ADCY2_HUMAN
ID ADCY2_HUMAN Reviewed; 1091 AA.
AC Q08462; B7Z2C1; Q2NKL8; Q9UDB2; Q9UPU2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 5.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Adenylate cyclase type 2;
DE EC=4.6.1.1 {ECO:0000269|PubMed:15385642};
DE AltName: Full=ATP pyrophosphate-lyase 2;
DE AltName: Full=Adenylate cyclase type II;
DE AltName: Full=Adenylyl cyclase 2;
GN Name=ADCY2; Synonyms=KIAA1060;
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] (ISOFORM 1).
RA Guo J.H., Yu L.;
RT "Molecular cloning of human adenylyl cyclase gene.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-147.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 205-1091 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 616-1091 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=1427768; DOI=10.1007/bf00210755;
RA Stengel D., Parma J., Gannage M.-H., Roeckel N., Mattei M.-G., Barouki R.,
RA Hanoune J.;
RT "Different chromosomal localization of two adenylyl cyclase genes expressed
RT in human brain.";
RL Hum. Genet. 90:126-130(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 948-1017 (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8476432; DOI=10.1006/bbrc.1993.1415;
RA Hellevuo K., Yoshimura M., Kao M., Hoffman P.L., Cooper D.M.F.,
RA Tabakoff B.;
RT "A novel adenylyl cyclase sequence cloned from the human erythroleukemia
RT cell line.";
RL Biochem. Biophys. Res. Commun. 192:311-318(1993).
RN [8]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11549699; DOI=10.1210/jcem.86.9.7837;
RA Cote M., Guillon G., Payet M.D., Gallo-Payet N.;
RT "Expression and regulation of adenylyl cyclase isoforms in the human
RT adrenal gland.";
RL J. Clin. Endocrinol. Metab. 86:4495-4503(2001).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP PHOSPHORYLATION BY RAF1, SUBCELLULAR LOCATION, AND INTERACTION WITH RAF1.
RX PubMed=15385642; DOI=10.1124/mol.66.4.921;
RA Ding Q., Gros R., Gray I.D., Taussig R., Ferguson S.S., Feldman R.D.;
RT "Raf kinase activation of adenylyl cyclases: isoform-selective
RT regulation.";
RL Mol. Pharmacol. 66:921-928(2004).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=21228062; DOI=10.1124/jpet.110.177923;
RA Bogard A.S., Xu C., Ostrom R.S.;
RT "Human bronchial smooth muscle cells express adenylyl cyclase isoforms 2,
RT 4, and 6 in distinct membrane microdomains.";
RL J. Pharmacol. Exp. Ther. 337:209-217(2011).
CC -!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP in
CC response to G-protein signaling (PubMed:15385642). Down-stream
CC signaling cascades mediate changes in gene expression patterns and lead
CC to increased IL6 production. Functions in signaling cascades downstream
CC of the muscarinic acetylcholine receptors (By similarity).
CC {ECO:0000250|UniProtKB:P26769, ECO:0000269|PubMed:15385642}.
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:0000269|PubMed:15385642};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15385642};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15385642};
CC Note=Binds 2 magnesium ions per subunit. Is also active with manganese
CC (in vitro). {ECO:0000250|UniProtKB:P26769};
CC -!- ACTIVITY REGULATION: Activated by forskolin (PubMed:15385642). Is not
CC activated by calmodulin. Inhibited by calcium ions, already at
CC micromolar concentration. Activated by the G protein alpha subunit
CC GNAS. Activated by the G protein beta and gamma subunit complex (By
CC similarity). Phosphorylation by RAF1 results in its activation
CC (PubMed:15385642). Phosphorylation by PKC activates the enzyme (By
CC similarity). {ECO:0000250|UniProtKB:P26769,
CC ECO:0000269|PubMed:15385642}.
CC -!- SUBUNIT: Interacts with RAF1 (PubMed:15385642). Interacts with GNAS.
CC Interacts with the G protein beta and gamma subunit complex (By
CC similarity). {ECO:0000250|UniProtKB:P26769,
CC ECO:0000269|PubMed:15385642}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15385642}; Multi-
CC pass membrane protein {ECO:0000305}. Cell membrane
CC {ECO:0000269|PubMed:11549699, ECO:0000269|PubMed:21228062}; Multi-pass
CC membrane protein {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:11549699}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q08462-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08462-2; Sequence=VSP_055811, VSP_055812;
CC -!- TISSUE SPECIFICITY: Detected in zona glomerulosa and zona fasciculata
CC in the adrenal gland (at protein level) (PubMed:11549699). Expressed in
CC brain, especially in caudate nucleus, cerebellum and hippocampus.
