ID ADCY7_HUMAN Reviewed; 1080 AA. AC P51828; A0AVA6; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 24-JAN-2024, entry version 188. DE RecName: Full=Adenylate cyclase type 7 {ECO:0000305}; DE EC=4.6.1.1 {ECO:0000305|PubMed:18541530, ECO:0000305|PubMed:23229509}; DE AltName: Full=ATP pyrophosphate-lyase 7; DE AltName: Full=Adenylate cyclase type VII; DE AltName: Full=Adenylyl cyclase 7; GN Name=ADCY7 {ECO:0000312|HGNC:HGNC:238}; GN Synonyms=KIAA0037 {ECO:0000303|PubMed:7584026}; 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 [LARGE SCALE MRNA]. RC TISSUE=Bone marrow; RX PubMed=7584026; DOI=10.1093/dnares/1.1.27; RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., RA Nagase T., Seki N., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. I. The RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of RT randomly sampled cDNA clones from human immature myeloid cell line KG-1."; RL DNA Res. 1:27-35(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP PHOSPHORYLATION, AND ACTIVITY REGULATION. RX PubMed=12454008; DOI=10.1074/jbc.m210386200; RA Nelson E.J., Hellevuo K., Yoshimura M., Tabakoff B.; RT "Ethanol-induced phosphorylation and potentiation of the activity of type 7 RT adenylyl cyclase. Involvement of protein kinase C delta."; RL J. Biol. Chem. 278:4552-4560(2003). RN [5] RP REGION. RX PubMed=15581358; DOI=10.1021/bi049088+; RA Beeler J.A., Yan S.Z., Bykov S., Murza A., Asher S., Tang W.J.; RT "A soluble C1b protein and its regulation of soluble type 7 adenylyl RT cyclase."; RL Biochemistry 43:15463-15471(2004). RN [6] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=18541530; DOI=10.1074/jbc.m803281200; RA Jiang L.I., Collins J., Davis R., Fraser I.D., Sternweis P.C.; RT "Regulation of cAMP responses by the G12/13 pathway converges on adenylyl RT cyclase VII."; RL J. Biol. Chem. 283:23429-23439(2008). RN [7] RP FUNCTION, REGION, MUTAGENESIS OF 477-LYS--VAL-482; 485-THR--SER-490; RP 491-TRP--PRO-496; 494-ALA--HIS-499 AND 564-SER--PHE-569, AND ACTIVITY RP REGULATION. RX PubMed=23229509; DOI=10.1124/mol.112.082446; RA Jiang L.I., Wang J.E., Sternweis P.C.; RT "Regions on adenylyl cyclase VII required for selective regulation by the RT G13 pathway."; RL Mol. Pharmacol. 83:587-593(2013). RN [8] RP FUNCTION. RX PubMed=23842570; DOI=10.1124/mol.113.087288; RA Ehrlich A.T., Furuyashiki T., Kitaoka S., Kakizuka A., Narumiya S.; RT "Prostaglandin E receptor EP1 forms a complex with dopamine D1 receptor and RT directs D1-induced cAMP production to adenylyl cyclase 7 through mobilizing RT G(betagamma) subunits in human embryonic kidney 293T cells."; RL Mol. Pharmacol. 84:476-486(2013). CC -!- FUNCTION: Catalyzes the formation of cAMP in response to activation of CC G protein-coupled receptors (Probable). Functions in signaling cascades CC activated namely by thrombin and sphingosine 1-phosphate and mediates CC regulation of cAMP synthesis through synergistic action of the CC stimulatory G alpha protein with GNA13 (PubMed:23229509, CC PubMed:18541530). Also, during inflammation, mediates zymosan-induced CC increase intracellular cAMP, leading to protein kinase A pathway CC activation in order to modulate innate immune responses through CC heterotrimeric G proteins G(12/13) (By similarity). Functions in CC signaling cascades activated namely by dopamine and C5 alpha chain and CC mediates regulation of cAMP synthesis through synergistic action of the CC stimulatory G protein with G beta:gamma complex (PubMed:23842570, CC PubMed:23229509). Functions, through cAMP response regulation, to keep CC inflammation under control during bacterial infection by sensing the CC presence of serum factors, such as the bioactive lysophospholipid (LPA) CC that regulate LPS-induced TNF-alpha production. However, it is also CC required for the optimal functions of B and T cells during adaptive CC immune responses by regulating cAMP synthesis in both B and T cells (By CC similarity). {ECO:0000250|UniProtKB:P51829, CC ECO:0000269|PubMed:18541530, ECO:0000269|PubMed:23229509, CC ECO:0000269|PubMed:23842570, ECO:0000305|PubMed:18541530, CC ECO:0000305|PubMed:23229509}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; CC Evidence={ECO:0000305|PubMed:18541530, ECO:0000305|PubMed:23229509}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P30803}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:P30803}; CC Note=Binds 2 magnesium ions per subunit. Is also active with manganese CC (in vitro). {ECO:0000250|UniProtKB:P30803}; CC -!