ID   ADCY4_HUMAN             Reviewed;        1077 AA.
AC   Q8NFM4; B3KV74; D3DS75; Q17R40; Q6ZTM6; Q96ML7;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 181.
DE   RecName: Full=Adenylate cyclase type 4;
DE            EC=4.6.1.1 {ECO:0000250|UniProtKB:P26770};
DE   AltName: Full=ATP pyrophosphate-lyase 4;
DE   AltName: Full=Adenylate cyclase type IV;
DE   AltName: Full=Adenylyl cyclase 4;
GN   Name=ADCY4;
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 1).
RC   TISSUE=Spleen;
RX   PubMed=12503609; DOI=10.1081/rrs-120014589;
RA   Ludwig M.G., Seuwen K.;
RT   "Characterization of the human adenylyl cyclase gene family: cDNA, gene
RT   structure, and tissue distribution of the nine isoforms.";
RL   J. Recept. Signal Transduct. 22:79-110(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Placenta, Tongue, and Uterus;
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=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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   [7]
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. {ECO:0000250|UniProtKB:P26770}.
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:0000250|UniProtKB:P26770};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P26770};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P26770};
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 forskolin. Insensitive to
CC       calcium/calmodulin. Stimulated by GNAS and by the G-protein beta and
CC       gamma subunit complex. {ECO:0000250|UniProtKB:P26770}.
CC   -!- INTERACTION:
CC       Q8NFM4; Q9BV19: C1orf50; NbExp=3; IntAct=EBI-2838710, EBI-2874661;
CC       Q8NFM4; P62508-3: ESRRG; NbExp=6; IntAct=EBI-2838710, EBI-12001340;
CC       Q8NFM4; P37231: PPARG; NbExp=3; IntAct=EBI-2838710, EBI-781384;
CC       Q8NFM4; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-2838710, EBI-2130429;
CC       Q8NFM4; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-2838710, EBI-9090990;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21228062};
CC       Multi-pass 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=Q8NFM4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8NFM4-2; Sequence=VSP_055816, VSP_055817, VSP_055818,
CC                                  VSP_055819;
CC   -!- TISSUE SPECIFICITY: Detected in the zona glomerulosa and the zona
CC       fasciculata in the adrenal gland (at protein level).
CC       {ECO:0000269|PubMed:11549699}.
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 modules have no catalytic activity, but when they are
CC       brought together, enzyme activity is restored. The active site is at
CC       the interface of the two modules. {ECO:0000250|UniProtKB:P30803}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB71270.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF497516; AAM94373.1; -; mRNA.
DR   EMBL; AK056745; BAB71270.1; ALT_INIT; mRNA.
DR   EMBL; AK122714; BAG53686.1; -; mRNA.
DR   EMBL; AK126468; BAC86560.1; -; mRNA.
DR   EMBL; AL096870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471078; EAW66023.1; -; Genomic_DNA.
DR   EMBL; CH471078; EAW66026.1; -; Genomic_DNA.
DR   EMBL; CH471078; EAW66027.1; -; Genomic_DNA.
DR   EMBL; CH471078; EAW66028.1; -; Genomic_DNA.
DR   EMBL; BC117473; AAI17474.1; -; mRNA.
DR   EMBL; BC117475; AAI17476.1; -; mRNA.
DR   CCDS; CCDS9627.1; -. [Q8NFM4-1]
DR   RefSeq; NP_001185497.1; NM_001198568.1. [Q8NFM4-1]
DR   RefSeq; NP_001185521.1; NM_001198592.1. [Q8NFM4-1]
DR   RefSeq; NP_640340.2; NM_139247.3. [Q8NFM4-1]
DR   AlphaFoldDB; Q8NFM4; -.
DR   SMR; Q8NFM4; -.
DR   BioGRID; 128229; 6.
DR   IntAct; Q8NFM4; 9.
DR   STRING; 9606.ENSP00000312126; -.
DR   BindingDB; Q8NFM4; -.
DR   ChEMBL; CHEMBL2097167; -.
DR   DrugBank; DB02587; Colforsin.
DR   GlyCosmos; Q8NFM4; 2 sites, No reported glycans.
DR   GlyGen; Q8NFM4; 2 sites.
DR   iPTMnet; Q8NFM4; -.
DR   PhosphoSitePlus; Q8NFM4; -.
DR   BioMuta; ADCY4; -.
DR   DMDM; 25008336; -.
DR   EPD; Q8NFM4; -.
