G6B_HUMAN
ID G6B_HUMAN Reviewed; 241 AA.
AC O95866; A2BEZ1; A2BEZ2; A2BEZ3; A2BEZ4; A2BEZ5; B0UXC4; B0UXC7; B0UXC8;
AC B0V024; B0V026; Q14CK2; Q96A86; Q96A87; Q96A88; Q96A89; Q96A90; Q96A91;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Megakaryocyte and platelet inhibitory receptor G6b {ECO:0000312|HGNC:HGNC:13937};
DE AltName: Full=Protein G6b {ECO:0000305};
DE Flags: Precursor;
GN Name=MPIG6B {ECO:0000312|HGNC:HGNC:13937};
GN Synonyms=C6orf25 {ECO:0000312|HGNC:HGNC:13937},
GN G6B {ECO:0000312|HGNC:HGNC:13937}, G6B-B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAC83497.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D; E; F AND G), INTERACTION
RP WITH PTPN6 AND PTPN11, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP GLYCOSYLATION, PHOSPHORYLATION AT TYR-211, AND MUTAGENESIS OF TYR-211 AND
RP TYR-237.
RC TISSUE=T-cell;
RX PubMed=11544253; DOI=10.1074/jbc.m103214200;
RA de Vet E.C.M., Aguado B., Campbell R.D.;
RT "G6b, a novel immunoglobulin superfamily member encoded in the human major
RT histocompatibility complex, interacts with SHP-1 and SHP-2.";
RL J. Biol. Chem. 276:42070-42076(2001).
RN [2] {ECO:0000312|EMBL:AAD18075.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAB63378.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAB63378.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:CAI18408.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-175.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM G).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7] {ECO:0000305}
RP PROTEIN SEQUENCE OF 18-30.
RC TISSUE=Platelet {ECO:0000269|PubMed:12665801};
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP HEPARIN-BINDING.
RX PubMed=15848171; DOI=10.1016/j.febslet.2005.03.032;
RA de Vet E.C., Newland S.A., Lyons P.A., Aguado B., Campbell R.D.;
RT "The cell surface receptor G6b, a member of the immunoglobulin superfamily,
RT binds heparin.";
RL FEBS Lett. 579:2355-2358(2005).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17311996; DOI=10.1182/blood-2006-09-047449;
RA Newland S.A., Macaulay I.C., Floto A.R., de Vet E.C., Ouwehand W.H.,
RA Watkins N.A., Lyons P.A., Campbell D.R.;
RT "The novel inhibitory receptor G6B is expressed on the surface of platelets
RT and attenuates platelet function in vitro.";
RL Blood 109:4806-4809(2007).
RN [10]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF TYR-211 AND TYR-237.
RX PubMed=18955485; DOI=10.1074/jbc.m806895200;
RA Mori J., Pearce A.C., Spalton J.C., Grygielska B., Eble J.A.,
RA Tomlinson M.G., Senis Y.A., Watson S.P.;
RT "G6b-B inhibits constitutive and agonist-induced signaling by glycoprotein
RT VI and CLEC-2.";
RL J. Biol. Chem. 283:35419-35427(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [12]
RP GLYCOSYLATION, PHOSPHORYLATION, AND INTERACTION WITH PTPN6 AND PTPN11.
RX PubMed=23112346; DOI=10.1126/scisignal.2002936;
RA Mazharian A., Wang Y.J., Mori J., Bem D., Finney B., Heising S., Gissen P.,
RA White J.G., Berndt M.C., Gardiner E.E., Nieswandt B., Douglas M.R.,
RA Campbell R.D., Watson S.P., Senis Y.A.;
RT "Mice lacking the ITIM-containing receptor G6b-B exhibit
RT macrothrombocytopenia and aberrant platelet function.";
RL Sci. Signal. 5:RA78-RA78(2012).
RN [13]
RP INVOLVEMENT IN THAMY, VARIANT THAMY 108-CYS--VAL-241 DEL, CHARACTERIZATION
RP OF VARIANT THAMY 108-CYS--VAL-241 DEL, AND FUNCTION.