- ACTIVITY REGULATION: Activated by the G protein alpha subunit CC (PubMed:18541530). Activated by the G protein beta and gamma subunit CC complex (PubMed:23229509). Activated by GNA13 and GNA12 CC (PubMed:18541530). Ethanol and phorbol 12,13-dibutanoate significantly CC potentiate adenylate cyclase activity generated in response to the CC activation of the prostanoid receptor by the agonist prostaglandin CC E1(1-) in a PKC-dependent manner (PubMed:12454008). Inhibited by CC lithium (By similarity). {ECO:0000250|UniProtKB:P51829, CC ECO:0000269|PubMed:12454008, ECO:0000269|PubMed:18541530, CC ECO:0000269|PubMed:23229509}. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- DOMAIN: The protein contains two modules with six transmembrane helices CC each; both are required for catalytic activity. Isolated N-terminal or CC C-terminal guanylate cyclase domains have no catalytic activity, but CC when they are brought together, enzyme activity is restored. The active CC site is at the interface of the two domains. Both contribute substrate- CC binding residues, but the catalytic metal ions are bound exclusively CC via the N-terminal guanylate cyclase domain. CC {ECO:0000250|UniProtKB:P26769}. CC -!- PTM: Phosphorylated by PRKCD. {ECO:0000269|PubMed:12454008}. CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA05021.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D25538; BAA05021.2; ALT_INIT; mRNA. DR EMBL; AC007597; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC126271; AAI26272.1; -; mRNA. DR CCDS; CCDS10741.1; -. DR PIR; PN0453; PN0453. DR RefSeq; NP_001105.1; NM_001114.4. DR RefSeq; XP_016878384.1; XM_017022895.1. DR AlphaFoldDB; P51828; -. DR SMR; P51828; -. DR BioGRID; 106626; 12. DR IntAct; P51828; 4. DR STRING; 9606.ENSP00000501053; -. DR BindingDB; P51828; -. DR ChEMBL; CHEMBL2097167; -. DR DrugBank; DB02587; Colforsin. DR GlyCosmos; P51828; 3 sites, No reported glycans. DR GlyGen; P51828; 3 sites. DR iPTMnet; P51828; -. DR PhosphoSitePlus; P51828; -. DR SwissPalm; P51828; -. DR BioMuta; ADCY7; -. DR DMDM; 1706218; -. DR EPD; P51828; -. DR jPOST; P51828; -. DR MassIVE; P51828; -. DR MaxQB; P51828; -. DR PaxDb; 9606-ENSP00000378187; -. DR PeptideAtlas; P51828; -. DR ProteomicsDB; 56430; -. DR Antibodypedia; 28237; 186 antibodies from 28 providers. DR DNASU; 113; -. DR Ensembl; ENST00000254235.7; ENSP00000254235.3; ENSG00000121281.13. DR Ensembl; ENST00000394697.7; ENSP00000378187.2; ENSG00000121281.13. DR Ensembl; ENST00000673801.1; ENSP00000501053.1; ENSG00000121281.13. DR GeneID; 113; -. DR KEGG; hsa:113; -. DR MANE-Select; ENST00000673801.1; ENSP00000501053.1; NM_001114.5; NP_001105.1. DR UCSC; uc002egd.3; human. DR AGR; HGNC:238; -. DR CTD; 113; -. DR DisGeNET; 113; -. DR GeneCards; ADCY7; -. DR HGNC; HGNC:238; ADCY7. DR HPA; ENSG00000121281; Tissue enhanced (lymphoid). DR MIM; 600385; gene. DR neXtProt; NX_P51828; -. DR OpenTargets; ENSG00000121281; -. DR PharmGKB; PA28; -. DR VEuPathDB; HostDB:ENSG00000121281; -. DR eggNOG; KOG3619; Eukaryota. DR GeneTree; ENSGT00940000159096; -. DR HOGENOM; CLU_001072_2_5_1; -. DR InParanoid; P51828; -. DR OMA; LIMPKTA; -. DR OrthoDB; 3686360at2759; -. DR PhylomeDB; P51828; -. DR TreeFam; TF313845; -. DR BRENDA; 4.6.1.1; 2681. DR PathwayCommons; P51828; -. DR Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation. DR Reactome; R-HSA-163615; PKA activation. DR Reactome; R-HSA-164378; PKA activation in glucagon signalling. DR