CC {ECO:0000269|PubMed:11549699, ECO:0000269|PubMed:8476432}.
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 RAF1. {ECO:0000269|PubMed:15385642}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AF410885; AAP97285.1; -; mRNA.
DR EMBL; AK294555; BAH11807.1; -; mRNA.
DR EMBL; AC010346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC111743; AAI11744.1; -; mRNA.
DR EMBL; AB028983; BAA83012.1; -; mRNA.
DR EMBL; X74210; CAA52282.1; -; mRNA.
DR EMBL; L21993; AAA64923.1; -; mRNA.
DR CCDS; CCDS3872.2; -. [Q08462-1]
DR PIR; I37136; I37136.
DR RefSeq; NP_065433.2; NM_020546.2. [Q08462-1]
DR AlphaFoldDB; Q08462; -.
DR SMR; Q08462; -.
DR BioGRID; 106622; 10.
DR DIP; DIP-422N; -.
DR IntAct; Q08462; 3.
DR MINT; Q08462; -.
DR STRING; 9606.ENSP00000342952; -.
DR BindingDB; Q08462; -.
DR ChEMBL; CHEMBL3760; -.
DR DrugBank; DB06843; 2',5'-DIDEOXY-ADENOSINE 3'-MONOPHOSPHATE.
DR DrugBank; DB09121; Aurothioglucose.
DR DrugBank; DB02587; Colforsin.
DR GlyGen; Q08462; 2 sites.
DR iPTMnet; Q08462; -.
DR PhosphoSitePlus; Q08462; -.
DR BioMuta; ADCY2; -.
DR DMDM; 118572617; -.
DR EPD; Q08462; -.
DR jPOST; Q08462; -.
DR MassIVE; Q08462; -.
DR MaxQB; Q08462; -.
DR PaxDb; Q08462; -.
DR PeptideAtlas; Q08462; -.
DR PRIDE; Q08462; -.
DR ProteomicsDB; 58613; -. [Q08462-1]
DR ProteomicsDB; 6429; -.
DR Antibodypedia; 22409; 180 antibodies from 31 providers.
DR DNASU; 108; -.
DR Ensembl; ENST00000338316.9; ENSP00000342952.4; ENSG00000078295.17. [Q08462-1]
DR GeneID; 108; -.
DR KEGG; hsa:108; -.
DR MANE-Select; ENST00000338316.9; ENSP00000342952.4; NM_020546.3; NP_065433.2.
DR UCSC; uc003jdz.2; human. [Q08462-1]
DR CTD; 108; -.
DR DisGeNET; 108; -.
DR GeneCards; ADCY2; -.
DR HGNC; HGNC:233; ADCY2.
DR HPA; ENSG00000078295; Group enriched (brain, skeletal muscle, tongue).
DR MIM; 103071; gene.
DR neXtProt; NX_Q08462; -.
DR OpenTargets; ENSG00000078295; -.
DR PharmGKB; PA24561; -.
DR VEuPathDB; HostDB:ENSG00000078295; -.
DR eggNOG; KOG3619; Eukaryota.
DR GeneTree; ENSGT00940000156424; -.
DR HOGENOM; CLU_001072_2_5_1; -.
DR InParanoid; Q08462; -.
DR OMA; STMDVPM; -.
DR PhylomeDB; Q08462; -.
DR TreeFam; TF313845; -.
DR BRENDA; 4.6.1.1; 2681.
DR PathwayCommons; Q08462; -.
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; Q08462; -.
DR SIGNOR; Q08462; -.
DR BioGRID-ORCS; 108; 3 hits in 1065 CRISPR screens.
DR ChiTaRS; ADCY2; human.
DR GeneWiki; ADCY2; -.
DR GenomeRNAi; 108; -.
DR Pharos; Q08462; Tbio.
DR PRO; PR:Q08462; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q08462; protein.
DR Bgee; ENSG00000078295; Expressed in middle temporal gyrus and 177 other tissues.
DR ExpressionAtlas; Q08462; baseline and differential.
DR Genevisible; Q08462; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004016; F:adenylate cyclase activity; ISS:BHF-UCL.
