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Megakaryocyte and platelet inhibitory receptor G6b (Protein G6b)

 G6B_HUMAN               Reviewed;         241 AA.
O95866; A2BEZ1; A2BEZ2; A2BEZ3; A2BEZ4; A2BEZ5; B0UXC4; B0UXC7;
B0UXC8; B0V024; B0V026; Q14CK2; Q96A86; Q96A87; Q96A88; Q96A89;
Q96A90; Q96A91;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
30-AUG-2017, entry version 127.
RecName: Full=Megakaryocyte and platelet inhibitory receptor G6b {ECO:0000312|HGNC:HGNC:13937};
AltName: Full=Protein G6b {ECO:0000305};
Flags: Precursor;
Name=MPIG6B {ECO:0000312|HGNC:HGNC:13937};
Synonyms=C6orf25 {ECO:0000312|HGNC:HGNC:13937},
G6B {ECO:0000312|HGNC:HGNC:13937}, G6B-B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:CAC83497.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D; E; F AND G),
INTERACTION WITH PTPN6 AND PTPN11, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, GLYCOSYLATION, PHOSPHORYLATION AT TYR-211, AND
MUTAGENESIS OF TYR-211 AND TYR-237.
TISSUE=T-cell;
PubMed=11544253; DOI=10.1074/jbc.M103214200;
de Vet E.C.M., Aguado B., Campbell R.D.;
"G6b, a novel immunoglobulin superfamily member encoded in the human
major histocompatibility complex, interacts with SHP-1 and SHP-2.";
J. Biol. Chem. 276:42070-42076(2001).
[2] {ECO:0000312|EMBL:AAD18075.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[3] {ECO:0000305, ECO:0000312|EMBL:BAB63378.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000305, ECO:0000312|EMBL:BAB63378.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000312|EMBL:CAI18408.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-175.
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM G).
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).
[7] {ECO:0000305}
PROTEIN SEQUENCE OF 18-30.
TISSUE=Platelet {ECO:0000269|PubMed:12665801};
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
HEPARIN-BINDING.
PubMed=15848171; DOI=10.1016/j.febslet.2005.03.032;
de Vet E.C., Newland S.A., Lyons P.A., Aguado B., Campbell R.D.;
"The cell surface receptor G6b, a member of the immunoglobulin
superfamily, binds heparin.";
FEBS Lett. 579:2355-2358(2005).
[9]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17311996; DOI=10.1182/blood-2006-09-047449;
Newland S.A., Macaulay I.C., Floto A.R., de Vet E.C., Ouwehand W.H.,
Watkins N.A., Lyons P.A., Campbell D.R.;
"The novel inhibitory receptor G6B is expressed on the surface of
platelets and attenuates platelet function in vitro.";
Blood 109:4806-4809(2007).
[10]
FUNCTION, DOMAIN, AND MUTAGENESIS OF TYR-211 AND TYR-237.
PubMed=18955485; DOI=10.1074/jbc.M806895200;
Mori J., Pearce A.C., Spalton J.C., Grygielska B., Eble J.A.,
Tomlinson M.G., Senis Y.A., Watson S.P.;
"G6b-B inhibits constitutive and agonist-induced signaling by
glycoprotein VI and CLEC-2.";
J. Biol. Chem. 283:35419-35427(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
GLYCOSYLATION, PHOSPHORYLATION, AND INTERACTION WITH PTPN6 AND PTPN11.
PubMed=23112346; DOI=10.1126/scisignal.2002936;
Mazharian A., Wang Y.J., Mori J., Bem D., Finney B., Heising S.,
Gissen P., White J.G., Berndt M.C., Gardiner E.E., Nieswandt B.,
Douglas M.R., Campbell R.D., Watson S.P., Senis Y.A.;
"Mice lacking the ITIM-containing receptor G6b-B exhibit
macrothrombocytopenia and aberrant platelet function.";
Sci. Signal. 5:RA78-RA78(2012).