RX PubMed=27743390; DOI=10.1111/ejh.12819;
RA Melhem M., Abu-Farha M., Antony D., Madhoun A.A., Bacchelli C., Alkayal F.,
RA AlKhairi I., John S., Alomari M., Beales P.L., Alsmadi O.;
RT "Novel G6B gene variant causes familial autosomal recessive
RT thrombocytopenia and anemia.";
RL Eur. J. Haematol. 98:218-227(2017).
CC -!- FUNCTION: Inhibitory receptor that acts as a critical regulator of
CC hematopoietic lineage differentiation, megakaryocyte function and
CC platelet production (PubMed:12665801, PubMed:17311996,
CC PubMed:27743390). Inhibits platelet aggregation and activation by
CC agonists such as ADP and collagen-related peptide (PubMed:12665801).
CC This regulation of megakaryocate function as well as platelet
CC production ann activation is done through the inhibition (via the 2
CC ITIM motifs) of the receptors CLEC1B and GP6:FcRgamma signaling
CC (PubMed:17311996). Appears to operate in a calcium-independent manner
CC (PubMed:12665801). {ECO:0000269|PubMed:12665801,
CC ECO:0000269|PubMed:17311996, ECO:0000269|PubMed:27743390}.
CC -!- FUNCTION: Isoform B, displayed in this entry, is the only isoform to
CC contain both a transmembrane region and 2 immunoreceptor tyrosine-based
CC inhibitor motifs (ITIMs) and, thus, the only one which probably has a
CC role of inhibitory receptor. Isoform A may be the activating
CC counterpart of isoform B. {ECO:0000305|PubMed:11544253}.
CC -!- SUBUNIT: Interacts (via ITIM motif) with PTPN6 and PTPN11
CC (PubMed:11544253, PubMed:23112346). Binds to heparin (PubMed:15848171).
CC {ECO:0000269|PubMed:11544253, ECO:0000269|PubMed:15848171,
CC ECO:0000269|PubMed:23112346, ECO:0000305|PubMed:18955485}.
CC -!- SUBCELLULAR LOCATION: [Isoform E]: Endoplasmic reticulum
CC {ECO:0000269|PubMed:11544253}. Golgi apparatus
CC {ECO:0000269|PubMed:11544253}.
CC -!- SUBCELLULAR LOCATION: [Isoform D]: Endoplasmic reticulum
CC {ECO:0000269|PubMed:11544253}. Golgi apparatus
CC {ECO:0000269|PubMed:11544253}.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Cell membrane
CC {ECO:0000269|PubMed:11544253}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Cell membrane
CC {ECO:0000269|PubMed:11544253}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=B {ECO:0000269|PubMed:11544253};
CC IsoId=O95866-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:11544253};
CC IsoId=O95866-2; Sequence=VSP_014176;
CC Name=C {ECO:0000269|PubMed:11544253};
CC IsoId=O95866-3; Sequence=VSP_014174;
CC Name=D {ECO:0000269|PubMed:11544253};
CC IsoId=O95866-4; Sequence=VSP_014172;
CC Name=E {ECO:0000269|PubMed:11544253};
CC IsoId=O95866-5; Sequence=VSP_014173;
CC Name=F {ECO:0000269|PubMed:11544253};
CC IsoId=O95866-6; Sequence=VSP_014175;
CC Name=G {ECO:0000269|PubMed:11544253};
CC IsoId=O95866-7; Sequence=VSP_014177;
CC -!- TISSUE SPECIFICITY: Expressed in platelets. Expressed in a restricted
CC set of hematopoietic cell lines including the erythroleukemia cell line
CC K-562 and the T-cell leukemia cell lines MOLT-4 and Jurkat. Not
CC detected in the monocyte-like cell line U-937, the B-cell-like cell
CC line Raji, the fibroblast cell lines TK and HeLa, or the natural killer
CC cell lines NKL, NK 62 and YT. {ECO:0000269|PubMed:11544253,
CC ECO:0000269|PubMed:17311996}.
CC -!- DOMAIN: Isoform B, displayed in this entry, is the only one of the
CC isoforms to contain both a transmembrane region and 2 copies of a
CC cytoplasmic motif that is referred to as the immunoreceptor tyrosine-
CC based inhibitor motif (ITIM). This motif is involved in modulation of
CC cellular responses. The phosphorylated ITIM motif can bind the SH2
CC domain of several SH2-containing phosphatases. The 2 ITIM motifs of
CC isoform B are required for the inhibition of CLEC1B and GP6:FCER1G
CC signaling and platelet activation. {ECO:0000305|PubMed:18955485}.
