P2RX7_HUMAN
ID P2RX7_HUMAN Reviewed; 595 AA.
AC Q99572; A8K2Z0; E7EMK6; F5H6P2; F5H7E8; F8W951; O14991; Q4VKH8; Q4VKH9;
AC Q4VKI0; Q4VKI1; Q4VKI2; Q4VKI3; Q4VKI4; Q7Z771; Q96EV7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 4.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=P2X purinoceptor 7;
DE Short=P2X7;
DE AltName: Full=ATP receptor;
DE AltName: Full=P2Z receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2RX7;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND VARIANTS HIS-155 AND HIS-270.
RC TISSUE=Brain;
RX PubMed=9038151; DOI=10.1074/jbc.272.9.5482;
RA Rassendren F., Buell G.N., Virginio C., Collo G., North R.A.,
RA Surprenant A.;
RT "The permeabilizing ATP receptor, P2X7. Cloning and expression of a human
RT cDNA.";
RL J. Biol. Chem. 272:5482-5486(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-155 AND THR-348.
RX PubMed=9826911;
RA Buell G.N., Talabot F., Gos A., Lorenz J., Lai E., Morris M.A.,
RA Antonarakis S.E.;
RT "Gene structure and chromosomal localization of the human P2X7 receptor.";
RL Recept. Channels 5:347-354(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C; D; E; F; G AND H), ALTERNATIVE
RP SPLICING, TISSUE SPECIFICITY, AND VARIANTS HIS-155 AND HIS-270.
RC TISSUE=Brain;
RX PubMed=15896293; DOI=10.1016/j.bbrc.2005.04.087;
RA Cheewatrakoolpong B., Gilchrest H., Anthes J.C., Greenfeder S.;
RT "Identification and characterization of splice variants of the human P2X7
RT ATP channel.";
RL Biochem. Biophys. Res. Commun. 332:17-27(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C), AND VARIANT
RP SER-357.
RC TISSUE=Brain, and Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-568.
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND D), AND VARIANTS
RP HIS-155; HIS-270 AND ALA-496.
RC TISSUE=Brain, and Skin;
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]
RP PHOSPHORYLATION AT TYR-343, AND INTERACTION WITH LAMA3; ITGB2; ACTB; ACTN4;
RP SVIL; MPP3; HSPA1; HSPCB; HSPA8; PIK230 AND PTPRB.
RX PubMed=11707406; DOI=10.1093/emboj/20.22.6347;
RA Kim M., Jiang L.H., Wilson H.L., North R.A., Surprenant A.;
RT "Proteomic and functional evidence for a P2X7 receptor signalling
RT complex.";
RL EMBO J. 20:6347-6358(2001).
RN [8]
RP INTERACTION WITH EMP2, AND SUBCELLULAR LOCATION.
RX PubMed=12107182; DOI=10.1074/jbc.m205120200;
RA Wilson H.L., Wilson S.A., Surprenant A., North R.A.;
RT "Epithelial membrane proteins induce membrane blebbing and interact with
RT the P2X7 receptor C terminus.";
RL J. Biol. Chem. 277:34017-34023(2002).
RN [9]
RP PALMITOYLATION.
RX PubMed=18971257; DOI=10.1096/fj.08-114637;
RA Gonnord P., Delarasse C., Auger R., Benihoud K., Prigent M., Cuif M.H.,
RA Lamaze C., Kanellopoulos J.M.;
RT "Palmitoylation of the P2X7 receptor, an ATP-gated channel, controls its
RT expression and association with lipid rafts.";
RL FASEB J. 23:795-805(2009).
RN [10]
RP GLYCOSYLATION AT ASN-187; ASN-202; ASN-213; ASN-241 AND ASN-284, AND
RP MUTAGENESIS OF ASN-187.
RX PubMed=20450227; DOI=10.1021/bi902083n;
RA Lenertz L.Y., Wang Z., Guadarrama A., Hill L.M., Gavala M.L., Bertics P.J.;
RT "Mutation of putative N-linked glycosylation sites on the human nucleotide
RT receptor P2X7 reveals a key residue important for receptor function.";
RL Biochemistry 49:4611-4619(2010).
RN [11]
RP FUNCTION.
