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Adhesion G-protein coupled receptor G6 (Developmentally regulated G-protein-coupled receptor) (G-protein coupled receptor 126) (Vascular inducible G protein-coupled receptor) [Cleaved into: ADGRG6 N-terminal fragment (ADGRG6-NTF); ADGRG6 C-terminal fragment (ADGRG6-CTF)]

 AGRG6_HUMAN             Reviewed;        1221 AA.
Q86SQ4; Q5TGN7; Q6DHZ4; Q6F3F5; Q6F3F6; Q6F3F7; Q6F3F8; Q6MZU7;
Q8IXA4; Q8NC14; Q96JW0;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 3.
07-JUN-2017, entry version 144.
RecName: Full=Adhesion G-protein coupled receptor G6;
AltName: Full=Developmentally regulated G-protein-coupled receptor {ECO:0000303|PubMed:15189448};
AltName: Full=G-protein coupled receptor 126;
AltName: Full=Vascular inducible G protein-coupled receptor {ECO:0000303|PubMed:15225624};
Contains:
RecName: Full=ADGRG6 N-terminal fragment;
Short=ADGRG6-NTF;
Contains:
RecName: Full=ADGRG6 C-terminal fragment;
Short=ADGRG6-CTF;
Flags: Precursor;
Name=ADGRG6 {ECO:0000312|HGNC:HGNC:13841};
Synonyms=DREG, GPR126, VIGR;
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 4), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, INDUCTION, AND GLYCOSYLATION.
TISSUE=Vein;
PubMed=15225624; DOI=10.1016/j.febslet.2004.05.038;
Stehlik C., Kroismayr R., Dorfleutner A., Binder B.R., Lipp J.;
"VIGR -- a novel inducible adhesion family G-protein coupled receptor
in endothelial cells.";
FEBS Lett. 569:149-155(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), PROTEIN SEQUENCE
OF 469-483 AND 841-845, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-468;
SER-469; CYS-803; CYS-822; CYS-835; CYS-837 AND THR-841, PROTEOLYTIC
PROCESSING, CLEAVAGE BY FURIN-LIKE CONVERTASE, AND VARIANT ARG-1127.
PubMed=15189448; DOI=10.1111/j.1356-9597.2004.00743.x;
Moriguchi T., Haraguchi K., Ueda N., Okada M., Furuya T., Akiyama T.;
"DREG, a developmentally regulated G protein-coupled receptor
containing two conserved proteolytic cleavage sites.";
Genes Cells 9:549-560(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
ARG-1127.
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS
GLN-230 AND ARG-1127.
TISSUE=Placenta;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 646-1221, AND VARIANT
ARG-1127.
TISSUE=Placenta;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 710-1221 (ISOFORM 3), AND VARIANT
ARG-1127.
PubMed=12565841; DOI=10.1016/S0006-291X(03)00026-3;
Fredriksson R., Gloriam D.E.I., Hoeglund P.J., Lagerstroem M.C.,
Schioeth H.B.;
"There exist at least 30 human G-protein-coupled receptors with long
Ser/Thr-rich N-termini.";
Biochem. Biophys. Res. Commun. 301:725-734(2003).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1032-1221, AND VARIANT ARG-1127.
Ji D., Cheng J., Wang J., Dong J., Yang Q., Dang X., Liu Y.;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-324.
TISSUE=Bile;
PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
"A proteomic analysis of human bile.";
Mol. Cell. Proteomics 3:715-728(2004).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-143; ASN-438 AND ASN-445.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[11]
INVOLVEMENT IN STATURE AS A QUANTITATIVE TRAIT.