[13]
INVOLVEMENT IN THAMY, VARIANT THAMY 108-CYS--VAL-241 DEL,
CHARACTERIZATION OF VARIANT THAMY 108-CYS--VAL-241 DEL, AND FUNCTION.
PubMed=27743390; DOI=10.1111/ejh.12819;
Melhem M., Abu-Farha M., Antony D., Madhoun A.A., Bacchelli C.,
Alkayal F., AlKhairi I., John S., Alomari M., Beales P.L., Alsmadi O.;
"Novel G6B gene variant causes familial autosomal recessive
thrombocytopenia and anemia.";
Eur. J. Haematol. 98:218-227(2017).
-!- FUNCTION: Inhibitory receptor that acts as a critical regulator of
hematopoietic lineage differentiation, megakaryocyte function and
platelet production (PubMed:12665801, PubMed:17311996,
PubMed:27743390). Inhibits platelet aggregation and activation by
agonists such as ADP and collagen-related peptide
(PubMed:12665801). This regulation of megakaryocate function as
well as platelet production ann activation is done through the
inhibition (via the 2 ITIM motifs) of the receptors CLEC1B and
GP6:FcRgamma signaling (PubMed:17311996). Appears to operate in a
calcium-independent manner (PubMed:12665801).
{ECO:0000269|PubMed:12665801, ECO:0000269|PubMed:17311996,
ECO:0000269|PubMed:27743390}.
-!- FUNCTION: Isoform B, displayed in this entry, is the only isoform
to contain both a transmembrane region and 2 immunoreceptor
tyrosine-based inhibitor motifs (ITIMs) and, thus, the only one
which probably has a role of inhibitory receptor. Isoform A may be
the activating counterpart of isoform B.
{ECO:0000305|PubMed:11544253}.
-!- SUBUNIT: Interacts (via ITIM motif) with PTPN6 and PTPN11
(PubMed:11544253, PubMed:23112346). Binds to heparin
(PubMed:15848171). {ECO:0000269|PubMed:11544253,
ECO:0000269|PubMed:15848171, ECO:0000269|PubMed:23112346,
ECO:0000305|PubMed:18955485}.
-!- SUBCELLULAR LOCATION: Isoform E: Endoplasmic reticulum
{ECO:0000269|PubMed:11544253}. Golgi apparatus
{ECO:0000269|PubMed:11544253}.
-!- SUBCELLULAR LOCATION: Isoform D: Endoplasmic reticulum
{ECO:0000269|PubMed:11544253}. Golgi apparatus
{ECO:0000269|PubMed:11544253}.
-!- SUBCELLULAR LOCATION: Isoform B: Cell membrane
{ECO:0000269|PubMed:11544253}; Single-pass type I membrane protein
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform A: Cell membrane
{ECO:0000269|PubMed:11544253}; Single-pass type I membrane protein
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=B {ECO:0000269|PubMed:11544253};
IsoId=O95866-1; Sequence=Displayed;
Name=A {ECO:0000269|PubMed:11544253};
IsoId=O95866-2; Sequence=VSP_014176;
Name=C {ECO:0000269|PubMed:11544253};
IsoId=O95866-3; Sequence=VSP_014174;
Name=D {ECO:0000269|PubMed:11544253};
IsoId=O95866-4; Sequence=VSP_014172;
Name=E {ECO:0000269|PubMed:11544253};
IsoId=O95866-5; Sequence=VSP_014173;
Name=F {ECO:0000269|PubMed:11544253};
IsoId=O95866-6; Sequence=VSP_014175;
Name=G {ECO:0000269|PubMed:11544253};
IsoId=O95866-7; Sequence=VSP_014177;
-!- TISSUE SPECIFICITY: Expressed in platelets. Expressed in a
restricted set of hematopoietic cell lines including the
erythroleukemia cell line K-562 and the T-cell leukemia cell lines
MOLT-4 and Jurkat. Not detected in the monocyte-like cell line U-
937, the B-cell-like cell line Raji, the fibroblast cell lines TK
and HeLa, or the natural killer cell lines NKL, NK 62 and YT.