RX PubMed=21821797; DOI=10.4049/jimmunol.1101178;
RA Gu B.J., Saunders B.M., Petrou S., Wiley J.S.;
RT "P2X(7) is a scavenger receptor for apoptotic cells in the absence of its
RT ligand, extracellular ATP.";
RL J. Immunol. 187:2365-2375(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP VARIANT ALA-496.
RX PubMed=11150303; DOI=10.1074/jbc.m010353200;
RA Gu B.J., Zhang W., Worthington R.A., Sluyter R., Dao-Ung P., Petrou S.,
RA Barden J.A., Wiley J.S.;
RT "A Glu-496 to Ala polymorphism leads to loss of function of the human P2X7
RT receptor.";
RL J. Biol. Chem. 276:11135-11142(2001).
RN [14]
RP CHARACTERIZATION OF VARIANT ASN-568.
RX PubMed=12586825; DOI=10.1074/jbc.m212759200;
RA Wiley J.S., Dao-Ung L.P., Li C., Shemon A.N., Gu B.J., Smart M.L.,
RA Fuller S.J., Barden J.A., Petrou S., Sluyter R.;
RT "An Ile-568 to Asn polymorphism prevents normal trafficking and function of
RT the human P2X7 receptor.";
RL J. Biol. Chem. 278:17108-17113(2003).
RN [15]
RP CHARACTERIZATION OF VARIANT GLN-307.
RX PubMed=15123679; DOI=10.1074/jbc.m313902200;
RA Gu B.J., Sluyter R., Skarratt K.K., Shemon A.N., Dao-Ung L.P., Fuller S.J.,
RA Barden J.A., Clarke A.L., Petrou S., Wiley J.S.;
RT "An Arg307 to Gln polymorphism within the ATP-binding site causes loss of
RT function of the human P2X7 receptor.";
RL J. Biol. Chem. 279:31287-31295(2004).
RN [16]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-25 AND LEU-574.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [17]
RP VARIANTS ALA-76; ARG-150; HIS-155; HIS-270; HIS-276; GLN-307; THR-348;
RP SER-357; ARG-460; ALA-496 AND ASN-568, SUBCELLULAR LOCATION,
RP CHARACTERIZATION OF VARIANT ARG-150, AND FUNCTION.
RX PubMed=23303206; DOI=10.1096/fj.12-215368;
RA Gu B.J., Baird P.N., Vessey K.A., Skarratt K.K., Fletcher E.L.,
RA Fuller S.J., Richardson A.J., Guymer R.H., Wiley J.S.;
RT "A rare functional haplotype of the P2RX4 and P2RX7 genes leads to loss of
RT innate phagocytosis and confers increased risk of age-related macular
RT degeneration.";
RL FASEB J. 27:1479-1487(2013).
RN [18]
RP VARIANTS ALA-76; TRP-117; LEU-125; ARG-148; ARG-150; HIS-155; MET-205;
RP HIS-264; HIS-270; HIS-276; HIS-288; GLN-307; THR-348; SER-357; SER-361;
RP VAL-433; ARG-460; ALA-496; GLN-521; ILE-522; VAL-535; GLN-544 AND ASN-568,
RP CHARACTERIZATION OF VARIANTS MET-205 AND SER-361, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=28326637; DOI=10.1002/humu.23218;
RA Sadovnick A.D., Gu B.J., Traboulsee A.L., Bernales C.Q., Encarnacion M.,
RA Yee I.M., Criscuoli M.G., Huang X., Ou A., Milligan C.J., Petrou S.,
RA Wiley J.S., Vilarino-Gueell C.;
RT "Purinergic receptors P2RX4 and P2RX7 in familial multiple sclerosis.";
RL Hum. Mutat. 38:736-744(2017).
CC -!- FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel.
CC Responsible for ATP-dependent lysis of macrophages through the
CC formation of membrane pores permeable to large molecules. Could
CC function in both fast synaptic transmission and the ATP-mediated lysis
CC of antigen-presenting cells. In the absence of its natural ligand, ATP,
CC functions as a scavenger receptor in the recognition and engulfment of
CC apoptotic cells (PubMed:21821797, PubMed:23303206).
CC {ECO:0000269|PubMed:21821797, ECO:0000269|PubMed:23303206,
CC ECO:0000269|PubMed:28326637}.