PubMed=18391950; DOI=10.1038/ng.125;
Lettre G., Jackson A.U., Gieger C., Schumacher F.R., Berndt S.I.,
Sanna S., Eyheramendy S., Voight B.F., Butler J.L., Guiducci C.,
Illig T., Hackett R., Heid I.M., Jacobs K.B., Lyssenko V., Uda M.,
Boehnke M., Chanock S.J., Groop L.C., Hu F.B., Isomaa B., Kraft P.,
Peltonen L., Salomaa V., Schlessinger D., Hunter D.J., Hayes R.B.,
Abecasis G.R., Wichmann H.-E., Mohlke K.L., Hirschhorn J.N.;
"Identification of ten loci associated with height highlights new
biological pathways in human growth.";
Nat. Genet. 40:584-591(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1165, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=24227709; DOI=10.1523/JNEUROSCI.1809-13.2013;
Mogha A., Benesh A.E., Patra C., Engel F.B., Schoeneberg T.,
Liebscher I., Monk K.R.;
"Gpr126 functions in Schwann cells to control differentiation and
myelination via G-protein activation.";
J. Neurosci. 33:17976-17985(2013).
[14]
STACHEL MOTIF, AND MUTAGENESIS OF SER-813; GLY-815; ASN-818 AND
THR-819.
PubMed=25533341; DOI=10.1016/j.celrep.2014.11.036;
Liebscher I., Schoen J., Petersen S.C., Fischer L., Auerbach N.,
Demberg L.M., Mogha A., Coester M., Simon K.U., Rothemund S.,
Monk K.R., Schoeneberg T.;
"A tethered agonist within the ectodomain activates the adhesion G
protein-coupled receptors GPR126 and GPR133.";
Cell Rep. 9:2018-2026(2014).
[15]
FUNCTION, INVOLVEMENT IN LCCS9, VARIANTS LCCS9 GLU-741 AND GLU-769,
AND CHARACTERIZATION OF VARIANT LCCS9 GLU-741.
PubMed=26004201; DOI=10.1016/j.ajhg.2015.04.014;
Ravenscroft G., Nolent F., Rajagopalan S., Meireles A.M.,
Paavola K.J., Gaillard D., Alanio E., Buckland M., Arbuckle S.,
Krivanek M., Maluenda J., Pannell S., Gooding R., Ong R.W.,
Allcock R.J., Carvalho E.D., Carvalho M.D., Kok F., Talbot W.S.,
Melki J., Laing N.G.;
"Mutations of GPR126 are responsible for severe arthrogryposis
multiplex congenita.";
Am. J. Hum. Genet. 96:955-961(2015).
[16]
VARIANT GLN-1057, AND CHARACTERIZATION OF VARIANT GLN-1057.
PubMed=27509131; DOI=10.1371/journal.pone.0160765;
Kitagaki J., Miyauchi S., Asano Y., Imai A., Kawai S., Michikami I.,
Yamashita M., Yamada S., Kitamura M., Murakami S.;
"A Putative association of a single nucleotide polymorphism in GPR126
with aggressive periodontitis in a japanese population.";
PLoS ONE 11:E0160765-E0160765(2016).
-!- FUNCTION: 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). {ECO:0000250|UniProtKB:C6KFA3,
ECO:0000269|PubMed:24227709, ECO:0000269|PubMed:26004201}.
-!- SUBUNIT: 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.
{ECO:0000250|UniProtKB:Q6F3F9}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15189448,
ECO:0000269|PubMed:15225624, ECO:0000269|PubMed:24227709}; Multi-
pass membrane protein {ECO:0000255}. Note=Detected on the cell
surface of activated but not resting umbilical vein.
{ECO:0000269|PubMed:15225624}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q86SQ4-1; Sequence=Displayed;
Name=2;
IsoId=Q86SQ4-2; Sequence=VSP_010747;
Name=3;
IsoId=Q86SQ4-3; Sequence=VSP_010748;
Name=4;
IsoId=Q86SQ4-4; Sequence=VSP_010747, VSP_010748;
-!- TISSUE SPECIFICITY: Expressed in placenta and to a lower extent in
pancreas and liver. Detected in aortic endothelial cells but not
in skin microvascular endothelial cells.
{ECO:0000269|PubMed:15225624}.
