GGCX
entrez
2677
canonical
uniprot
P38435
canonical
ensembl
ENSG00000115486
resolver
ensp
ENSP00000233838
resolver
ensp
ENSP00000408045
resolver
ensp
ENSP00000508856
resolver
ensp
ENSP00000510264
resolver
ensp
ENSP00000566517
resolver
ensp
ENSP00000566518
resolver
ensp
ENSP00000748475
resolver
enst
ENST00000496962
resolver
genesymbol
GGCX
resolver
genesymbol_syn
GC
resolver
hgnc
HGNC:4247
resolver
uniprot
A0A8I5QJA4
resolver
uniprot
B4DMC5
resolver
uniprot
E9PEE1
resolver
uniprot
Q14415
resolver
uniprot
Q6GU45
resolver
uniprot_entry
A0A8I5QJA4_HUMAN
resolver
uniprot_entry
VKGC_HUMAN
resolver
uniprot_sec
B4DMC5
resolver
uniprot_sec
E9PEE1
resolver
uniprot_sec
Q14415
resolver
uniprot_sec
Q6GU45
resolver
activity_regulation
ACTIVITY REGULATION: Interacts with lipids such as phosphatidylcholine and cholesterol; this interaction is required for optimal carboxylation activity. {ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952}.
uniprot
proteins
amino_acid_sequence
MAVSAGSARTSPSSDKVQKDKAELISGPRQDSRIGKLLGFEWTDLSSWRRLVTLLNRPTDPASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSPFKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFSYVMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSVSCVYKRSRGKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQPLLMDLSPWRAKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTTSPSPSCYMYVYVNTTELALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNTPFHERFFRFLLRKLYVFRRSFLMTCISLRNLILGRPSLEQLAQEVTYANLRPFEAVGELNPSNTDSSHSNPPESNPDPVHSEF
uniprot
proteins
disease_involvement
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 variants affecting the gene represented in this entry.; DISEASE: Pseudoxanthoma elasticum-like disorder with multiple coagulation factor deficiency (PXECD) [MIM:610842]: An autosomal recessive disorder characterized by hyperlaxity of the skin involving the entire body. Important phenotypic differences with classical pseudoxanthoma elasticum 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. Detailed electron microscopic analyses revealed that alterations of elastic fibers as well as their mineralization are slightly different from those in classic pseudoxanthoma elasticum. {ECO:0000269|PubMed:17110937}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
4.1.1.90
uniprot
proteins
function
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). {ECO:0000269|PubMed:17073445, ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952}.
uniprot
proteins
mass_dalton
87561
uniprot
proteins
mutagenesis
MUTAGEN 160; /note="H->A: No effect on epoxidase activity. Impairs carboxylase activity."; /evidence="ECO:0000269|PubMed:17073445, ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952"; MUTAGEN 160; /note="H->K,R,N: Abolishes carboxylase activity."; /evidence="ECO:0000269|PubMed:39880037"; MUTAGEN 218; /note="K->A: Abolishes epoxidase activity. Impairs carboxylase activity."; /evidence="ECO:0000269|PubMed:17073445, ECO:0000269|PubMed:39880952"; MUTAGEN 287; /note="H->A: No effect on epoxidase activity."; /evidence="ECO:0000269|PubMed:17073445"; MUTAGEN 299; /note="F->S,A: Abolishes carboxylase activity. No effect on epoxidase activity."; /evidence="ECO:0000269|PubMed:39880037"; MUTAGEN 381; /note="H->A: No effect on epoxidase activity."; /evidence="ECO:0000269|PubMed:17073445"; MUTAGEN 395; /note="Y->F,A: Impairs carboxylase activity."; /evidence="ECO:0000269|PubMed:39880037"; MUTAGEN 401; /note="M->C,I,A: Abolishes carboxylase activity. No effect on epoxidase activity."; /evidence="ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952"; MUTAGEN 402; /note="M->C,I,A: Abolishes carboxylase activity. No effect on epoxidase activity."; /evidence="ECO:0000269|PubMed:39880037"; MUTAGEN 601; /note="Y->A: Abolishes carboxylase activity; when associated with A-603."; /evidence="ECO:0000269|PubMed:39880037"; MUTAGEN 603; /note="Y->A: Abolishes carboxylase activity; when associated with A-601."; /evidence="ECO:0000269|PubMed:39880037
uniprot
proteins
protein_family
Vitamin K-dependent gamma-carboxylase family
uniprot
proteins
pubmed
10910912
uniprot
proteins
pubmed
10934213
uniprot
proteins
pubmed
11071668
uniprot
proteins
pubmed
11570873
uniprot
proteins
pubmed
12963724
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15287948
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16011462
uniprot
proteins
pubmed
17073445
uniprot
proteins
pubmed
17110937
uniprot
proteins
pubmed
1749935
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
39880037
uniprot
proteins
pubmed
39880952
uniprot
proteins
pubmed
9166845
uniprot
proteins
pubmed
9845520
uniprot
proteins
sequence_length
758
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10910912}; Multi-pass membrane protein {ECO:0000269|PubMed:10910912, ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952}.