CC -!- PTM: All isoforms are N-glycosylated. {ECO:0000269|PubMed:11544253,
CC ECO:0000269|PubMed:23112346}.
CC -!- PTM: Isoform E is O-glycosylated. {ECO:0000269|PubMed:11544253}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:11544253,
CC ECO:0000269|PubMed:23112346}.
CC -!- DISEASE: Thrombocytopenia, anemia, and myelofibrosis (THAMY)
CC [MIM:617441]: An autosomal recessive disorder characterized by
CC thrombocytopenia, increased number of giant platelets, and anemia
CC manifesting in early childhood. Bone marrow biopsy shows increased
CC number of megakaryocytes and reticular fibrosis consistent with
CC myelofibrosis. {ECO:0000269|PubMed:27743390}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
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DR EMBL; AJ292259; CAC83497.1; -; mRNA.
DR EMBL; AJ292260; CAC83496.1; -; mRNA.
DR EMBL; AJ292261; CAC83498.1; -; mRNA.
DR EMBL; AJ292262; CAC83502.1; -; mRNA.
DR EMBL; AJ292263; CAC83499.1; -; mRNA.
DR EMBL; AJ292264; CAC83500.1; -; mRNA.
DR EMBL; AJ292265; CAC83501.1; -; mRNA.
DR EMBL; AF129756; AAD18075.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63378.1; -; Genomic_DNA.
DR EMBL; AL670886; CAI17813.2; -; Genomic_DNA.
DR EMBL; AL670886; CAI17814.2; -; Genomic_DNA.
DR EMBL; AL670886; CAI17815.1; -; Genomic_DNA.
DR EMBL; AL670886; CAI17816.2; -; Genomic_DNA.
DR EMBL; AL670886; CAI17818.2; -; Genomic_DNA.
DR EMBL; AL662899; CAI18406.2; -; Genomic_DNA.
DR EMBL; AL662899; CAI18407.2; -; Genomic_DNA.
DR EMBL; AL662899; CAI18408.1; -; Genomic_DNA.
DR EMBL; AL662899; CAI18409.2; -; Genomic_DNA.
DR EMBL; AL662899; CAI18412.2; -; Genomic_DNA.
DR EMBL; BX248244; CAM26092.1; -; Genomic_DNA.
DR EMBL; BX248244; CAM26093.1; -; Genomic_DNA.
DR EMBL; BX248244; CAM26094.1; -; Genomic_DNA.
DR EMBL; BX248244; CAM26095.1; -; Genomic_DNA.
DR EMBL; BX248244; CAM26096.1; -; Genomic_DNA.
DR EMBL; AL844216; CAM45767.1; -; Genomic_DNA.
DR EMBL; AL844216; CAM45768.1; -; Genomic_DNA.
DR EMBL; AL844216; CAM45769.1; -; Genomic_DNA.
DR EMBL; AL844216; CAM45770.1; -; Genomic_DNA.
DR EMBL; AL844216; CAM45771.1; -; Genomic_DNA.
DR EMBL; CR354443; CAQ07017.1; -; Genomic_DNA.
DR EMBL; CR354443; CAQ07020.1; -; Genomic_DNA.
DR EMBL; CR354443; CAQ07021.1; -; Genomic_DNA.
DR EMBL; CR936239; CAQ08890.1; -; Genomic_DNA.
DR EMBL; CR936239; CAQ08892.1; -; Genomic_DNA.
DR EMBL; CR936239; CAQ08893.1; -; Genomic_DNA.
DR EMBL; CR936239; CAQ08894.1; -; Genomic_DNA.
DR EMBL; CR759787; CAQ10105.1; -; Genomic_DNA.
DR EMBL; CR759787; CAQ10107.1; -; Genomic_DNA.
DR EMBL; CR759787; CAQ10108.1; -; Genomic_DNA.
DR EMBL; CR759787; CAQ10109.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03493.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03494.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03497.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03498.1; -; Genomic_DNA.
DR EMBL; BC113719; AAI13720.1; -; mRNA.
DR EMBL; BC113721; AAI13722.1; -; mRNA.