-!- INDUCTION: Up-regulated by bacterial lipopolysaccharides (LPS) and
thrombin, but not by other inflammatory stimuli in primary
umbilical veins. {ECO:0000269|PubMed:15225624}.
-!- DOMAIN: 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. {ECO:0000269|PubMed:25533341}.
-!- PTM: 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. {ECO:0000269|PubMed:15189448,
ECO:0000269|PubMed:26004201}.
-!- PTM: Highly glycosylated. {ECO:0000269|PubMed:15225624}.
-!- POLYMORPHISM: Genetic variations in ADGRG6 influences stature as a
quantitative trait (STQTL) [MIM: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. {ECO:0000269|PubMed:18391950}.
-!- DISEASE: Lethal congenital contracture syndrome 9 (LCCS9)
[MIM:616503]: A 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. {ECO:0000269|PubMed:26004201}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
Adhesion G-protein coupled receptor (ADGR) subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAO13250.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
Sequence=BAB55406.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC11393.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAE45930.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAI20053.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF216967; AAO13250.1; ALT_SEQ; mRNA.
EMBL; AB183546; BAD27571.1; -; mRNA.
EMBL; AB183547; BAD27572.1; -; mRNA.
EMBL; AB183548; BAD27573.1; -; mRNA.
EMBL; AB183549; BAD27574.1; -; mRNA.
EMBL; BX640971; CAE45986.1; -; mRNA.
EMBL; BX640873; CAE45930.1; ALT_INIT; mRNA.
EMBL; AL033377; CAI20053.1; ALT_SEQ; Genomic_DNA.
EMBL; AL360007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC075798; AAH75798.1; -; mRNA.
EMBL; AK027843; BAB55406.1; ALT_INIT; mRNA.
EMBL; AK075087; BAC11393.1; ALT_INIT; mRNA.
EMBL; AY181244; AAO27356.1; -; mRNA.
EMBL; AY426673; AAR88427.1; -; mRNA.
CCDS; CCDS47489.1; -. [Q86SQ4-3]
CCDS; CCDS47490.1; -. [Q86SQ4-1]
CCDS; CCDS47491.1; -. [Q86SQ4-2]
CCDS; CCDS55064.1; -. [Q86SQ4-4]
RefSeq; NP_001027566.1; NM_001032394.2.
RefSeq; NP_001027567.1; NM_001032395.2.
RefSeq; NP_065188.4; NM_020455.5.
RefSeq; NP_940971.1; NM_198569.2.
UniGene; Hs.743302; -.
ProteinModelPortal; Q86SQ4; -.
SMR; Q86SQ4; -.
BioGrid; 121449; 1.
STRING; 9606.ENSP00000356581; -.
MEROPS; P02.017; -.
iPTMnet; Q86SQ4; -.
PhosphoSitePlus; Q86SQ4; -.
SwissPalm; Q86SQ4; -.
BioMuta; GPR126; -.
DMDM; 215274152; -.
MaxQB; Q86SQ4; -.
PaxDb; Q86SQ4; -.
PeptideAtlas; Q86SQ4; -.
PRIDE; Q86SQ4; -.
Ensembl; ENST00000230173; ENSP00000230173; ENSG00000112414. [Q86SQ4-1]
Ensembl; ENST00000296932; ENSP00000296932; ENSG00000112414. [Q86SQ4-2]
Ensembl; ENST00000367608; ENSP00000356580; ENSG00000112414. [Q86SQ4-4]
Ensembl; ENST00000367609; ENSP00000356581; ENSG00000112414. [Q86SQ4-3]
GeneID; 57211; -.
KEGG; hsa:57211; -.
UCSC; uc010khc.4; human. [Q86SQ4-1]
CTD; 57211; -.
DisGeNET; 57211; -.
GeneCards; ADGRG6; -.
HGNC; HGNC:13841; ADGRG6.
HPA; HPA017346; -.
MalaCards; ADGRG6; -.
MIM; 606255; phenotype.
MIM; 612243; gene.
MIM; 616503; phenotype.
neXtProt; NX_Q86SQ4; -.
