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Protein

Adhesion G-protein coupled receptor G6

Gene

ADGRG6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

G-protein coupled receptor which is activated by type IV collagen, a major constituent of the basement membrane (By similarity). Couples to G(i)-proteins as well as G(s)-proteins (PubMed:24227709). Essential for normal differentiation of promyelinating Schwann cells and for normal myelination of axons (PubMed:24227709). Regulates neural, cardiac and ear development via G-protein- and/or N-terminus-dependent signaling (By similarity). May act as a receptor for PRNP which may promote myelin homeostasis (By similarity).By similarity2 Publications

GO - Molecular functioni

  • collagen binding Source: UniProtKB
  • extracellular matrix binding Source: UniProtKB
  • G-protein coupled receptor activity Source: UniProtKB

GO - Biological processi

  • cAMP-mediated signaling Source: UniProtKB
  • cell surface receptor signaling pathway Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • myelination Source: UniProtKB
  • Schwann cell differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

SignaLinkiQ86SQ4.

Protein family/group databases

MEROPSiP02.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Adhesion G-protein coupled receptor G6
Alternative name(s):
Developmentally regulated G-protein-coupled receptor1 Publication
G-protein coupled receptor 126
Vascular inducible G protein-coupled receptor1 Publication
Cleaved into the following 2 chains:
ADGRG6 N-terminal fragment
Short name:
ADGRG6-NTF
ADGRG6 C-terminal fragment
Short name:
ADGRG6-CTF
Gene namesi
Name:ADGRG6Imported
Synonyms:DREG, GPR126, VIGR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:13841. ADGRG6.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini38 – 862ExtracellularSequence analysisAdd BLAST825
Transmembranei863 – 883Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini884 – 903CytoplasmicSequence analysisAdd BLAST20
Transmembranei904 – 924Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini925 – 929ExtracellularSequence analysis5
Transmembranei930 – 950Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini951 – 970CytoplasmicSequence analysisAdd BLAST20
Transmembranei971 – 991Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini992 – 1024ExtracellularSequence analysisAdd BLAST33
Transmembranei1025 – 1045Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini1046 – 1069CytoplasmicSequence analysisAdd BLAST24
Transmembranei1070 – 1090Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini1091 – 1092ExtracellularSequence analysis2
Transmembranei1093 – 1113Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini1114 – 1221CytoplasmicSequence analysisAdd BLAST108

GO - Cellular componenti

  • integral component of membrane Source: GDB
  • intracellular Source: GOC
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Lethal congenital contracture syndrome 9 (LCCS9)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy and congenital non-progressive joint contractures. The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth.
See also OMIM:616503
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075146741V → E in LCCS9; decreases the autoprocessing/cleavage of the receptor. 1 Publication1
Natural variantiVAR_075147769V → E in LCCS9. 1 PublicationCorresponds to variant rs793888525dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi468R → A: No cleavage. 1 Publication1
Mutagenesisi469S → A: No effect on cleavage. 1 Publication1
Mutagenesisi803C → S: No cleavage and not detected at the cell surface. 1 Publication1
Mutagenesisi813S → A: No effect on G-protein-mediated cAMP release. 1 Publication1
Mutagenesisi815G → A: Abolishes G-protein-mediated cAMP release. 1 Publication1
Mutagenesisi818N → A: Abolishes G-protein-mediated cAMP release. 1 Publication1
Mutagenesisi819T → A: Abolishes G-protein-mediated cAMP release. 1 Publication1
Mutagenesisi822C → S: No cleavage and not detected at the cell surface. 1 Publication1
Mutagenesisi835C → S: No cleavage and not detected at the cell surface. 1 Publication1
Mutagenesisi837C → S: No cleavage and not detected at the cell surface. 1 Publication1
Mutagenesisi841T → A: No cleavage but detected at cell surface. 1 Publication1
Mutagenesisi841T → P: No cleavage and not detected the cell surface. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi57211.
MIMi606255. phenotype.
616503. phenotype.
OpenTargetsiENSG00000112414.
PharmGKBiPA134878328.