DR CCDS; CCDS34405.1; -. [O95866-5]
DR CCDS; CCDS34406.1; -. [O95866-2]
DR CCDS; CCDS34407.1; -. [O95866-7]
DR CCDS; CCDS4715.1; -. [O95866-1]
DR CCDS; CCDS4716.1; -. [O95866-3]
DR CCDS; CCDS4717.1; -. [O95866-4]
DR RefSeq; NP_079536.2; NM_025260.3. [O95866-2]
DR RefSeq; NP_612116.1; NM_138272.2. [O95866-1]
DR RefSeq; NP_612117.1; NM_138273.2. [O95866-3]
DR RefSeq; NP_612118.1; NM_138274.2. [O95866-4]
DR RefSeq; NP_612119.1; NM_138275.2. [O95866-5]
DR RefSeq; NP_612121.1; NM_138277.2. [O95866-7]
DR PDB; 6R0X; X-ray; 3.13 A; E/F=18-133.
DR PDBsum; 6R0X; -.
DR AlphaFoldDB; O95866; -.
DR SMR; O95866; -.
DR BioGRID; 123283; 2.
DR IntAct; O95866; 3.
DR MINT; O95866; -.
DR STRING; 9606.ENSP00000364964; -.
DR GlyGen; O95866; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O95866; -.
DR PhosphoSitePlus; O95866; -.
DR BioMuta; MPIG6B; -.
DR MassIVE; O95866; -.
DR PaxDb; O95866; -.
DR PeptideAtlas; O95866; -.
DR PRIDE; O95866; -.
DR ProteomicsDB; 51105; -. [O95866-5]
DR ProteomicsDB; 51107; -. [O95866-7]
DR ABCD; O95866; 1 sequenced antibody.
DR Antibodypedia; 27557; 92 antibodies from 18 providers.
DR DNASU; 80739; -.
DR Ensembl; ENST00000375804.6; ENSP00000364962.2; ENSG00000204420.10. [O95866-4]
DR Ensembl; ENST00000375805.6; ENSP00000364963.2; ENSG00000204420.10. [O95866-3]
DR Ensembl; ENST00000375809.7; ENSP00000364967.3; ENSG00000204420.10. [O95866-2]
DR Ensembl; ENST00000375810.8; ENSP00000364968.4; ENSG00000204420.10. [O95866-7]
DR Ensembl; ENST00000375814.7; ENSP00000364972.3; ENSG00000204420.10. [O95866-5]
DR Ensembl; ENST00000383410.4; ENSP00000372902.4; ENSG00000206396.9. [O95866-5]
DR Ensembl; ENST00000383411.8; ENSP00000372903.4; ENSG00000206396.9. [O95866-3]
DR Ensembl; ENST00000383412.8; ENSP00000372904.4; ENSG00000206396.9. [O95866-2]
DR Ensembl; ENST00000400067.7; ENSP00000382940.3; ENSG00000206396.9. [O95866-4]
DR Ensembl; ENST00000400071.7; ENSP00000382944.3; ENSG00000206396.9. [O95866-1]
DR Ensembl; ENST00000411608.6; ENSP00000392961.2; ENSG00000228090.6. [O95866-4]
DR Ensembl; ENST00000415728.2; ENSP00000408430.2; ENSG00000224393.6. [O95866-1]
DR Ensembl; ENST00000415984.6; ENSP00000394082.2; ENSG00000237459.6. [O95866-5]
DR Ensembl; ENST00000417610.2; ENSP00000412747.2; ENSG00000230060.6. [O95866-4]
DR Ensembl; ENST00000422012.6; ENSP00000398061.2; ENSG00000230060.6. [O95866-3]
DR Ensembl; ENST00000425998.6; ENSP00000392917.2; ENSG00000224393.6. [O95866-4]
DR Ensembl; ENST00000426729.6; ENSP00000390272.2; ENSG00000230060.6. [O95866-2]
DR Ensembl; ENST00000428302.6; ENSP00000404519.2; ENSG00000231003.6. [O95866-2]
DR Ensembl; ENST00000431888.6; ENSP00000390821.2; ENSG00000230060.6. [O95866-5]
DR Ensembl; ENST00000433769.6; ENSP00000413647.2; ENSG00000228090.6. [O95866-5]