Reactome; R-HSA-170660; Adenylate cyclase activating pathway. DR Reactome; R-HSA-170670; Adenylate cyclase inhibitory pathway. DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-418597; G alpha (z) signalling events. DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins. DR Reactome; R-HSA-5610787; Hedgehog 'off' state. DR Reactome; R-HSA-9634597; GPER1 signaling. DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production. DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis. DR SignaLink; P51828; -. DR SIGNOR; P51828; -. DR BioGRID-ORCS; 113; 18 hits in 1157 CRISPR screens. DR ChiTaRS; ADCY7; human. DR GeneWiki; ADCY7; -. DR GenomeRNAi; 113; -. DR Pharos; P51828; Tbio. DR PRO; PR:P51828; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P51828; Protein. DR Bgee; ENSG00000121281; Expressed in granulocyte and 186 other cell types or tissues. DR ExpressionAtlas; P51828; baseline and differential. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0006171; P:cAMP biosynthetic process; IDA:UniProtKB. DR GO; GO:0071361; P:cellular response to ethanol; IDA:UniProtKB. DR GO; GO:0071285; P:cellular response to lithium ion; ISS:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl. DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISS:UniProtKB. DR GO; GO:0002819; P:regulation of adaptive immune response; ISS:UniProtKB. DR CDD; cd07302; CHD; 2. DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 2. DR InterPro; IPR001054; A/G_cyclase. DR InterPro; IPR018297; A/G_cyclase_CS. DR InterPro; IPR032628; AC_N. DR InterPro; IPR030672; Adcy. DR InterPro; IPR009398; Adcy_conserved_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1. DR PANTHER; PTHR45627:SF9; ADENYLATE CYCLASE TYPE 7; 1. DR Pfam; PF16214; AC_N; 1. DR Pfam; PF06327; Adcy_cons_dom; 1. DR Pfam; PF00211; Guanylate_cyc; 2. DR PIRSF; PIRSF039050; Ade_cyc; 1. DR SMART; SM00044; CYCc; 2. DR SUPFAM; SSF55073; Nucleotide cyclase; 2. DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1. DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2. DR Genevisible; P51828; HS. PE 1: Evidence at protein level; KW ATP-binding; cAMP biosynthesis; Glycoprotein; Lyase; Magnesium; Manganese; KW Membrane; Metal-binding; Nucleotide-binding; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix. FT CHAIN 1..1080 FT /note="Adenylate cyclase type 7" FT /id="PRO_0000195703" FT TOPO_DOM 1..33 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 34..54 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 63..83 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 95..117 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 122..142 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 147..167 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 176..196 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 197..594 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 595..615 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 620..640 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 669..688 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 718..737 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 746..773 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 794..814 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 815..1080 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 279..406 FT /note="Guanylate cyclase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099" FT DOMAIN 879..1023 FT /note="Guanylate cyclase 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099" FT REGION 454..474 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 477..482 FT /note="Mediates regulation of adenylate cyclase activity by FT C5 alpha-induced G- beta and gamma pathway" FT /evidence="ECO:0000269|PubMed:23229509" FT REGION 491..499 FT /note="Mediates regulation of adenylate cyclase activity by FT sphingosine 1-phosphate-induced G alpha 13 pathway" FT /evidence="ECO:0000269|PubMed:23229509" FT REGION 504..546 