CC -!- SUBUNIT: Functional P2XRs are organized as homomeric and heteromeric
CC trimers. Interacts with LAMA3, ITGB2, ACTB, ACTN4, SVIL, MPP3, HSPA1,
CC HSPCB, HSPA8, PIK230 and PTPRB. Interacts (via C-terminus) with EMP2
CC (PubMed:12107182). {ECO:0000269|PubMed:11707406,
CC ECO:0000269|PubMed:12107182}.
CC -!- INTERACTION:
CC Q99572; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1753251, EBI-3867333;
CC Q99572; O95967: EFEMP2; NbExp=3; IntAct=EBI-1753251, EBI-743414;
CC Q99572; O75031: HSF2BP; NbExp=3; IntAct=EBI-1753251, EBI-7116203;
CC Q99572; Q15323: KRT31; NbExp=6; IntAct=EBI-1753251, EBI-948001;
CC Q99572; O76011: KRT34; NbExp=3; IntAct=EBI-1753251, EBI-1047093;
CC Q99572; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1753251, EBI-10171774;
CC Q99572; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-1753251, EBI-22310682;
CC Q99572; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-1753251, EBI-742388;
CC Q99572; P14373: TRIM27; NbExp=3; IntAct=EBI-1753251, EBI-719493;
CC Q99572; Q8N720: ZNF655; NbExp=3; IntAct=EBI-1753251, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12107182,
CC ECO:0000269|PubMed:23303206, ECO:0000269|PubMed:28326637}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=A;
CC IsoId=Q99572-1; Sequence=Displayed;
CC Name=B; Synonyms=Delta-C, cytoplasmic tail deleted;
CC IsoId=Q99572-2; Sequence=VSP_047784, VSP_047785;
CC Name=C;
CC IsoId=Q99572-3; Sequence=VSP_047781, VSP_047782;
CC Name=D;
CC IsoId=Q99572-4; Sequence=VSP_047777, VSP_047780;
CC Name=E;
CC IsoId=Q99572-5; Sequence=VSP_047783, VSP_047784, VSP_047785;
CC Name=F;
CC IsoId=Q99572-6; Sequence=VSP_047778, VSP_047779;
CC Name=G;
CC IsoId=Q99572-7; Sequence=VSP_047776, VSP_047784, VSP_047785;
CC Name=H; Synonyms=Delta-TM1;
CC IsoId=Q99572-8; Sequence=VSP_047776;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain and
CC immune tissues. {ECO:0000269|PubMed:15896293}.
CC -!- PTM: Phosphorylation results in its inactivation.
CC {ECO:0000269|PubMed:11707406}.
CC -!- PTM: ADP-ribosylation at Arg-125 is necessary and sufficient to
CC activate P2RX7 and gate the channel. {ECO:0000250}.
CC -!- PTM: Palmitoylation of several cysteines in the C-terminal cytoplasmic
CC tail is required for efficient localization to cell surface.
CC {ECO:0000269|PubMed:18971257}.
CC -!- MISCELLANEOUS: [Isoform B]: Predominant form in many tissues.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform H]: Non-functional channel. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/P2RX7ID41623ch12q24.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=P2X receptor entry;
CC URL="https://en.wikipedia.org/wiki/P2X_receptor";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=P2RX7 entry;
CC URL="https://en.wikipedia.org/wiki/P2RX7";
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DR EMBL; Y09561; CAA70755.1; -; mRNA.
DR EMBL; Y12851; CAA73360.1; -; Genomic_DNA.
DR EMBL; Y12852; CAA73360.1; JOINED; Genomic_DNA.
DR EMBL; Y12853; CAA73360.1; JOINED; Genomic_DNA.
DR EMBL; Y12854; CAA73360.1; JOINED; Genomic_DNA.
DR EMBL; Y12855; CAA73360.1; JOINED; Genomic_DNA.
DR EMBL; AY847298; AAX82087.1; -; mRNA.
DR EMBL; AY847299; AAX82088.1; -; mRNA.
DR EMBL; AY847300; AAX82089.1; -; mRNA.
DR EMBL; AY847301; AAX82090.1; -; mRNA.
DR EMBL; AY847302; AAX82091.1; -; mRNA.
DR EMBL; AY847303; AAX82092.1; -; mRNA.
DR EMBL; AY847304; AAX82093.1; -; mRNA.
DR EMBL; AK290405; BAF83094.1; -; mRNA.
DR EMBL; AK294126; BAH11678.1; -; mRNA.