{ECO:0000269|PubMed:11544253, ECO:0000269|PubMed:17311996}.
-!- DOMAIN: Isoform B, displayed in this entry, is the only one of the
isoforms to contain both a transmembrane region and 2 copies of a
cytoplasmic motif that is referred to as the immunoreceptor
tyrosine-based inhibitor motif (ITIM). This motif is involved in
modulation of cellular responses. The phosphorylated ITIM motif
can bind the SH2 domain of several SH2-containing phosphatases.
The 2 ITIM motifs of isoform B are required for the inhibition of
CLEC1B and GP6:FCER1G signaling and platelet activation.
{ECO:0000305|PubMed:18955485}.
-!- PTM: All isoforms are N-glycosylated.
{ECO:0000269|PubMed:11544253, ECO:0000269|PubMed:23112346}.
-!- PTM: Isoform E is O-glycosylated. {ECO:0000269|PubMed:11544253}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:11544253,
ECO:0000269|PubMed:23112346}.
-!- DISEASE: Thrombocytopenia, anemia, and myelofibrosis (THAMY)
[MIM:617441]: An autosomal recessive disorder characterized by
thrombocytopenia, increased number of giant platelets, and anemia
manifesting in early childhood. Bone marrow biopsy shows increased
number of megakaryocytes and reticular fibrosis consistent with
myelofibrosis. {ECO:0000269|PubMed:27743390}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
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EMBL; AJ292259; CAC83497.1; -; mRNA.
EMBL; AJ292260; CAC83496.1; -; mRNA.
EMBL; AJ292261; CAC83498.1; -; mRNA.
EMBL; AJ292262; CAC83502.1; -; mRNA.
EMBL; AJ292263; CAC83499.1; -; mRNA.
EMBL; AJ292264; CAC83500.1; -; mRNA.
EMBL; AJ292265; CAC83501.1; -; mRNA.
EMBL; AF129756; AAD18075.1; -; Genomic_DNA.
EMBL; BA000025; BAB63378.1; -; Genomic_DNA.
EMBL; AL670886; CAI17813.2; -; Genomic_DNA.
EMBL; AL670886; CAI17814.2; -; Genomic_DNA.
EMBL; AL670886; CAI17815.1; -; Genomic_DNA.
EMBL; AL670886; CAI17816.2; -; Genomic_DNA.
EMBL; AL670886; CAI17818.2; -; Genomic_DNA.
EMBL; AL662899; CAI18406.2; -; Genomic_DNA.
EMBL; AL662899; CAI18407.2; -; Genomic_DNA.
EMBL; AL662899; CAI18408.1; -; Genomic_DNA.
EMBL; AL662899; CAI18409.2; -; Genomic_DNA.
EMBL; AL662899; CAI18412.2; -; Genomic_DNA.
EMBL; BX248244; CAM26092.1; -; Genomic_DNA.
EMBL; BX248244; CAM26093.1; -; Genomic_DNA.
EMBL; BX248244; CAM26094.1; -; Genomic_DNA.
EMBL; BX248244; CAM26095.1; -; Genomic_DNA.
EMBL; BX248244; CAM26096.1; -; Genomic_DNA.
EMBL; AL844216; CAM45767.1; -; Genomic_DNA.
EMBL; AL844216; CAM45768.1; -; Genomic_DNA.
EMBL; AL844216; CAM45769.1; -; Genomic_DNA.
EMBL; AL844216; CAM45770.1; -; Genomic_DNA.
EMBL; AL844216; CAM45771.1; -; Genomic_DNA.
EMBL; CR354443; CAQ07017.1; -; Genomic_DNA.
EMBL; CR354443; CAQ07020.1; -; Genomic_DNA.
EMBL; CR354443; CAQ07021.1; -; Genomic_DNA.
EMBL; CR936239; CAQ08890.1; -; Genomic_DNA.
EMBL; CR936239; CAQ08892.1; -; Genomic_DNA.
EMBL; CR936239; CAQ08893.1; -; Genomic_DNA.
EMBL; CR936239; CAQ08894.1; -; Genomic_DNA.