Polymorphism and mutation databases

BioMutaiGPR126.
DMDMi215274152.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 37Sequence analysisAdd BLAST37
ChainiPRO_000001290238 – 1221Adhesion G-protein coupled receptor G6Add BLAST1184
ChainiPRO_000043859638 – 840ADGRG6 N-terminal fragment1 PublicationAdd BLAST803
ChainiPRO_0000438597841 – 1221ADGRG6 C-terminal fragment1 PublicationAdd BLAST381

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi41 ↔ 67PROSITE-ProRule annotation
Disulfide bondi94 ↔ 111PROSITE-ProRule annotation
Glycosylationi121N-linked (GlcNAc...)Sequence analysis1
Glycosylationi143N-linked (GlcNAc...)1 Publication1
Glycosylationi206N-linked (GlcNAc...)Sequence analysis1
Glycosylationi258N-linked (GlcNAc...)Sequence analysis1
Glycosylationi314N-linked (GlcNAc...)Sequence analysis1
Glycosylationi324N-linked (GlcNAc...)1 Publication1
Glycosylationi353N-linked (GlcNAc...)Sequence analysis1
Glycosylationi438N-linked (GlcNAc...)1 Publication1
Glycosylationi445N-linked (GlcNAc...)1 Publication1
Glycosylationi452N-linked (GlcNAc...)Sequence analysis1
Glycosylationi485N-linked (GlcNAc...)Sequence analysis1
Glycosylationi488N-linked (GlcNAc...)Sequence analysis1
Glycosylationi505N-linked (GlcNAc...)Sequence analysis1
Glycosylationi563N-linked (GlcNAc...)Sequence analysis1
Glycosylationi593N-linked (GlcNAc...)Sequence analysis1
Glycosylationi600N-linked (GlcNAc...)Sequence analysis1
Glycosylationi605N-linked (GlcNAc...)Sequence analysis1
Glycosylationi667N-linked (GlcNAc...)Sequence analysis1
Glycosylationi673N-linked (GlcNAc...)Sequence analysis1
Glycosylationi695N-linked (GlcNAc...)Sequence analysis1
Glycosylationi704N-linked (GlcNAc...)Sequence analysis1
Glycosylationi750N-linked (GlcNAc...)Sequence analysis1
Glycosylationi776N-linked (GlcNAc...)Sequence analysis1
Glycosylationi811N-linked (GlcNAc...)Sequence analysis1
Glycosylationi818N-linked (GlcNAc...)Sequence analysis1
Modified residuei1165PhosphoserineCombined sources1
Modified residuei1168PhosphoserineBy similarity1

Post-translational modificationi

Proteolytically cleaved into 2 conserved sites: one in the GPS domain (S1 site) and the other in the middle of the extracellular domain (S2 site). The proteolytic cleavage at S1 site generates an extracellular subunit and a seven-transmembrane subunit. Furin is involved in the cleavage of the S2 site generating a soluble fragment. Processing at the GPS domain occurred independent of and probably prior to the cleavage at the S2 site. Proteolytic cleavage is required for activation of the receptor.2 Publications
Highly glycosylated.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei467 – 468Cleavage; by furin like-convertase1 Publication2
Sitei840 – 841Cleavage1 Publication2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ86SQ4.
PaxDbiQ86SQ4.
PeptideAtlasiQ86SQ4.
PRIDEiQ86SQ4.

PTM databases

iPTMnetiQ86SQ4.
PhosphoSitePlusiQ86SQ4.
SwissPalmiQ86SQ4.

Expressioni

Tissue specificityi

Expressed in placenta and to a lower extent in pancreas and liver. Detected in aortic endothelial cells but not in skin microvascular endothelial cells.1 Publication

Inductioni

Up-regulated by bacterial lipopolysaccharides (LPS) and thrombin, but not by other inflammatory stimuli in primary umbilical veins.1 Publication

Gene expression databases

BgeeiENSG00000112414.
CleanExiHS_GPR126.
ExpressionAtlasiQ86SQ4. baseline and differential.
GenevisibleiQ86SQ4. HS.