DR Ensembl; ENST00000435007.6; ENSP00000401892.2; ENSG00000231003.6. [O95866-3]
DR Ensembl; ENST00000436030.6; ENSP00000406706.2; ENSG00000231003.6. [O95866-1]
DR Ensembl; ENST00000437153.6; ENSP00000412937.2; ENSG00000231003.6. [O95866-4]
DR Ensembl; ENST00000440063.6; ENSP00000388982.2; ENSG00000237459.6. [O95866-4]
DR Ensembl; ENST00000444404.6; ENSP00000415282.2; ENSG00000237459.6. [O95866-2]
DR Ensembl; ENST00000445381.6; ENSP00000396823.2; ENSG00000224393.6. [O95866-3]
DR Ensembl; ENST00000447587.2; ENSP00000416447.2; ENSG00000237459.6. [O95866-1]
DR Ensembl; ENST00000449633.2; ENSP00000388484.2; ENSG00000231003.6. [O95866-5]
DR Ensembl; ENST00000451549.6; ENSP00000395801.2; ENSG00000224393.6. [O95866-2]
DR Ensembl; ENST00000455185.6; ENSP00000414824.2; ENSG00000224393.6. [O95866-5]
DR Ensembl; ENST00000457450.6; ENSP00000395279.2; ENSG00000237459.6. [O95866-3]
DR Ensembl; ENST00000457884.6; ENSP00000391097.2; ENSG00000230060.6. [O95866-1]
DR Ensembl; ENST00000649779.1; ENSP00000497720.1; ENSG00000204420.10. [O95866-1]
DR GeneID; 80739; -.
DR KEGG; hsa:80739; -.
DR MANE-Select; ENST00000649779.1; ENSP00000497720.1; NM_138272.3; NP_612116.1.
DR UCSC; uc003nwk.4; human. [O95866-1]
DR CTD; 80739; -.
DR DisGeNET; 80739; -.
DR GeneCards; MPIG6B; -.
DR HGNC; HGNC:13937; MPIG6B.
DR HPA; ENSG00000204420; Tissue enhanced (lung, lymphoid tissue, skin).
DR MalaCards; MPIG6B; -.
DR MIM; 606520; gene.
DR MIM; 617441; phenotype.
DR neXtProt; NX_O95866; -.
DR OpenTargets; ENSG00000204420; -.
DR PharmGKB; PA25926; -.
DR VEuPathDB; HostDB:ENSG00000204420; -.
DR eggNOG; ENOG502TEAD; Eukaryota.
DR GeneTree; ENSGT00390000017793; -.
DR HOGENOM; CLU_101026_0_0_1; -.
DR InParanoid; O95866; -.
DR OMA; YMALRRP; -.
DR OrthoDB; 1615599at2759; -.
DR PhylomeDB; O95866; -.
DR TreeFam; TF337394; -.
DR PathwayCommons; O95866; -.
DR Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR SignaLink; O95866; -.
DR BioGRID-ORCS; 80739; 7 hits in 1054 CRISPR screens.
DR ChiTaRS; C6orf25; human.
DR GeneWiki; G6B_(gene); -.
DR GenomeRNAi; 80739; -.
DR Pharos; O95866; Tbio.
DR PRO; PR:O95866; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O95866; protein.
DR Bgee; ENSG00000204420; Expressed in monocyte and 94 other tissues.
DR ExpressionAtlas; O95866; baseline and differential.
DR Genevisible; O95866; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; ISS:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0035855; P:megakaryocyte development; ISS:UniProtKB.
DR GO; GO:0030219; P:megakaryocyte differentiation; IMP:UniProtKB.
DR GO; GO:0009968; P:negative regulation of signal transduction; IDA:UniProtKB.
DR GO; GO:0030220; P:platelet formation; ISS:UniProtKB.
DR InterPro; IPR028070; G6B.
DR PANTHER; PTHR37347; PTHR37347; 1.