DR GO; GO:0008179; F:adenylate cyclase binding; ISS:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0006171; P:cAMP biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:1904322; P:cellular response to forskolin; 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; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; cAMP biosynthesis; Cell membrane;
KW Cytoplasm; Glycoprotein; Lyase; Magnesium; Manganese; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1091
FT /note="Adenylate cyclase type 2"
FT /id="PRO_0000195684"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..601
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..652
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 680..701
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 763..780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 822..1091
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 905..922
FT /note="Interaction with GNAS"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT REGION 990..993
FT /note="Interaction with GNAS"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 295..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 295
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 295
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 296
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 337..339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 339
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 339
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 383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 939
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1019..1021
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1026..1030
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1066
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT MOD_RES 491
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT MOD_RES 544
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..59
FT /note="MWQEAMRRRRYLRDRSEEAAGGGDGLPRSRDWLYESYYCMSQQHPLIVFLLL
FT IVMGSCL -> MDLRWARDLHLREASRSVAFTTLRLGAVTTGLLTFREPGDKEKSGKGL
FT GKRWRIQREES (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055811"
FT VAR_SEQ 60..239
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055812"
FT VARIANT 147
FT /note="V -> L (in dbSNP:rs13166360)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029012"
FT VARIANT 163
FT /note="V -> I (in dbSNP:rs34043481)"
FT /id="VAR_048247"
FT CONFLICT 188..207
FT /note="VWQILANVIIFICGNLAGAY -> GLADPGQCDHFHLWEPGXTN (in
FT Ref. 1; AAP97285)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="R -> Q (in Ref. 6; CAA52282/AAA64923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1091 AA; 123603 MW; 41FD8BC607C075D1 CRC64;
MWQEAMRRRR YLRDRSEEAA GGGDGLPRSR DWLYESYYCM SQQHPLIVFL LLIVMGSCLA
LLAVFFALGL EVEDHVAFLI TVPTALAIFF AIFILVCIES VFKKLLRLFS LVIWICLVAM
GYLFMCFGGT VSPWDQVSFF LFIIFVVYTM LPFNMRDAII ASVLTSSSHT IVLSVCLSAT
PGGKEHLVWQ ILANVIIFIC GNLAGAYHKH LMELALQQTY QDTCNCIKSR IKLEFEKRQQ
ERLLLSLLPA HIAMEMKAEI IQRLQGPKAG QMENTNNFHN LYVKRHTNVS ILYADIVGFT
RLASDCSPGE LVHMLNELFG KFDQIAKENE CMRIKILGDC YYCVSGLPIS LPNHAKNCVK
MGLDMCEAIK KVRDATGVDI NMRVGVHSGN VLCGVIGLQK WQYDVWSHDV TLANHMEAGG
VPGRVHISSV TLEHLNGAYK VEEGDGDIRD PYLKQHLVKT YFVINPKGER RSPQHLFRPR
HTLDGAKMRA SVRMTRYLES WGAAKPFAHL HHRDSMTTEN GKISTTDVPM GQHNFQNRTL
RTKSQKKRFE EELNERMIQA IDGINAQKQW LKSEDIQRIS LLFYNKVLEK EYRATALPAF
KYYVTCACLI FFCIFIVQIL VLPKTSVLGI SFGAAFLLLA FILFVCFAGQ LLQCSKKASP
LLMWLLKSSG IIANRPWPRI SLTIITTAII LMMAVFNMFF LSDSEETIPP TANTTNTSFS
ASNNQVAILR AQNLFFLPYF IYSCILGLIS CSVFLRVNYE LKMLIMMVAL VGYNTILLHT
HAHVLGDYSQ VLFERPGIWK DLKTMGSVSL SIFFITLLVL GRQNEYYCRL DFLWKNKFKK
EREEIETMEN LNRVLLENVL PAHVAEHFLA RSLKNEELYH QSYDCVCVMF ASIPDFKEFY
TESDVNKEGL ECLRLLNEII ADFDDLLSKP KFSGVEKIKT IGSTYMAATG LSAVPSQEHS
QEPERQYMHI GTMVEFAFAL VGKLDAINKH SFNDFKLRVG INHGPVIAGV IGAQKPQYDI
WGNTVNVASR MDSTGVLDKI QVTEETSLVL QTLGYTCTCR GIINVKGKGD LKTYFVNTEM
SRSLSQSNVA S