Organism-specific databases

HPAiHPA017346.

Interactioni

Subunit structurei

Interacts with Laminin-2; this interaction stabilizes the receptor in an inactive state. Laminin-2 polymerization could facilitate ADGRG6-NTF removal, thereby exposing the tethered agonist to drive myelination. Interacts with PRNP.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi121449. 1 interactor.
STRINGi9606.ENSP00000356581.

Structurei

3D structure databases

ProteinModelPortaliQ86SQ4.
SMRiQ86SQ4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 149CUBPROSITE-ProRule annotationAdd BLAST109
Domaini150 – 355PentaxinAdd BLAST206
Domaini800 – 852GPSPROSITE-ProRule annotationAdd BLAST53

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni41 – 852Inhibits receptor signaling in absence of type IV collagenBy similarityAdd BLAST812
Regioni41 – 355Mediates interaction with type IV collagenBy similarityAdd BLAST315
Regioni473 – 837Mediates interaction with laminin-2By similarityAdd BLAST365

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi842 – 850Stachel1 Publication9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1153 – 1205Ser-richAdd BLAST53

Domaini

A short peptide sequence (termed the Stachel sequence) in the C-terminal part of the extra-cellular domain (ECD) functions as a tethered agonist. Upon structural changes within the ECD, e.g. due to extracellular ligand binding or mechanical movements, this intramolecular agonist is exposed to the 7TM domain, triggering G-protein activation.1 Publication

Sequence similaritiesi

Contains 1 CUB domain.PROSITE-ProRule annotation
Contains 1 GPS domain.PROSITE-ProRule annotation
Contains 1 pentaxin domain.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3714. Eukaryota.
KOG4193. Eukaryota.
ENOG410XSD2. LUCA.
GeneTreeiENSGT00830000128227.
HOVERGENiHBG051778.
InParanoidiQ86SQ4.
KOiK08463.
OMAiSCGSYLI.
OrthoDBiEOG091G00P5.
PhylomeDBiQ86SQ4.
TreeFamiTF321769.