DR EMBL; AC069209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z98941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007679; AAH07679.1; -; mRNA.
DR EMBL; BC011913; AAH11913.1; -; mRNA.
DR CCDS; CCDS9213.1; -. [Q99572-1]
DR RefSeq; NP_002553.3; NM_002562.5. [Q99572-1]
DR RefSeq; XP_011536722.1; XM_011538420.2. [Q99572-6]
DR AlphaFoldDB; Q99572; -.
DR SMR; Q99572; -.
DR BioGRID; 111066; 16.
DR CORUM; Q99572; -.
DR ELM; Q99572; -.
DR IntAct; Q99572; 17.
DR STRING; 9606.ENSP00000330696; -.
DR BindingDB; Q99572; -.
DR ChEMBL; CHEMBL4805; -.
DR DrugBank; DB01069; Promethazine.
DR GuidetoPHARMACOLOGY; 484; -.
DR TCDB; 1.A.7.1.3; the atp-gated p2x receptor cation channel (p2x receptor) family.
DR GlyConnect; 1591; 1 N-Linked glycan (1 site).
DR GlyGen; Q99572; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q99572; -.
DR PhosphoSitePlus; Q99572; -.
DR SwissPalm; Q99572; -.
DR BioMuta; P2RX7; -.
DR DMDM; 395398617; -.
DR CPTAC; CPTAC-2229; -.
DR jPOST; Q99572; -.
DR MassIVE; Q99572; -.
DR PaxDb; Q99572; -.
DR PeptideAtlas; Q99572; -.
DR PRIDE; Q99572; -.
DR ProteomicsDB; 16961; -.
DR ProteomicsDB; 27247; -.
DR ProteomicsDB; 27466; -.
DR ProteomicsDB; 30262; -.
DR ProteomicsDB; 62309; -.
DR ProteomicsDB; 78332; -. [Q99572-1]
DR Antibodypedia; 19042; 453 antibodies from 43 providers.
DR DNASU; 5027; -.
DR Ensembl; ENST00000328963.10; ENSP00000330696.6; ENSG00000089041.17. [Q99572-1]
DR Ensembl; ENST00000535250.5; ENSP00000442572.2; ENSG00000089041.17. [Q99572-2]
DR Ensembl; ENST00000535600.2; ENSP00000442470.1; ENSG00000089041.17. [Q99572-5]
DR Ensembl; ENST00000541022.5; ENSP00000441230.1; ENSG00000089041.17. [Q99572-3]
DR Ensembl; ENST00000541716.5; ENSP00000437729.1; ENSG00000089041.17. [Q99572-3]
DR GeneID; 5027; -.
DR KEGG; hsa:5027; -.
DR MANE-Select; ENST00000328963.10; ENSP00000330696.6; NM_002562.6; NP_002553.3.
DR UCSC; uc001tzm.4; human. [Q99572-1]
DR CTD; 5027; -.
DR DisGeNET; 5027; -.
DR GeneCards; P2RX7; -.
DR HGNC; HGNC:8537; P2RX7.
DR HPA; ENSG00000089041; Tissue enhanced (brain).
DR MalaCards; P2RX7; -.
DR MIM; 602566; gene.
DR neXtProt; NX_Q99572; -.
DR OpenTargets; ENSG00000089041; -.
DR Orphanet; 67038; B-cell chronic lymphocytic leukemia.
DR PharmGKB; PA32866; -.
DR VEuPathDB; HostDB:ENSG00000089041; -.
DR eggNOG; ENOG502QSBN; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR HOGENOM; CLU_034469_7_0_1; -.
DR InParanoid; Q99572; -.
DR OMA; YRKKCET; -.
DR OrthoDB; 1128763at2759; -.
DR TreeFam; TF328633; -.
DR PathwayCommons; Q99572; -.
DR Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-HSA-418346; Platelet homeostasis.
DR Reactome; R-HSA-844456; The NLRP3 inflammasome.
DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR SignaLink; Q99572; -.
DR SIGNOR; Q99572; -.
DR BioGRID-ORCS; 5027; 34 hits in 1074 CRISPR screens.
DR ChiTaRS; P2RX7; human.
DR GeneWiki; P2RX7; -.
DR GenomeRNAi; 5027; -.
DR Pharos; Q99572; Tchem.
