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Protein

Vitamin K-dependent gamma-carboxylase

Gene

GGCX

Organism
Ovis aries (Sheep)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

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.

Miscellaneous

The vitamin K-dependent protein substrates of carboxylase have usually a propeptide that binds to a high-affinity site on the carboxylase. CO2, O2 and reduced vitamin K are cosubstrates.

Catalytic activityi

[Peptidyl]-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O = [peptidyl]-glutamate + CO2 + O2 + phylloquinol.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin K-dependent gamma-carboxylase (EC:4.1.1.90)
Alternative name(s):
Gamma-glutamyl carboxylase
Peptidyl-glutamate 4-carboxylase
Vitamin K gamma glutamyl carboxylase
Gene namesi
Name:GGCX
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
Proteomesi
  • UP000002356 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 60CytoplasmicSequence analysisAdd BLAST59
Transmembranei61 – 81HelicalSequence analysisAdd BLAST21
Topological domaini82 – 113LumenalSequence analysisAdd BLAST32
Transmembranei114 – 134HelicalSequence analysisAdd BLAST21
Topological domaini135 – 136CytoplasmicSequence analysis2
Transmembranei137 – 157HelicalSequence analysisAdd BLAST21
Topological domaini158 – 292LumenalSequence analysisAdd BLAST135
Transmembranei293 – 313HelicalSequence analysisAdd BLAST21
Topological domaini314 – 361CytoplasmicSequence analysisAdd BLAST48
Transmembranei362 – 382HelicalSequence analysisAdd BLAST21
Topological domaini383 – 758LumenalSequence analysisAdd BLAST376

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001918272 – 758Vitamin K-dependent gamma-carboxylaseAdd BLAST757

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Disulfide bondi99 ↔ 450By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PRIDEiQ9GL59

Interactioni

Subunit structurei

Monomer. May interact with CALU.By similarity

Structurei

3D structure databases

SMRiQ9GL59
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG012798
KOiK10106

Family and domain databases

InterProiView protein in InterPro
IPR011020 HTTM
IPR011051 RmlC_Cupin_sf
IPR007782 VKG_COase
PANTHERiPTHR12639 PTHR12639, 1 hit
PfamiView protein in Pfam
PF05090 VKG_Carbox, 1 hit
SMARTiView protein in SMART
SM00752 HTTM, 1 hit
SUPFAMiSSF51182 SSF51182, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9GL59-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSARPARA PRGPDKVKKD KAAQTSGPRQ GSQMGKLLGF EWTDVSSWER
60 70 80 90 100
LVTLLNRPTD PASLAVFRFL FGLMMVLDIP QERGLSSLDR RYLDGLEVCR
110 120 130 140 150
FPLLDALQPL PLDWMYLVYT IMFLGALGMM LGLCYRISCV LFLLPYWYVF
160 170 180 190 200
LLDKTSWNNH SYLYGLLAFQ LTFVDAHHYW SVDGLLRARK RNAHVPLWNY
210 220 230 240 250
AVLRGQIFIV YFIAGIKKLD ADWVEGYSME YLSRHWLFSP FKLVLSEEMT
260 270 280 290 300
SLLVVHWCGL LLDLSAGFLL FFDASRPIGF VFVSYFHCMN SQLFSIGMFP
310 320 330 340 350
YVMLASSPLF CSPEWPRKLV AHCPKKLQEL LPLRTAPQPS TSCMYKRSRA
360 370 380 390 400
RGSQKPGLRH QLSTAFTLLY LLEQLFLPYS HFLTQGYNNW TNGLYGYSWD
410 420 430 440 450
MMVHSRSHQH VKITYRDGRT GELGYLNPGV FTQSRRWKDH ADMLKQYATC
460 470 480 490 500
LSRLLPKYNV TEPQIYFDIW VSINDRFQQR IFDPRVDIVQ AAWSPFQRTP
510 520 530 540 550
WLQPLLMDLS PWRTKLQEIK SSLDNHTEVV FIADFPGLHL ENFVSEDLGN
560 570 580 590 600
TSIQLLQGEV TVELVAEQKN QTLQEGEKMQ LPAGEYHKVY TVSSSPSCYM
610 620 630 640 650
YIYVNTTEVA LEQDLAYLQE LKEKVENGSE TGPLPPELQP LLEGEVKGGP
660 670 680 690 700
EPTPLVQTFL RRQQRLQEIE RRRNAPFYER FVRFLLRKLF IFRRSFLMTC
710 720 730 740 750
ISLRNLALGR PSLEQLAQEV TYANLRPFEP AGEPSPVNTD SSNPNPPEPD

SHPVHSEF
Length:758
Mass (Da):87,581
Last modified:March 1, 2001 - v1
Checksum:i87F8B58C187B9091
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF312035 mRNA Translation: AAG30935.1
RefSeqiNP_001009750.1, NM_001009750.1
UniGeneiOar.788

Genome annotation databases

GeneIDi443129
KEGGioas:443129

Similar proteinsi

Entry informationi

Entry nameiVKGC_SHEEP
AccessioniPrimary (citable) accession number: Q9GL59
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2001
Last modified: May 23, 2018
This is version 72 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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