EMBL; CR759787; CAQ10105.1; -; Genomic_DNA.
EMBL; CR759787; CAQ10107.1; -; Genomic_DNA.
EMBL; CR759787; CAQ10108.1; -; Genomic_DNA.
EMBL; CR759787; CAQ10109.1; -; Genomic_DNA.
EMBL; CH471081; EAX03493.1; -; Genomic_DNA.
EMBL; CH471081; EAX03494.1; -; Genomic_DNA.
EMBL; CH471081; EAX03497.1; -; Genomic_DNA.
EMBL; CH471081; EAX03498.1; -; Genomic_DNA.
EMBL; BC113719; AAI13720.1; -; mRNA.
EMBL; BC113721; AAI13722.1; -; mRNA.
CCDS; CCDS34405.1; -. [O95866-5]
CCDS; CCDS34406.1; -. [O95866-2]
CCDS; CCDS34407.1; -. [O95866-7]
CCDS; CCDS4715.1; -. [O95866-1]
CCDS; CCDS4716.1; -. [O95866-3]
CCDS; CCDS4717.1; -. [O95866-4]
RefSeq; NP_079536.2; NM_025260.3. [O95866-2]
RefSeq; NP_612116.1; NM_138272.2. [O95866-1]
RefSeq; NP_612117.1; NM_138273.2. [O95866-3]
RefSeq; NP_612118.1; NM_138274.2. [O95866-4]
RefSeq; NP_612119.1; NM_138275.2. [O95866-5]
RefSeq; NP_612121.1; NM_138277.2. [O95866-7]
UniGene; Hs.247879; -.
ProteinModelPortal; O95866; -.
SMR; O95866; -.
BioGrid; 123283; 2.
IntAct; O95866; 3.
MINT; MINT-8020429; -.
STRING; 9606.ENSP00000364964; -.
iPTMnet; O95866; -.
PhosphoSitePlus; O95866; -.
BioMuta; G6B; -.
PaxDb; O95866; -.
PeptideAtlas; O95866; -.
PRIDE; O95866; -.
DNASU; 80739; -.
Ensembl; ENST00000375804; ENSP00000364962; ENSG00000204420. [O95866-4]
Ensembl; ENST00000375805; ENSP00000364963; ENSG00000204420. [O95866-3]
Ensembl; ENST00000375806; ENSP00000364964; ENSG00000204420. [O95866-1]
Ensembl; ENST00000375809; ENSP00000364967; ENSG00000204420. [O95866-2]
Ensembl; ENST00000375810; ENSP00000364968; ENSG00000204420. [O95866-7]
Ensembl; ENST00000375814; ENSP00000364972; ENSG00000204420. [O95866-5]
Ensembl; ENST00000383410; ENSP00000372902; ENSG00000206396. [O95866-5]
Ensembl; ENST00000383411; ENSP00000372903; ENSG00000206396. [O95866-3]
Ensembl; ENST00000383412; ENSP00000372904; ENSG00000206396. [O95866-2]
Ensembl; ENST00000400067; ENSP00000382940; ENSG00000206396. [O95866-4]
Ensembl; ENST00000400071; ENSP00000382944; ENSG00000206396. [O95866-1]
Ensembl; ENST00000411608; ENSP00000392961; ENSG00000228090. [O95866-4]
Ensembl; ENST00000415728; ENSP00000408430; ENSG00000224393. [O95866-1]
Ensembl; ENST00000415984; ENSP00000394082; ENSG00000237459. [O95866-5]
Ensembl; ENST00000417610; ENSP00000412747; ENSG00000230060. [O95866-4]
Ensembl; ENST00000422012; ENSP00000398061; ENSG00000230060. [O95866-3]
Ensembl; ENST00000425998; ENSP00000392917; ENSG00000224393. [O95866-4]
Ensembl; ENST00000426729; ENSP00000390272; ENSG00000230060. [O95866-2]
Ensembl; ENST00000428302; ENSP00000404519; ENSG00000231003. [O95866-2]
Ensembl; ENST00000431888; ENSP00000390821; ENSG00000230060. [O95866-5]
Ensembl; ENST00000433769; ENSP00000413647; ENSG00000228090. [O95866-5]