DR PRO; PR:Q99572; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q99572; protein.
DR Bgee; ENSG00000089041; Expressed in inferior vagus X ganglion and 165 other tissues.
DR ExpressionAtlas; Q99572; baseline and differential.
DR Genevisible; Q99572; HS.
DR GO; GO:0032059; C:bleb; ISS:BHF-UCL.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:BHF-UCL.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IC:BHF-UCL.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISS:BHF-UCL.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IDA:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; ISS:BHF-UCL.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISS:BHF-UCL.
DR GO; GO:0032060; P:bleb assembly; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; TAS:ARUK-UCL.
DR GO; GO:0035585; P:calcium-mediated signaling using extracellular calcium source; TAS:ARUK-UCL.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:1905114; P:cell surface receptor signaling pathway involved in cell-cell signaling; TAS:ARUK-UCL.
DR GO; GO:0071318; P:cellular response to ATP; TAS:ARUK-UCL.
DR GO; GO:0071359; P:cellular response to dsRNA; IEA:Ensembl.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
DR GO; GO:0046513; P:ceramide biosynthetic process; IEA:Ensembl.
DR GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:BHF-UCL.
DR GO; GO:0014051; P:gamma-aminobutyric acid secretion; IEA:Ensembl.
DR GO; GO:0014047; P:glutamate secretion; IEA:Ensembl.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0051899; P:membrane depolarization; IDA:BHF-UCL.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:Ensembl.
DR GO; GO:0051882; P:mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR GO; GO:0043132; P:NAD transport; IEA:Ensembl.
DR GO; GO:0045779; P:negative regulation of bone resorption; ISS:BHF-UCL.
DR GO; GO:0045794; P:negative regulation of cell volume; IMP:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISS:BHF-UCL.
DR GO; GO:0001845; P:phagolysosome assembly; IEA:Ensembl.
DR GO; GO:0006649; P:phospholipid transfer to membrane; IEA:Ensembl.
DR GO; GO:0017121; P:plasma membrane phospholipid scrambling; IDA:UniProtKB.
DR GO; GO:0046931; P:pore complex assembly; IDA:BHF-UCL.
DR GO; GO:1904172; P:positive regulation of bleb assembly; IMP:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:BHF-UCL.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IDA:BHF-UCL.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; ISS:BHF-UCL.
DR GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:CACAO.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; IEA:Ensembl.
DR GO; GO:0045821; P:positive regulation of glycolytic process; IMP:CACAO.
DR GO; GO:0032730; P:positive regulation of interleukin-1 alpha production; IEA:Ensembl.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:BHF-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0034767; P:positive regulation of ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IEA:Ensembl.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; IEA:Ensembl.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0070234; P:positive regulation of T cell apoptotic process; IEA:Ensembl.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0032310; P:prostaglandin secretion; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR GO; GO:0009306; P:protein secretion; IEA:Ensembl.
DR GO; GO:0035590; P:purinergic nucleotide receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0051709; P:regulation of killing of cells of another organism; NAS:BHF-UCL.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISS:BHF-UCL.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:0033198; P:response to ATP; IDA:BHF-UCL.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; NAS:ARUK-UCL.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
DR GO; GO:0019233; P:sensory perception of pain; ISS:BHF-UCL.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0070231; P:T cell apoptotic process; IEA:Ensembl.
DR GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR GO; GO:0006900; P:vesicle budding from membrane; IEA:Ensembl.
DR Gene3D; 2.60.490.10; -; 1.
DR InterPro; IPR003050; P2X7_purinoceptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR PANTHER; PTHR10125:SF13; PTHR10125:SF13; 1.