OpenTargets; ENSG00000112414; -.
PharmGKB; PA134878328; -.
eggNOG; KOG3714; Eukaryota.
eggNOG; KOG4193; Eukaryota.
eggNOG; ENOG410XSD2; LUCA.
GeneTree; ENSGT00830000128227; -.
HOVERGEN; HBG051778; -.
InParanoid; Q86SQ4; -.
KO; K08463; -.
OMA; NLSCGSY; -.
OrthoDB; EOG091G00P5; -.
PhylomeDB; Q86SQ4; -.
TreeFam; TF321769; -.
SignaLink; Q86SQ4; -.
ChiTaRS; GPR126; human.
GeneWiki; GPR126; -.
GenomeRNAi; 57211; -.
PRO; PR:Q86SQ4; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112414; -.
CleanEx; HS_GPR126; -.
ExpressionAtlas; Q86SQ4; baseline and differential.
Genevisible; Q86SQ4; HS.
GO; GO:0016021; C:integral component of membrane; TAS:GDB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
GO; GO:0050840; F:extracellular matrix binding; ISS:UniProtKB.
GO; GO:0004930; F:G-protein coupled receptor activity; IMP:UniProtKB.
GO; GO:0043236; F:laminin binding; ISS:UniProtKB.
GO; GO:0019933; P:cAMP-mediated signaling; IMP:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0060347; P:heart trabecula formation; IEA:Ensembl.
GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
GO; GO:0042552; P:myelination; IMP:UniProtKB.
GO; GO:0022011; P:myelination in peripheral nervous system; ISS:UniProtKB.
GO; GO:0010579; P:positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0014037; P:Schwann cell differentiation; IMP:UniProtKB.
CDD; cd00041; CUB; 1.
Gene3D; 2.60.120.290; -; 1.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR000859; CUB_dom.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
InterPro; IPR000203; GPS.
InterPro; IPR001759; Pentraxin-related.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF00431; CUB; 1.
Pfam; PF01825; GPS; 1.
Pfam; PF00354; Pentaxin; 1.
PRINTS; PR00249; GPCRSECRETIN.
SMART; SM00042; CUB; 1.
SMART; SM00303; GPS; 1.
SMART; SM00159; PTX; 1.
SUPFAM; SSF49854; SSF49854; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS01180; CUB; 1.
PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PROSITE; PS50221; GPS; 1.
PROSITE; PS51828; PTX_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Signal; Transducer;
Transmembrane; Transmembrane helix.
SIGNAL 1 37 {ECO:0000255}.
CHAIN 38 1221 Adhesion G-protein coupled receptor G6.
/FTId=PRO_0000012902.
CHAIN 38 840 ADGRG6 N-terminal fragment.
{ECO:0000305|PubMed:15189448}.
/FTId=PRO_0000438596.
CHAIN 841 1221 ADGRG6 C-terminal fragment.
{ECO:0000305|PubMed:15189448}.
/FTId=PRO_0000438597.
TOPO_DOM 38 862 Extracellular. {ECO:0000255}.
TRANSMEM 863 883 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 884 903 Cytoplasmic. {ECO:0000255}.
TRANSMEM 904 924 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 925 929 Extracellular. {ECO:0000255}.
TRANSMEM 930 950 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 951 970 Cytoplasmic. {ECO:0000255}.
TRANSMEM 971 991 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 992 1024 Extracellular. {ECO:0000255}.
TRANSMEM 1025 1045 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 1046 1069 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1070 1090 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 1091 1092 Extracellular. {ECO:0000255}.
TRANSMEM 1093 1113 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 1114 1221 Cytoplasmic. {ECO:0000255}.
DOMAIN 41 149 CUB. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 154 356 Pentraxin (PTX). {ECO:0000255|PROSITE-
ProRule:PRU01172}.
DOMAIN 800 852 GPS. {ECO:0000255|PROSITE-
ProRule:PRU00098}.
REGION 41 852 Inhibits receptor signaling in absence of
type IV collagen.