Ensembl; ENST00000435007; ENSP00000401892; ENSG00000231003. [O95866-3]
Ensembl; ENST00000436030; ENSP00000406706; ENSG00000231003. [O95866-1]
Ensembl; ENST00000437153; ENSP00000412937; ENSG00000231003. [O95866-4]
Ensembl; ENST00000440063; ENSP00000388982; ENSG00000237459. [O95866-4]
Ensembl; ENST00000444404; ENSP00000415282; ENSG00000237459. [O95866-2]
Ensembl; ENST00000445381; ENSP00000396823; ENSG00000224393. [O95866-3]
Ensembl; ENST00000447587; ENSP00000416447; ENSG00000237459. [O95866-1]
Ensembl; ENST00000449633; ENSP00000388484; ENSG00000231003. [O95866-5]
Ensembl; ENST00000451549; ENSP00000395801; ENSG00000224393. [O95866-2]
Ensembl; ENST00000455185; ENSP00000414824; ENSG00000224393. [O95866-5]
Ensembl; ENST00000457450; ENSP00000395279; ENSG00000237459. [O95866-3]
Ensembl; ENST00000457884; ENSP00000391097; ENSG00000230060. [O95866-1]
GeneID; 80739; -.
KEGG; hsa:80739; -.
UCSC; uc003nwk.4; human. [O95866-1]
CTD; 80739; -.
DisGeNET; 80739; -.
GeneCards; C6orf25; -.
HGNC; HGNC:13937; MPIG6B.
HPA; HPA073017; -.
MIM; 606520; gene.
MIM; 617441; phenotype.
neXtProt; NX_O95866; -.
OpenTargets; ENSG00000204420; -.
PharmGKB; PA25926; -.
eggNOG; ENOG410IYA7; Eukaryota.
eggNOG; ENOG41118MY; LUCA.
GeneTree; ENSGT00390000017793; -.
HOVERGEN; HBG080566; -.
InParanoid; O95866; -.
OMA; RTYCKAP; -.
OrthoDB; EOG09370O4K; -.
PhylomeDB; O95866; -.
TreeFam; TF337394; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
GeneWiki; G6B_(gene); -.
GenomeRNAi; 80739; -.
PRO; PR:O95866; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204420; -.
ExpressionAtlas; O95866; baseline and differential.
Genevisible; O95866; HS.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0007596; P:blood coagulation; ISS:UniProtKB.
GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0035855; P:megakaryocyte development; ISS:UniProtKB.
GO; GO:0030219; P:megakaryocyte differentiation; IMP:UniProtKB.
GO; GO:0009968; P:negative regulation of signal transduction; IDA:UniProtKB.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0030220; P:platelet formation; ISS:UniProtKB.
InterPro; IPR028070; G6B.
Pfam; PF15096; G6B; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
Golgi apparatus; Heparin-binding; Membrane; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 17 {ECO:0000269|PubMed:12665801}.
CHAIN 18 241 Megakaryocyte and platelet inhibitory
receptor G6b.
/FTId=PRO_0000021312.
TOPO_DOM 18 142 Extracellular. {ECO:0000255,
ECO:0000303|PubMed:11544253}.
TRANSMEM 143 163 Helical. {ECO:0000255}.
TOPO_DOM 164 241 Cytoplasmic. {ECO:0000255,
ECO:0000303|PubMed:11544253}.
MOTIF 209 214 ITIM motif.
{ECO:0000305|PubMed:18955485}.
MOTIF 235 240 ITIM motif.
{ECO:0000305|PubMed:18955485}.
MOD_RES 211 211 Phosphotyrosine.
{ECO:0000269|PubMed:11544253}.
