340
LPLKAAPQPS
350
VSCVYKRSRG
360
KSGQKPGLRH
370
QLGAAFTLLY
380
LLEQLFLPYS
390
HFLTQGYNNW
400
TNGLYGYSWD
410
MMVHSRSHQH
420
VKITYRDGRT
430
GELGYLNPGV
440
FTQSRRWKDH
450
ADMLKQYATC
460
LSRLLPKYNV
470
TEPQIYFDIW
480
VSINDRFQQR
490
IFDPRVDIVQ
500
AAWSPFQRTS
510
WVQPLLMDLS
520
PWRAKLQEIK
530
SSLDNHTEVV
540
FIADFPGLHL
550
ENFVSEDLGN
560
TSIQLLQGEV
570
TVELVAEQKN
580
QTLREGEKMQ
590
LPAGEYHKVY
600
TTSPSPSCYM
610
YVYVNTTELA
620
LEQDLAYLQE
630
LKEKVENGSE
640
TGPLPPELQP
650
LLEGEVKGGP
660
EPTPLVQTFL
670
RRQQRLQEIE
680
RRRNTPFHER
690
FFRFLLRKLY
700
VFRRSFLMTC
710
ISLRNLILGR
720
PSLEQLAQEV
730
TYANLRPFEA
740
VGELNPSNTD
750
SSHSNPPESN
PDPVHSEF
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005788 |
endoplasmic reticulum lumen |
| Cellular Component |
GO:0005789 |
endoplasmic reticulum membrane |
| Cellular Component |
GO:0016020 |
membrane |
| Molecular Function |
GO:0008488 |
gamma-glutamyl carboxylase activity |
| Molecular Function |
GO:0008289 |
lipid binding |
| Molecular Function |
GO:0019842 |
vitamin binding |
| Biological Process |
GO:0007596 |
blood coagulation |
| Biological Process |
GO:1903011 |
negative regulation of bone development |
| Biological Process |
GO:0046929 |
negative regulation of neurotransmitter secretion |
| Biological Process |
GO:2000225 |
negative regulation of testosterone biosynthetic process |
| Biological Process |
GO:0017187 |
peptidyl-glutamic acid carboxylation |
| Biological Process |
GO:0051604 |
protein maturation |
| Biological Process |
GO:0036211 |
protein modification process |
| Biological Process |
GO:0042373 |
vitamin K metabolic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.