{ECO:0000250|UniProtKB:C6KFA3}.
REGION 41 355 Mediates interaction with type IV
collagen. {ECO:0000250|UniProtKB:C6KFA3}.
REGION 473 837 Mediates interaction with laminin-2.
{ECO:0000250|UniProtKB:Q6F3F9}.
MOTIF 842 850 Stachel. {ECO:0000269|PubMed:25533341}.
COMPBIAS 1153 1205 Ser-rich.
SITE 467 468 Cleavage; by furin like-convertase.
{ECO:0000269|PubMed:15189448}.
SITE 840 841 Cleavage. {ECO:0000269|PubMed:15189448}.
MOD_RES 1165 1165 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1168 1168 Phosphoserine.
{ECO:0000250|UniProtKB:Q6F3F9}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 143 143 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 314 314 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15084671}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 438 438 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 445 445 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 452 452 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 485 485 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 488 488 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 505 505 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 563 563 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 593 593 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 600 600 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 605 605 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 667 667 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 673 673 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 695 695 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 704 704 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 750 750 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 776 776 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 811 811 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 818 818 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 67 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 94 111 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 186 254 {ECO:0000255|PROSITE-ProRule:PRU01172}.
VAR_SEQ 380 407 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:15189448,
ECO:0000303|PubMed:15225624,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_010747.
VAR_SEQ 1193 1221 NVSYEHSFNKSGSLRQCFHGQVLVKTGPC -> SASMDKSL
SKLAHADGDQTSIIPVHQVIDKVKGYCNAHSDNFYKNIIMS
DTFSHSTKF (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:12565841,
ECO:0000303|PubMed:15189448,
ECO:0000303|PubMed:15225624,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010748.
VARIANT 123 123 S -> G (in dbSNP:rs17280293).
/FTId=VAR_054128.
VARIANT 230 230 K -> Q (in dbSNP:rs11155242).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_024478.
VARIANT 741 741 V -> E (in LCCS9; decreases the
autoprocessing/cleavage of the receptor).
{ECO:0000269|PubMed:26004201}.
/FTId=VAR_075146.
VARIANT 769 769 V -> E (in LCCS9; dbSNP:rs793888525).
{ECO:0000269|PubMed:26004201}.
/FTId=VAR_075147.
VARIANT 1057 1057 R -> Q (found in patients with aggressive
periodontitis; impairs cAMP production;
abrogates osteoblastic differentiation;
dbSNP:rs536714306).
{ECO:0000269|PubMed:27509131}.
/FTId=VAR_076965.
VARIANT 1127 1127 Q -> R (in dbSNP:rs1262686).
{ECO:0000269|PubMed:12565841,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15189448,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|Ref.8}.
/FTId=VAR_054129.
MUTAGEN 468 468 R->A: No cleavage.
{ECO:0000269|PubMed:15189448}.
MUTAGEN 469 469 S->A: No effect on cleavage.
{ECO:0000269|PubMed:15189448}.
MUTAGEN 803 803 C->S: No cleavage and not detected at the
cell surface.
{ECO:0000269|PubMed:15189448}.
MUTAGEN 813 813 S->A: No effect on G-protein-mediated
cAMP release.
{ECO:0000269|PubMed:25533341}.
MUTAGEN 815 815 G->A: Abolishes G-protein-mediated cAMP
release. {ECO:0000269|PubMed:25533341}.
MUTAGEN 818 818 N->A: Abolishes G-protein-mediated cAMP
release. {ECO:0000269|PubMed:25533341}.
MUTAGEN 819 819 T->A: Abolishes G-protein-mediated cAMP
release. {ECO:0000269|PubMed:25533341}.
MUTAGEN 822 822 C->S: No cleavage and not detected at the
cell surface.
{ECO:0000269|PubMed:15189448}.
MUTAGEN 835 835 C->S: No cleavage and not detected at the
cell surface.
{ECO:0000269|PubMed:15189448}.
MUTAGEN 837 837 C->S: No cleavage and not detected at the
cell surface.
