ADCY7_HUMAN
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 03-AUG-2022, entry version 180.
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};
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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; 11.
DR IntAct; P51828; 4.
DR STRING; 9606.ENSP00000378187; -.
DR BindingDB; P51828; -.
DR ChEMBL; CHEMBL2097167; -.
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; P51828; -.
DR PeptideAtlas; P51828; -.
DR PRIDE; P51828; -.
DR ProteomicsDB; 56430; -.
DR Antibodypedia; 28237; 169 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 CTD; 113; -.
DR DisGeNET; 113; -.
DR GeneCards; ADCY7; -.
DR HGNC; HGNC:238; ADCY7.
DR HPA; ENSG00000121281; Low tissue specificity.
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; PRSKQCL; -.
DR OrthoDB; 363718at2759; -.
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; 16 hits in 1075 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 184 other tissues.
DR ExpressionAtlas; P51828; baseline and differential.
DR Genevisible; P51828; HS.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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; -; 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 Pfam; PF16214; AC_N; 1.
DR Pfam; PF06327; DUF1053; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR PIRSF; PIRSF039050; Ade_cyc; 1.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; SSF55073; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
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