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 506..584 FT /note="Modulates adenylate cyclase activity by modulating FT the binding of G(s)alpha to the high-affinity G(s)alpha FT binding site in 7C1a/7C2" FT /evidence="ECO:0000269|PubMed:15581358" FT COMPBIAS 526..546 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 284..289 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P30803" FT BINDING 284 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099" FT BINDING 284 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099" FT BINDING 285 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099" FT BINDING 326..328 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P30803" FT BINDING 328 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099" FT BINDING 328 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099" FT BINDING 372 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P30803" FT BINDING 931 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P26769" FT BINDING 1010..1012 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P26769" FT BINDING 1017..1021 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P26769" FT BINDING 1057 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P26769" FT CARBOHYD 701 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 776 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 781 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT MUTAGEN 477..482 FT /note="KMRASV->NAAIRS: Does not affect cAMP biosynthetic FT process in response to sphingosine 1-phosphate stimulation. FT Reduces by 40% cAMP biosynthetic process in response to C5 FT alpha chain stimulation." FT /evidence="ECO:0000269|PubMed:23229509" FT MUTAGEN 485..489 FT /note="TRYLE->NAAIR: Reduces cAMP biosynthetic process in FT response to C5 alpha chain stimulation and more severely in FT response to sphingosine 1-phosphate stimulation." FT /evidence="ECO:0000269|PubMed:23229509" FT MUTAGEN 491..496 FT /note="WGAARP->NAAIRS: Does not affect cAMP biosynthetic FT process in response to C5 alpha chain stimulation. Reduces FT by 40?60% cAMP biosynthetic process in response to FT sphingosine 1-phosphate stimulation." FT /evidence="ECO:0000269|PubMed:23229509" FT MUTAGEN 494..499 FT /note="ARPFAH->NAAIRS: Does not affect cAMP biosynthetic FT process in response to C5 alpha chain stimulation. Reduces FT by 40?60% cAMP biosynthetic process in response to FT sphingosine 1-phosphate stimulation." FT /evidence="ECO:0000269|PubMed:23229509" FT MUTAGEN 564..569 FT /note="SKSDDF->NAAIRS: Reduces cAMP biosynthetic process in FT response to C5 alpha chain stimulation and more severely in FT response to sphingosine 1-phosphate stimulation." FT /evidence="ECO:0000269|PubMed:23229509" SQ SEQUENCE 1080 AA; 120308 MW; E33951621E281242 CRC64; MPAKGRYFLN EGEEGPDQDA LYEKYQLTSQ HGPLLLTLLL VAATACVALI IIAFSQGDPS RHQAILGMAF LVLAVFAALS VLMYVECLLR RWLRALALLT WACLVALGYV LVFDAWTKAA CAWEQVPFFL FIVFVVYTLL PFSMRGAVAV GAVSTASHLL VLGSLMGGFT TPSVRVGLQL LANAVIFLCG NLTGAFHKHQ MQDASRDLFT YTVKCIQIRR KLRIEKRQQE NLLLSVLPAH ISMGMKLAII ERLKEHGDRR CMPDNNFHSL YVKRHQNVSI LYADIVGFTQ LASDCSPKEL VVVLNELFGK FDQIAKANEC MRIKILGDCY YCVSGLPVSL PTHARNCVKM GLDMCQAIKQ VREATGVDIN MRVGIHSGNV LCGVIGLRKW QYDVWSHDVS LANRMEAAGV PGRVHITEAT LKHLDKAYEV EDGHGQQRDP YLKEMNIRTY LVIDPRSQQP PPPSQHLPRP KGDAALKMRA SVRMTRYLES WGAARPFAHL NHRESVSSGE THVPNGRRPK SVPQRHRRTP DRSMSPKGRS EDDSYDDEML SAIEGLSSTR PCCSKSDDFY TFGSIFLEKG FEREYRLAPI PRARHDFACA SLIFVCILLV HVLLMPRTAA LGVSFGLVAC VLGLVLGLCF ATKFSRCCPA RGTLCTISER VETQPLLRLT LAVLTIGSLL TVAIINLPLM PFQVPELPVG NETGLLAASS KTRALCEPLP YYTCSCVLGF IACSVFLRMS LEPKVVLLTV ALVAYLVLFN LSPCWQWDCC GQGLGNLTKP NGTTSGTPSC SWKDLKTMTN FYLVLFYITL LTLSRQIDYY CRLDCLWKKK FKKEHEEFET MENVNRLLLE NVLPAHVAAH FIGDKLNEDW YHQSYDCVCV MFASVPDFKV FYTECDVNKE GLECLRLLNE IIADFDELLL KPKFSGVEKI KTIGSTYMAA AGLSVASGHE NQELERQHAH IGVMVEFSIA LMSKLDGINR HSFNSFRLRV GINHGPVIAG VIGARKPQYD IWGNTVNVAS RMESTGELGK IQVTEETCTI LQGLGYSCEC RGLINVKGKG ELRTYFVCTD TAKFQGLGLN //