DR PRINTS; PR01314; P2X7RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR TIGRFAMs; TIGR00863; P2X; 1.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..595
FT /note="P2X purinoceptor 7"
FT /id="PRO_0000161560"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 125
FT /note="ADP-ribosylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 133
FT /note="ADP-ribosylarginine"
FT /evidence="ECO:0000250"
FT MOD_RES 343
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11707406"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20450227"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20450227"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20450227"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20450227"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20450227"
FT DISULFID 119..168
FT /evidence="ECO:0000250"
FT DISULFID 129..152
FT /evidence="ECO:0000250"
FT DISULFID 135..162
FT /evidence="ECO:0000250"
FT DISULFID 216..226
FT /evidence="ECO:0000250"
FT DISULFID 260..269
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..98
FT /note="MPACCSCSDVFQYETNKVTRIQSMNYGTIKWFFHVIIFSYVCFALVSDKLYQ
FT RKEPVISSVHTKVKGIAEVKEEIVENGVKKLVHSVFDTADYTFPLQ -> MTPGDHSW
FT (in isoform G and isoform H)"
FT /evidence="ECO:0000303|PubMed:15896293"
FT /id="VSP_047776"
FT VAR_SEQ 1..7
FT /note="MPACCSC -> MDGPAEQ (in isoform D)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15896293"
FT /id="VSP_047777"
FT VAR_SEQ 1..3
FT /note="MPA -> MWQ (in isoform F)"
FT /evidence="ECO:0000303|PubMed:15896293"
FT /id="VSP_047778"
FT VAR_SEQ 4..292
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000303|PubMed:15896293"
FT /id="VSP_047779"
FT VAR_SEQ 8..177
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15896293"
FT /id="VSP_047780"
FT VAR_SEQ 122..128
FT /note="YPTRRTL -> EFRPEGV (in isoform C)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15896293"
FT /id="VSP_047781"
FT VAR_SEQ 129..595
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15896293"
FT /id="VSP_047782"
FT VAR_SEQ 206..294
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:15896293"
FT /id="VSP_047783"
FT VAR_SEQ 347..364
FT /note="AAVFIDFLIDTYSSNCCR -> VRDSLFHALGKWFGEGSD (in isoform
FT B, isoform E and isoform G)"
FT /evidence="ECO:0000303|PubMed:15896293"
FT /id="VSP_047784"
FT VAR_SEQ 365..595
FT /note="Missing (in isoform B, isoform E and isoform G)"
FT /evidence="ECO:0000303|PubMed:15896293"
FT /id="VSP_047785"
FT VARIANT 25
FT /note="N -> S (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036444"
FT VARIANT 76
FT /note="V -> A (in dbSNP:rs17525809)"
FT /evidence="ECO:0000269|PubMed:23303206,
FT ECO:0000269|PubMed:28326637"
FT /id="VAR_057665"
FT VARIANT 117
FT /note="R -> W (in dbSNP:rs28360445)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_079880"
FT VARIANT 125
FT /note="R -> L (in dbSNP:rs201668926)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_079881"
FT VARIANT 148
FT /note="Q -> R (in dbSNP:rs150235326)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_079882"
FT VARIANT 150
FT /note="G -> R (decreases cell surface expression; decreases
FT phagocytosis activity; dbSNP:rs28360447)"
FT /evidence="ECO:0000269|PubMed:23303206,
FT ECO:0000269|PubMed:28326637"
FT /id="VAR_057666"
FT VARIANT 155
FT /note="Y -> H (in dbSNP:rs208294)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15896293, ECO:0000269|PubMed:23303206,
FT ECO:0000269|PubMed:28326637, ECO:0000269|PubMed:9038151,
FT ECO:0000269|PubMed:9826911"
FT /id="VAR_019649"
FT VARIANT 205
FT /note="T -> M (may influence susceptibility to multiple
FT sclerosis in the presence of variant S-135 in P2RX4;
FT decreases cell surface expression; decreases pore complex
FT assembly; decreases phagocytosis activity;
FT dbSNP:rs140915863)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_079883"
FT VARIANT 264