CARBOHYD 32 32 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 137 241 GSVYPQLLIPLLGAGLVLGLGALGLVWWLHRRLPPQPIRPL
PRFAPLVKTEPQRPVKEEEPKIPGDLDQEPSLLYADLDHLA
LSRPRRLSTADPADASTIYAVVV -> ALSPPHSSTCENRA
PEASKGGRAQDSRGPGPGTEPALCGSGPSSPQQAPPAVHSG
PC (in isoform D).
{ECO:0000303|PubMed:11544253}.
/FTId=VSP_014172.
VAR_SEQ 137 180 Missing (in isoform E).
{ECO:0000303|PubMed:11544253}.
/FTId=VSP_014173.
VAR_SEQ 138 180 SVYPQLLIPLLGAGLVLGLGALGLVWWLHRRLPPQPIRPLP
RF -> ACPRNRFDHSLDLLCPPHI (in isoform C).
{ECO:0000303|PubMed:11544253}.
/FTId=VSP_014174.
VAR_SEQ 181 241 APLVKTEPQRPVKEEEPKIPGDLDQEPSLLYADLDHLALSR
PRRLSTADPADASTIYAVVV -> GETNSTPFSFSYMPTPH
PSIPESEPLLGADTLVTFSPSFSSVPPT (in isoform
F). {ECO:0000303|PubMed:11544253}.
/FTId=VSP_014175.
VAR_SEQ 182 241 PLVKTEPQRPVKEEEPKIPGDLDQEPSLLYADLDHLALSRP
RRLSTADPADASTIYAVVV -> LSPPHSSTCENRAPEASK
GGRAQDSRGPGPGTEPALCGSGPSSPQQAPPAVHSGPC
(in isoform A).
{ECO:0000303|PubMed:11544253}.
/FTId=VSP_014176.
VAR_SEQ 182 241 PLVKTEPQRPVKEEEPKIPGDLDQEPSLLYADLDHLALSRP
RRLSTADPADASTIYAVVV -> LSPPHSSTCENRAPEASK
GGRAQDSRGPGPGTGKGMGMGRG (in isoform G).
{ECO:0000303|PubMed:11544253,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_014177.
VARIANT 108 241 Missing (in THAMY; increased protein
degradation; decreased enhancement of
hematopoietic lineage differentiation).
{ECO:0000269|PubMed:27743390}.
/FTId=VAR_078570.
VARIANT 175 175 R -> G (in dbSNP:rs11575845).
{ECO:0000269|PubMed:14574404}.
/FTId=VAR_051004.
MUTAGEN 211 211 Y->F: Abolishes the inhibitory effect
against ligand-induced activation of
PLCG2 by CLEC1B and GP6:FCER1G; when
associated with F-237.
{ECO:0000269|PubMed:18955485}.
MUTAGEN 211 211 Y->F: Loss of tyrosine phosphorylation
and loss of interaction with PTPN6 and
PTPN11. {ECO:0000269|PubMed:11544253}.
MUTAGEN 237 237 Y->F: Abolishes the inhibitory effect
against ligand-induced activation of
PLCG2 by CLEC1B and GP6:FCER1G; when
associted with F-237.
{ECO:0000269|PubMed:18955485}.
MUTAGEN 237 237 Y->F: Reduced level of tyrosine
phosphorylation and interaction with
PTPN6 and PTPN11.
{ECO:0000269|PubMed:11544253}.
CONFLICT 137 138 GS -> ID (in Ref. 5; CAI18409).
{ECO:0000305}.
SEQUENCE 241 AA; 26163 MW; C1390699EAA109BD CRC64;
MAVFLQLLPL LLSRAQGNPG ASLDGRPGDR VNLSCGGVSH PIRWVWAPSF PACKGLSKGR
RPILWASSSG TPTVPPLQPF VGRLRSLDSG IRRLELLLSA GDSGTFFCKG RHEDESRTVL
HVLGDRTYCK APGPTHGSVY PQLLIPLLGA GLVLGLGALG LVWWLHRRLP PQPIRPLPRF
APLVKTEPQR PVKEEEPKIP GDLDQEPSLL YADLDHLALS RPRRLSTADP ADASTIYAVV
V


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