Family and domain databases

CDDicd00041. CUB. 1 hit.
Gene3Di2.60.120.200. 1 hit.
2.60.120.290. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR000859. CUB_dom.
IPR017981. GPCR_2-like.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR001759. Pentaxin-related.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF00431. CUB. 1 hit.
PF01825. GPS. 1 hit.
PF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSiPR00249. GPCRSECRETIN.
SMARTiSM00042. CUB. 1 hit.
SM00303. GPS. 1 hit.
SM00159. PTX. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS01180. CUB. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86SQ4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MMFRSDRMWS CHWKWKPSPL LFLFALYIMC VPHSVWGCAN CRVVLSNPSG
60 70 80 90 100
TFTSPCYPND YPNSQACMWT LRAPTGYIIQ ITFNDFDIEE APNCIYDSLS
110 120 130 140 150
LDNGESQTKF CGATAKGLSF NSSANEMHVS FSSDFSIQKK GFNASYIRVA
160 170 180 190 200
VSLRNQKVIL PQTSDAYQVS VAKSISIPEL SAFTLCFEAT KVGHEDSDWT
210 220 230 240 250
AFSYSNASFT QLLSFGKAKS GYFLSISDSK CLLNNALPVK EKEDIFAESF
260 270 280 290 300
EQLCLVWNNS LGSIGVNFKR NYETVPCDST ISKVIPGNGK LLLGSNQNEI
310 320 330 340 350
VSLKGDIYNF RLWNFTMNAK ILSNLSCNVK GNVVDWQNDF WNIPNLALKA
360 370 380 390 400
ESNLSCGSYL IPLPAAELAS CADLGTLCQA TVNSPSTTPP TVTTNMPVTN
410 420 430 440 450
RIDKQRNDGI IYRISVVIQN ILRHPEVKVQ SKVAEWLNST FQNWNYTVYV
460 470 480 490 500
VNISFHLSAG EDKIKVKRSL EDEPRLVLWA LLVYNATNNT NLEGKIIQQK
510 520 530 540 550
LLKNNESLDE GLRLHTVNVR QLGHCLAMEE PKGYYWPSIQ PSEYVLPCPD
560 570 580 590 600
KPGFSASRIC FYNATNPLVT YWGPVDISNC LKEANEVANQ ILNLTADGQN
610 620 630 640 650
LTSANITNIV EQVKRIVNKE ENIDITLGST LMNIFSNILS SSDSDLLESS
660 670 680 690 700
SEALKTIDEL AFKIDLNSTS HVNITTRNLA LSVSSLLPGT NAISNFSIGL
710 720 730 740 750
PSNNESYFQM DFESGQVDPL ASVILPPNLL ENLSPEDSVL VRRAQFTFFN
760 770 780 790 800
KTGLFQDVGP QRKTLVSYVM ACSIGNITIQ NLKDPVQIKI KHTRTQEVHH
810 820 830 840 850
PICAFWDLNK NKSFGGWNTS GCVAHRDSDA SETVCLCNHF THFGVLMDLP
860 870 880 890 900
RSASQLDARN TKVLTFISYI GCGISAIFSA ATLLTYVAFE KLRRDYPSKI
910 920 930 940 950
LMNLSTALLF LNLLFLLDGW ITSFNVDGLC IAVAVLLHFF LLATFTWMGL
960 970 980 990 1000
EAIHMYIALV KVFNTYIRRY ILKFCIIGWG LPALVVSVVL ASRNNNEVYG
1010 1020 1030 1040 1050
KESYGKEKGD EFCWIQDPVI FYVTCAGYFG VMFFLNIAMF IVVMVQICGR
1060 1070 1080 1090 1100
NGKRSNRTLR EEVLRNLRSV VSLTFLLGMT WGFAFFAWGP LNIPFMYLFS
1110 1120 1130 1140 1150
IFNSLQGLFI FIFHCAMKEN VQKQWRQHLC CGRFRLADNS DWSKTATNII
1160 1170 1180 1190 1200
KKSSDNLGKS LSSSSIGSNS TYLTSKSKSS STTYFKRNSH TDNVSYEHSF
1210 1220
NKSGSLRQCF HGQVLVKTGP C
Length:1,221
Mass (Da):136,695
Last modified:November 25, 2008 - v3
Checksum:i1950DE5AE648F1C4
GO
Isoform 2 (identifier: Q86SQ4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     380-407: Missing.

Show »
Length:1,193
Mass (Da):133,671
Checksum:iEDE274EF3096A242
GO
Isoform 3 (identifier: Q86SQ4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1193-1221: NVSYEHSFNKSGSLRQCFHGQVLVKTGPC → SASMDKSLSK...SDTFSHSTKF

Show »
Length:1,250
Mass (Da):139,901
Checksum:iBDDABA6A755A445B
GO
Isoform 4 (identifier: Q86SQ4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     380-407: Missing.
     1193-1221: NVSYEHSFNKSGSLRQCFHGQVLVKTGPC → SASMDKSLSK...SDTFSHSTKF

Show »
Length:1,222
Mass (Da):136,878
Checksum:i7B50E167F0EBBA97
GO

Sequence cautioni

The sequence AAO13250 differs from that shown. Sequencing errors.Curated
The sequence BAB55406 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC11393 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAE45930 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI20053 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti622N → S in CAE45986 (PubMed:17974005).Curated1
Sequence conflicti623I → V in CAE45930 (PubMed:17974005).Curated1
Sequence conflicti708F → S in CAE45986 (PubMed:17974005).Curated1
Sequence conflicti763K → Q in CAE45930 (PubMed:17974005).Curated1
Sequence conflicti908L → P in AAH75798 (PubMed:15489334).Curated1