{ECO:0000269|PubMed:15189448}.
MUTAGEN 841 841 T->A: No cleavage but detected at cell
surface. {ECO:0000269|PubMed:15189448}.
MUTAGEN 841 841 T->P: No cleavage and not detected at the
cell surface.
{ECO:0000269|PubMed:15189448}.
CONFLICT 622 622 N -> S (in Ref. 3; CAE45986).
{ECO:0000305}.
CONFLICT 623 623 I -> V (in Ref. 3; CAE45930).
{ECO:0000305}.
CONFLICT 708 708 F -> S (in Ref. 3; CAE45986).
{ECO:0000305}.
CONFLICT 763 763 K -> Q (in Ref. 3; CAE45930).
{ECO:0000305}.
CONFLICT 908 908 L -> P (in Ref. 5; AAH75798).
{ECO:0000305}.
SEQUENCE 1221 AA; 136695 MW; 1950DE5AE648F1C4 CRC64;
MMFRSDRMWS CHWKWKPSPL LFLFALYIMC VPHSVWGCAN CRVVLSNPSG TFTSPCYPND
YPNSQACMWT LRAPTGYIIQ ITFNDFDIEE APNCIYDSLS LDNGESQTKF CGATAKGLSF
NSSANEMHVS FSSDFSIQKK GFNASYIRVA VSLRNQKVIL PQTSDAYQVS VAKSISIPEL
SAFTLCFEAT KVGHEDSDWT AFSYSNASFT QLLSFGKAKS GYFLSISDSK CLLNNALPVK
EKEDIFAESF EQLCLVWNNS LGSIGVNFKR NYETVPCDST ISKVIPGNGK LLLGSNQNEI
VSLKGDIYNF RLWNFTMNAK ILSNLSCNVK GNVVDWQNDF WNIPNLALKA ESNLSCGSYL
IPLPAAELAS CADLGTLCQA TVNSPSTTPP TVTTNMPVTN RIDKQRNDGI IYRISVVIQN
ILRHPEVKVQ SKVAEWLNST FQNWNYTVYV VNISFHLSAG EDKIKVKRSL EDEPRLVLWA
LLVYNATNNT NLEGKIIQQK LLKNNESLDE GLRLHTVNVR QLGHCLAMEE PKGYYWPSIQ
PSEYVLPCPD KPGFSASRIC FYNATNPLVT YWGPVDISNC LKEANEVANQ ILNLTADGQN
LTSANITNIV EQVKRIVNKE ENIDITLGST LMNIFSNILS SSDSDLLESS SEALKTIDEL
AFKIDLNSTS HVNITTRNLA LSVSSLLPGT NAISNFSIGL PSNNESYFQM DFESGQVDPL
ASVILPPNLL ENLSPEDSVL VRRAQFTFFN KTGLFQDVGP QRKTLVSYVM ACSIGNITIQ
NLKDPVQIKI KHTRTQEVHH PICAFWDLNK NKSFGGWNTS GCVAHRDSDA SETVCLCNHF
THFGVLMDLP RSASQLDARN TKVLTFISYI GCGISAIFSA ATLLTYVAFE KLRRDYPSKI
LMNLSTALLF LNLLFLLDGW ITSFNVDGLC IAVAVLLHFF LLATFTWMGL EAIHMYIALV
KVFNTYIRRY ILKFCIIGWG LPALVVSVVL ASRNNNEVYG KESYGKEKGD EFCWIQDPVI
FYVTCAGYFG VMFFLNIAMF IVVMVQICGR NGKRSNRTLR EEVLRNLRSV VSLTFLLGMT
WGFAFFAWGP LNIPFMYLFS IFNSLQGLFI FIFHCAMKEN VQKQWRQHLC CGRFRLADNS
DWSKTATNII KKSSDNLGKS LSSSSIGSNS TYLTSKSKSS STTYFKRNSH TDNVSYEHSF
NKSGSLRQCF HGQVLVKTGP C


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