DR Pfam; PF15096; G6B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Heparin-binding; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 18..241
FT /note="Megakaryocyte and platelet inhibitory receptor G6b"
FT /id="PRO_0000021312"
FT TOPO_DOM 18..142
FT /note="Extracellular"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:11544253"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:11544253"
FT MOTIF 209..214
FT /note="ITIM motif"
FT /evidence="ECO:0000305|PubMed:18955485"
FT MOTIF 235..240
FT /note="ITIM motif"
FT /evidence="ECO:0000305|PubMed:18955485"
FT MOD_RES 211
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11544253"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 137..241
FT /note="GSVYPQLLIPLLGAGLVLGLGALGLVWWLHRRLPPQPIRPLPRFAPLVKTEP
FT QRPVKEEEPKIPGDLDQEPSLLYADLDHLALSRPRRLSTADPADASTIYAVVV -> AL
FT SPPHSSTCENRAPEASKGGRAQDSRGPGPGTEPALCGSGPSSPQQAPPAVHSGPC (in
FT isoform D)"
FT /evidence="ECO:0000303|PubMed:11544253"
FT /id="VSP_014172"
FT VAR_SEQ 137..180
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:11544253"
FT /id="VSP_014173"
FT VAR_SEQ 138..180
FT /note="SVYPQLLIPLLGAGLVLGLGALGLVWWLHRRLPPQPIRPLPRF -> ACPRN
FT RFDHSLDLLCPPHI (in isoform C)"
FT /evidence="ECO:0000303|PubMed:11544253"
FT /id="VSP_014174"
FT VAR_SEQ 181..241
FT /note="APLVKTEPQRPVKEEEPKIPGDLDQEPSLLYADLDHLALSRPRRLSTADPAD
FT ASTIYAVVV -> GETNSTPFSFSYMPTPHPSIPESEPLLGADTLVTFSPSFSSVPPT
FT (in isoform F)"
FT /evidence="ECO:0000303|PubMed:11544253"
FT /id="VSP_014175"
FT VAR_SEQ 182..241
FT /note="PLVKTEPQRPVKEEEPKIPGDLDQEPSLLYADLDHLALSRPRRLSTADPADA
FT STIYAVVV -> LSPPHSSTCENRAPEASKGGRAQDSRGPGPGTEPALCGSGPSSPQQA
FT PPAVHSGPC (in isoform A)"
FT /evidence="ECO:0000303|PubMed:11544253"
FT /id="VSP_014176"
FT VAR_SEQ 182..241
FT /note="PLVKTEPQRPVKEEEPKIPGDLDQEPSLLYADLDHLALSRPRRLSTADPADA
FT STIYAVVV -> LSPPHSSTCENRAPEASKGGRAQDSRGPGPGTGKGMGMGRG (in
FT isoform G)"
FT /evidence="ECO:0000303|PubMed:11544253,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_014177"
FT VARIANT 108..241
FT /note="Missing (in THAMY; increased protein degradation;
FT decreased enhancement of hematopoietic lineage
FT differentiation)"
FT /evidence="ECO:0000269|PubMed:27743390"
FT /id="VAR_078570"
FT VARIANT 175
FT /note="R -> G (in dbSNP:rs11575845)"
FT /evidence="ECO:0000269|PubMed:14574404"
FT /id="VAR_051004"
FT MUTAGEN 211
FT /note="Y->F: Abolishes the inhibitory effect against
FT ligand-induced activation of PLCG2 by CLEC1B and
FT GP6:FCER1G; when associated with F-237."
FT /evidence="ECO:0000269|PubMed:18955485"
FT MUTAGEN 211
FT /note="Y->F: Loss of tyrosine phosphorylation and loss of
FT interaction with PTPN6 and PTPN11."
FT /evidence="ECO:0000269|PubMed:11544253"
FT MUTAGEN 237
FT /note="Y->F: Abolishes the inhibitory effect against
FT ligand-induced activation of PLCG2 by CLEC1B and
FT GP6:FCER1G; when associated with F-237."
FT /evidence="ECO:0000269|PubMed:18955485"
FT MUTAGEN 237
FT /note="Y->F: Reduced level of tyrosine phosphorylation and
FT interaction with PTPN6 and PTPN11."
FT /evidence="ECO:0000269|PubMed:11544253"
FT CONFLICT 137..138
FT /note="GS -> ID (in Ref. 5; CAI18409)"
FT /evidence="ECO:0000305"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:6R0X"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:6R0X"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6R0X"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:6R0X"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:6R0X"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6R0X"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6R0X"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:6R0X"
SQ 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