FT /note="R -> H (in dbSNP:rs149639375)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_079884"
FT VARIANT 270
FT /note="R -> C (in dbSNP:rs16950860)"
FT /id="VAR_057667"
FT VARIANT 270
FT /note="R -> H (in dbSNP:rs7958311)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15896293, ECO:0000269|PubMed:23303206,
FT ECO:0000269|PubMed:28326637, ECO:0000269|PubMed:9038151"
FT /id="VAR_019648"
FT VARIANT 276
FT /note="R -> H (in dbSNP:rs7958316)"
FT /evidence="ECO:0000269|PubMed:23303206,
FT ECO:0000269|PubMed:28326637"
FT /id="VAR_057668"
FT VARIANT 288
FT /note="Y -> H (in dbSNP:rs146725537)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_079885"
FT VARIANT 307
FT /note="R -> Q (results in a loss of function;
FT dbSNP:rs28360457)"
FT /evidence="ECO:0000269|PubMed:15123679,
FT ECO:0000269|PubMed:23303206, ECO:0000269|PubMed:28326637"
FT /id="VAR_057669"
FT VARIANT 348
FT /note="A -> T (in dbSNP:rs1718119)"
FT /evidence="ECO:0000269|PubMed:23303206,
FT ECO:0000269|PubMed:28326637, ECO:0000269|PubMed:9826911"
FT /id="VAR_057670"
FT VARIANT 357
FT /note="T -> S (in dbSNP:rs2230911)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:23303206, ECO:0000269|PubMed:28326637"
FT /id="VAR_019650"
FT VARIANT 361
FT /note="N -> S (may influence susceptibility to multiple
FT sclerosis in the presence of variant S-135 in P2RX4; no
FT effect on cell surface expression; no effect on pore
FT complex assembly; dbSNP:rs201921967)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_079886"
FT VARIANT 430
FT /note="P -> R (in dbSNP:rs10160951)"
FT /id="VAR_057671"
FT VARIANT 433
FT /note="A -> V (in dbSNP:rs28360459)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_057672"
FT VARIANT 460
FT /note="Q -> R (in dbSNP:rs2230912)"
FT /evidence="ECO:0000269|PubMed:23303206,
FT ECO:0000269|PubMed:28326637"
FT /id="VAR_019651"
FT VARIANT 496
FT /note="E -> A (results in a loss of function;
FT dbSNP:rs3751143)"
FT /evidence="ECO:0000269|PubMed:11150303,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:23303206,
FT ECO:0000269|PubMed:28326637"
FT /id="VAR_019652"
FT VARIANT 521
FT /note="H -> Q (in dbSNP:rs2230913)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_057673"
FT VARIANT 522
FT /note="V -> I (in dbSNP:rs34219304)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_057674"
FT VARIANT 535
FT /note="A -> V (in dbSNP:rs201256156)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_079887"
FT VARIANT 544
FT /note="R -> Q (in dbSNP:rs34567077)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_079888"
FT VARIANT 568
FT /note="I -> N (results in trafficking defect and around 50%
FT loss of function; dbSNP:rs1653624)"
FT /evidence="ECO:0000269|PubMed:12586825,
FT ECO:0000269|PubMed:16541075, ECO:0000269|PubMed:23303206,
FT ECO:0000269|PubMed:28326637"
FT /id="VAR_068011"
FT VARIANT 574
FT /note="R -> L (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036445"
FT VARIANT 578
FT /note="R -> Q (in dbSNP:rs28360460)"
FT /id="VAR_057675"
FT MUTAGEN 187
FT /note="N->A: Alters cell surface expression."
FT /evidence="ECO:0000269|PubMed:20450227"
FT CONFLICT 481
FT /note="S -> R (in Ref. 2; CAA73360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 68585 MW; 584C17EF6D5EC899 CRC64;
MPACCSCSDV FQYETNKVTR IQSMNYGTIK WFFHVIIFSY VCFALVSDKL YQRKEPVISS
VHTKVKGIAE VKEEIVENGV KKLVHSVFDT ADYTFPLQGN SFFVMTNFLK TEGQEQRLCP
EYPTRRTLCS SDRGCKKGWM DPQSKGIQTG RCVVYEGNQK TCEVSAWCPI EAVEEAPRPA
LLNSAENFTV LIKNNIDFPG HNYTTRNILP GLNITCTFHK TQNPQCPIFR LGDIFRETGD
NFSDVAIQGG IMGIEIYWDC NLDRWFHHCR PKYSFRRLDD KTTNVSLYPG YNFRYAKYYK
ENNVEKRTLI KVFGIRFDIL VFGTGGKFDI IQLVVYIGST LSYFGLAAVF IDFLIDTYSS
NCCRSHIYPW CKCCQPCVVN EYYYRKKCES IVEPKPTLKY VSFVDESHIR MVNQQLLGRS
LQDVKGQEVP RPAMDFTDLS RLPLALHDTP PIPGQPEEIQ LLRKEATPRS RDSPVWCQCG
SCLPSQLPES HRCLEELCCR KKPGACITTS ELFRKLVLSR HVLQFLLLYQ EPLLALDVDS
TNSRLRHCAY RCYATWRFGS QDMADFAILP SCCRWRIRKE FPKSEGQYSG FKSPY