Polymorphismi

Genetic variations in ADGRG6 influences stature as a quantitative trait (STQTL) [MIMi:606255]. Adult height is an easily observable and highly heritable complex continuous trait. Because of this, it is a model trait for studying genetic influence on quantitative traits.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_054128123S → G.Corresponds to variant rs17280293dbSNPEnsembl.1
Natural variantiVAR_024478230K → Q.1 PublicationCorresponds to variant rs11155242dbSNPEnsembl.1
Natural variantiVAR_075146741V → E in LCCS9; decreases the autoprocessing/cleavage of the receptor. 1 Publication1
Natural variantiVAR_075147769V → E in LCCS9. 1 PublicationCorresponds to variant rs793888525dbSNPEnsembl.1
Natural variantiVAR_0769651057R → Q Found in patients with aggressive periodontitis; impairs cAMP production; abrogates osteoblastic differentiation. 1 Publication1
Natural variantiVAR_0541291127Q → R.6 PublicationsCorresponds to variant rs1262686dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_010747380 – 407Missing in isoform 2 and isoform 4. 4 PublicationsAdd BLAST28
Alternative sequenceiVSP_0107481193 – 1221NVSYE…KTGPC → SASMDKSLSKLAHADGDQTS IIPVHQVIDKVKGYCNAHSD NFYKNIIMSDTFSHSTKF in isoform 3 and isoform 4. 4 PublicationsAdd BLAST29

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF216967 mRNA. Translation: AAO13250.1. Sequence problems.
AB183546 mRNA. Translation: BAD27571.1.
AB183547 mRNA. Translation: BAD27572.1.
AB183548 mRNA. Translation: BAD27573.1.
AB183549 mRNA. Translation: BAD27574.1.
BX640971 mRNA. Translation: CAE45986.1.
BX640873 mRNA. Translation: CAE45930.1. Different initiation.
AL033377 Genomic DNA. Translation: CAI20053.1. Sequence problems.
AL360007 Genomic DNA. No translation available.
BC075798 mRNA. Translation: AAH75798.1.
AK027843 mRNA. Translation: BAB55406.1. Different initiation.
AK075087 mRNA. Translation: BAC11393.1. Different initiation.
AY181244 mRNA. Translation: AAO27356.1.
AY426673 mRNA. Translation: AAR88427.1.
CCDSiCCDS47489.1. [Q86SQ4-3]
CCDS47490.1. [Q86SQ4-1]
CCDS47491.1. [Q86SQ4-2]
CCDS55064.1. [Q86SQ4-4]
RefSeqiNP_001027566.1. NM_001032394.2.
NP_001027567.1. NM_001032395.2.
NP_065188.4. NM_020455.5.
NP_940971.1. NM_198569.2.
UniGeneiHs.743302.

Genome annotation databases

EnsembliENST00000230173; ENSP00000230173; ENSG00000112414. [Q86SQ4-1]
ENST00000296932; ENSP00000296932; ENSG00000112414. [Q86SQ4-2]
ENST00000367608; ENSP00000356580; ENSG00000112414. [Q86SQ4-4]
ENST00000367609; ENSP00000356581; ENSG00000112414. [Q86SQ4-3]
GeneIDi57211.
KEGGihsa:57211.
UCSCiuc010khc.4. human. [Q86SQ4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF216967 mRNA. Translation: AAO13250.1. Sequence problems.
AB183546 mRNA. Translation: BAD27571.1.
AB183547 mRNA. Translation: BAD27572.1.
AB183548 mRNA. Translation: BAD27573.1.
AB183549 mRNA. Translation: BAD27574.1.
BX640971 mRNA. Translation: CAE45986.1.
BX640873 mRNA. Translation: CAE45930.1. Different initiation.
AL033377 Genomic DNA. Translation: CAI20053.1. Sequence problems.
AL360007 Genomic DNA. No translation available.
BC075798 mRNA. Translation: AAH75798.1.
AK027843 mRNA. Translation: BAB55406.1. Different initiation.
AK075087 mRNA. Translation: BAC11393.1. Different initiation.
AY181244 mRNA. Translation: AAO27356.1.
AY426673 mRNA. Translation: AAR88427.1.
CCDSiCCDS47489.1. [Q86SQ4-3]
CCDS47490.1. [Q86SQ4-1]
CCDS47491.1. [Q86SQ4-2]
CCDS55064.1. [Q86SQ4-4]
RefSeqiNP_001027566.1. NM_001032394.2.
NP_001027567.1. NM_001032395.2.
NP_065188.4. NM_020455.5.
NP_940971.1. NM_198569.2.
UniGeneiHs.743302.