uniprot
proteins
transmembrane_region
TRANSMEM 65..80; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952, ECO:0007744|PDB:9BUM, ECO:0007744|PDB:9BUR, ECO:0007744|PDB:9BUX, ECO:0007744|PDB:9BVK, ECO:0007744|PDB:9BVL, ECO:0007744|PDB:9BVM, ECO:0007744|PDB:9BVO, ECO:0007744|PDB:9BVP, ECO:0007744|PDB:9BVQ, ECO:0007744|PDB:9BVR"; TRANSMEM 115..131; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952, ECO:0007744|PDB:9BUM, ECO:0007744|PDB:9BUR, ECO:0007744|PDB:9BUX, ECO:0007744|PDB:9BVK, ECO:0007744|PDB:9BVL, ECO:0007744|PDB:9BVM, ECO:0007744|PDB:9BVO, ECO:0007744|PDB:9BVP, ECO:0007744|PDB:9BVQ, ECO:0007744|PDB:9BVR"; TRANSMEM 137..150; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952, ECO:0007744|PDB:9BUM, ECO:0007744|PDB:9BUR, ECO:0007744|PDB:9BUX, ECO:0007744|PDB:9BVK, ECO:0007744|PDB:9BVL, ECO:0007744|PDB:9BVM, ECO:0007744|PDB:9BVO, ECO:0007744|PDB:9BVP, ECO:0007744|PDB:9BVQ, ECO:0007744|PDB:9BVR"; TRANSMEM 162..173; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952, ECO:0007744|PDB:9BUM, ECO:0007744|PDB:9BUR, ECO:0007744|PDB:9BUX, ECO:0007744|PDB:9BVK, ECO:0007744|PDB:9BVL, ECO:0007744|PDB:9BVM, ECO:0007744|PDB:9BVO, ECO:0007744|PDB:9BVP, ECO:0007744|PDB:9BVQ, ECO:0007744|PDB:9BVR"; TRANSMEM 202..216; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952, ECO:0007744|PDB:9BUM, ECO:0007744|PDB:9BUR, ECO:0007744|PDB:9BUX, ECO:0007744|PDB:9BVK, ECO:0007744|PDB:9BVL, ECO:0007744|PDB:9BVM, ECO:0007744|PDB:9BVO, ECO:0007744|PDB:9BVP, ECO:0007744|PDB:9BVQ, ECO:0007744|PDB:9BVR"; TRANSMEM 252..272; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952, ECO:0007744|PDB:9BUM, ECO:0007744|PDB:9BUR, ECO:0007744|PDB:9BUX, ECO:0007744|PDB:9BVK, ECO:0007744|PDB:9BVL, ECO:0007744|PDB:9BVM, ECO:0007744|PDB:9BVO, ECO:0007744|PDB:9BVP, ECO:0007744|PDB:9BVQ, ECO:0007744|PDB:9BVR"; TRANSMEM 277..289; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952, ECO:0007744|PDB:9BUM, ECO:0007744|PDB:9BUR, ECO:0007744|PDB:9BUX, ECO:0007744|PDB:9BVK, ECO:0007744|PDB:9BVL, ECO:0007744|PDB:9BVM, ECO:0007744|PDB:9BVO, ECO:0007744|PDB:9BVP, ECO:0007744|PDB:9BVQ, ECO:0007744|PDB:9BVR"; TRANSMEM 296..305; /note="Helical; Name=8"; /evidence="ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952, ECO:0007744|PDB:9BUM, ECO:0007744|PDB:9BUR, ECO:0007744|PDB:9BUX, ECO:0007744|PDB:9BVK, ECO:0007744|PDB:9BVL, ECO:0007744|PDB:9BVM, ECO:0007744|PDB:9BVO, ECO:0007744|PDB:9BVP, ECO:0007744|PDB:9BVQ, ECO:0007744|PDB:9BVR"; TRANSMEM 365..377; /note="Helical; Name=9"; /evidence="ECO:0000269|PubMed:39880037, ECO:0000269|PubMed:39880952, ECO:0007744|PDB:9BUM, ECO:0007744|PDB:9BUR, ECO:0007744|PDB:9BUX, ECO:0007744|PDB:9BVK, ECO:0007744|PDB:9BVL, ECO:0007744|PDB:9BVM, ECO:0007744|PDB:9BVO, ECO:0007744|PDB:9BVP, ECO:0007744|PDB:9BVQ, ECO:0007744|PDB:9BVR
uniprot
proteins