P2Y11_HUMAN
ID P2Y11_HUMAN Reviewed; 374 AA.
AC Q96G91; B2R8X9; O43190; Q9BYU4; Q9H170;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=P2Y purinoceptor 11;
DE Short=P2Y11;
GN Name=P2RY11;
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], TISSUE SPECIFICITY, AND TRANS-SPLICING.
RC TISSUE=Placenta, and Promyelocyte;
RX PubMed=11278528; DOI=10.1074/jbc.m009609200;
RA Communi D., Suarez-Huerta N., Dussossoy D., Savi P., Boeynaems J.-M.;
RT "Cotranscription and intergenic splicing of human P2Y11 and SSF1 genes.";
RL J. Biol. Chem. 276:16561-16566(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RA King M.M., Aronstam R.S., Sharma S.V.;
RT "Isolation of cDNA coding for purinergic receptor P2Y, G protein-coupled,
RT 11 (P2RY11).";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-374.
RC TISSUE=Placenta;
RX PubMed=9405388; DOI=10.1074/jbc.272.51.31969;
RA Communi D., Govaerts C., Parmentier M., Boeynaems J.-M.;
RT "Cloning of a human purinergic P2Y receptor coupled to phospholipase C and
RT adenylyl cyclase.";
RL J. Biol. Chem. 272:31969-31973(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 162-374.
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for ATP and ADP coupled to G-proteins that activate
CC both phosphatidylinositol-calcium and adenylyl cyclase second messenger
CC systems. Not activated by UTP or UDP.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Highest expression in liver and spleen.
CC {ECO:0000269|PubMed:11278528}.
CC -!- INDUCTION: Increased by DMSO and retinoic acid.
CC -!- MISCELLANEOUS: A chimeric transcript, characterized by the first third
CC of PPAN exon 12 joined to P2RY11 exon 2, has been detected. It is
CC possibly produced by trans-splicing. The chimeric transcript is widely
CC expressed and can be induced by retinoic acid during the granulocytic
CC differentiation of the HL-60 cell line. The resulting chimeric protein
CC shows a much lower activity than the non-chimeric P2RY11 gene product,
CC but qualitatively indistinguishable (PubMed:11278528).
CC {ECO:0000305|PubMed:11278528}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB88674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC18877.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF030335; AAB88674.1; ALT_INIT; mRNA.
DR EMBL; AJ298334; CAC29362.1; -; mRNA.
DR EMBL; AJ300588; CAC18877.1; ALT_INIT; mRNA.
DR EMBL; AY449733; AAR18077.1; -; mRNA.
DR EMBL; AK313550; BAG36326.1; -; mRNA.
DR EMBL; CH471106; EAW84077.1; -; Genomic_DNA.
DR EMBL; BC073827; AAH73827.1; -; mRNA.
DR EMBL; AF498921; AAM18130.1; -; mRNA.
DR CCDS; CCDS12226.1; -.
DR RefSeq; NP_002557.2; NM_002566.4.
DR AlphaFoldDB; Q96G91; -.
DR SMR; Q96G91; -.
DR BioGRID; 111071; 6.
DR IntAct; Q96G91; 1.
DR STRING; 9606.ENSP00000323872; -.
DR BindingDB; Q96G91; -.
DR ChEMBL; CHEMBL4867; -.
DR DrugBank; DB00171; ATP.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; Q96G91; -.
DR GuidetoPHARMACOLOGY; 327; -.
DR GlyGen; Q96G91; 2 sites.
DR iPTMnet; Q96G91; -.
DR PhosphoSitePlus; Q96G91; -.
DR BioMuta; P2RY11; -.
DR DMDM; 21263830; -.
DR MassIVE; Q96G91; -.
DR PaxDb; Q96G91; -.
DR PeptideAtlas; Q96G91; -.
DR PRIDE; Q96G91; -.
DR ProteomicsDB; 76604; -.
DR Antibodypedia; 35031; 256 antibodies from 31 providers.
DR DNASU; 5032; -.
DR Ensembl; ENST00000321826.5; ENSP00000323872.4; ENSG00000244165.2.
DR GeneID; 5032; -.
DR KEGG; hsa:5032; -.
DR MANE-Select; ENST00000321826.5; ENSP00000323872.4; NM_002566.5; NP_002557.2.
DR UCSC; uc002mnc.4; human.
DR CTD; 5032; -.
DR DisGeNET; 5032; -.
DR GeneCards; P2RY11; -.
DR HGNC; HGNC:8540; P2RY11.
DR HPA; ENSG00000244165; Low tissue specificity.
DR MalaCards; P2RY11; -.
DR MIM; 602697; gene.
DR neXtProt; NX_Q96G91; -.
DR OpenTargets; ENSG00000244165; -.
DR Orphanet; 2073; Narcolepsy type 1.
DR PharmGKB; PA32869; -.
DR VEuPathDB; HostDB:ENSG00000244165; -.
DR GeneTree; ENSGT01030000234518; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q96G91; -.
DR OMA; RVACCGK; -.
DR OrthoDB; 353508at2759; -.
DR PhylomeDB; Q96G91; -.
DR TreeFam; TF330775; -.
DR PathwayCommons; Q96G91; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-417957; P2Y receptors.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; Q96G91; -.
DR SIGNOR; Q96G91; -.
DR BioGRID-ORCS; 5032; 16 hits in 1032 CRISPR screens.
DR GeneWiki; P2RY11; -.
DR GenomeRNAi; 5032; -.
DR Pharos; Q96G91; Tchem.
DR PRO; PR:Q96G91; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96G91; protein.
DR Bgee; ENSG00000244165; Expressed in granulocyte and 93 other tissues.
DR Genevisible; Q96G91; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045031; F:G protein-coupled ATP receptor activity; IDA:BHF-UCL.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IDA:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:BHF-UCL.
DR GO; GO:0071318; P:cellular response to ATP; IDA:BHF-UCL.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0023041; P:neuronal signal transduction; IDA:BHF-UCL.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR027677; P2Y11_rcpt.
DR PANTHER; PTHR24231:SF46; PTHR24231:SF46; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..374
FT /note="P2Y purinoceptor 11"
FT /id="PRO_0000070035"
FT TOPO_DOM 1..29
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 345..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 102..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 87
FT /note="A -> T (in dbSNP:rs3745601)"
FT /id="VAR_020074"
SQ SEQUENCE 374 AA; 40345 MW; C02DF9B3B381D25E CRC64;
MAANVSGAKS CPANFLAAAD DKLSGFQGDF LWPILVVEFL VAVASNGLAL YRFSIRKQRP
WHPAVVFSVQ LAVSDLLCAL TLPPLAAYLY PPKHWRYGEA ACRLERFLFT CNLLGSVIFI
TCISLNRYLG IVHPFFARSH LRPKHAWAVS AAGWVLAALL AMPTLSFSHL KRPQQGAGNC
SVARPEACIK CLGTADHGLA AYRAYSLVLA GLGCGLPLLL TLAAYGALGR AVLRSPGMTV
AEKLRVAALV ASGVALYASS YVPYHIMRVL NVDARRRWST RCPSFADIAQ ATAALELGPY
VGYQVMRGLM PLAFCVHPLL YMAAVPSLGC CCRHCPGYRD SWNPEDAKST GQALPLNATA
APKPSEPQSR ELSQ