3D structure databases

ProteinModelPortaliQ86SQ4.
SMRiQ86SQ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121449. 1 interactor.
STRINGi9606.ENSP00000356581.

Protein family/group databases

MEROPSiP02.017.
GPCRDBiSearch...

PTM databases

iPTMnetiQ86SQ4.
PhosphoSitePlusiQ86SQ4.
SwissPalmiQ86SQ4.

Polymorphism and mutation databases

BioMutaiGPR126.
DMDMi215274152.

Proteomic databases

MaxQBiQ86SQ4.
PaxDbiQ86SQ4.
PeptideAtlasiQ86SQ4.
PRIDEiQ86SQ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000230173; ENSP00000230173; ENSG00000112414. [Q86SQ4-1]
ENST00000296932; ENSP00000296932; ENSG00000112414. [Q86SQ4-2]
ENST00000367608; ENSP00000356580; ENSG00000112414. [Q86SQ4-4]
ENST00000367609; ENSP00000356581; ENSG00000112414. [Q86SQ4-3]
GeneIDi57211.
KEGGihsa:57211.
UCSCiuc010khc.4. human. [Q86SQ4-1]

Organism-specific databases

CTDi57211.
DisGeNETi57211.
GeneCardsiADGRG6.
HGNCiHGNC:13841. ADGRG6.
HPAiHPA017346.
MIMi606255. phenotype.
612243. gene.
616503. phenotype.
neXtProtiNX_Q86SQ4.
OpenTargetsiENSG00000112414.
PharmGKBiPA134878328.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3714. Eukaryota.
KOG4193. Eukaryota.
ENOG410XSD2. LUCA.
GeneTreeiENSGT00830000128227.
HOVERGENiHBG051778.
InParanoidiQ86SQ4.
KOiK08463.
OMAiSCGSYLI.
OrthoDBiEOG091G00P5.
PhylomeDBiQ86SQ4.
TreeFamiTF321769.

Enzyme and pathway databases

SignaLinkiQ86SQ4.

Miscellaneous databases

ChiTaRSiGPR126. human.
GeneWikiiGPR126.
GenomeRNAii57211.
PROiQ86SQ4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000112414.
CleanExiHS_GPR126.
ExpressionAtlasiQ86SQ4. baseline and differential.
GenevisibleiQ86SQ4. HS.

Family and domain databases

CDDicd00041. CUB. 1 hit.
Gene3Di2.60.120.200. 1 hit.
2.60.120.290. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR000859. CUB_dom.
IPR017981. GPCR_2-like.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR001759. Pentaxin-related.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF00431. CUB. 1 hit.
PF01825. GPS. 1 hit.
PF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSiPR00249. GPCRSECRETIN.
SMARTiSM00042. CUB. 1 hit.
SM00303. GPS. 1 hit.
SM00159. PTX. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS01180. CUB. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAGRG6_HUMAN
AccessioniPrimary (citable) accession number: Q86SQ4
Secondary accession number(s): Q5TGN7
, Q6DHZ4, Q6F3F5, Q6F3F6, Q6F3F7, Q6F3F8, Q6MZU7, Q8IXA4, Q8NC14, Q96JW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.