DR   jPOST; Q8NFM4; -.
DR   MassIVE; Q8NFM4; -.
DR   MaxQB; Q8NFM4; -.
DR   PaxDb; 9606-ENSP00000312126; -.
DR   PeptideAtlas; Q8NFM4; -.
DR   ProteomicsDB; 73323; -. [Q8NFM4-1]
DR   Antibodypedia; 3908; 256 antibodies from 26 providers.
DR   DNASU; 196883; -.
DR   Ensembl; ENST00000310677.8; ENSP00000312126.4; ENSG00000129467.14. [Q8NFM4-1]
DR   Ensembl; ENST00000418030.7; ENSP00000393177.2; ENSG00000129467.14. [Q8NFM4-1]
DR   Ensembl; ENST00000554068.6; ENSP00000452250.2; ENSG00000129467.14. [Q8NFM4-1]
DR   Ensembl; ENST00000642645.1; ENSP00000495316.1; ENSG00000284814.1. [Q8NFM4-1]
DR   Ensembl; ENST00000644961.1; ENSP00000494454.1; ENSG00000284814.1. [Q8NFM4-1]
DR   Ensembl; ENST00000646612.1; ENSP00000494977.1; ENSG00000284814.1. [Q8NFM4-1]
DR   GeneID; 196883; -.
DR   KEGG; hsa:196883; -.
DR   MANE-Select; ENST00000418030.7; ENSP00000393177.2; NM_001198568.2; NP_001185497.1.
DR   UCSC; uc001wow.4; human. [Q8NFM4-1]
DR   AGR; HGNC:235; -.
DR   CTD; 196883; -.
DR   DisGeNET; 196883; -.
DR   GeneCards; ADCY4; -.
DR   HGNC; HGNC:235; ADCY4.
DR   HPA; ENSG00000129467; Low tissue specificity.
DR   MIM; 600292; gene.
DR   neXtProt; NX_Q8NFM4; -.
DR   OpenTargets; ENSG00000129467; -.
DR   PharmGKB; PA24562; -.
DR   VEuPathDB; HostDB:ENSG00000129467; -.
DR   eggNOG; KOG3619; Eukaryota.
DR   GeneTree; ENSGT00940000159445; -.
DR   HOGENOM; CLU_001072_2_5_1; -.
DR   InParanoid; Q8NFM4; -.
DR   OMA; NCPFRAP; -.
DR   OrthoDB; 3686360at2759; -.
DR   PhylomeDB; Q8NFM4; -.
DR   TreeFam; TF313845; -.
DR   PathwayCommons; Q8NFM4; -.
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; Q8NFM4; -.
DR   SIGNOR; Q8NFM4; -.
DR   BioGRID-ORCS; 196883; 14 hits in 1141 CRISPR screens.
DR   ChiTaRS; ADCY4; human.
DR   GeneWiki; ADCY4; -.
DR   GenomeRNAi; 196883; -.
DR   Pharos; Q8NFM4; Tbio.
DR   PRO; PR:Q8NFM4; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q8NFM4; Protein.
DR   Bgee; ENSG00000129467; Expressed in apex of heart and 93 other cell types or tissues.
DR   ExpressionAtlas; Q8NFM4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; ISS:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0004016; F:adenylate cyclase activity; ISS:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005080; F:protein kinase C binding; IDA:UniProtKB.
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:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006171; P:cAMP biosynthetic process; ISS:BHF-UCL.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
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:SF10; ADENYLATE CYCLASE TYPE 4; 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; 2.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
DR   Genevisible; Q8NFM4; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; cAMP biosynthesis; Cell membrane;
KW   Cytoplasm; Glycoprotein; Lyase; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..1077
FT                   /note="Adenylate cyclase type 4"
FT                   /id="PRO_0000195690"
FT   TOPO_DOM        1..28
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        29..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..585
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        586..607
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        611..633
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        664..687
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        688..714
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        715..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        744..764
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        791..807
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        808..1077
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         278..283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P30803"
FT   BINDING         278
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         278
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         279
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         320..322
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P30803"
FT   BINDING         322
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         322
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         366
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P30803"
FT   BINDING         925
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P26769"
FT   BINDING         1005..1007
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P26769"
FT   BINDING         1012..1016
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P26769"
FT   BINDING         1052
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P26769"
FT   MOD_RES         520
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26770"
FT   MOD_RES         536
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P26770"
FT   CARBOHYD        697
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        704
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..45
FT                   /note="MARLFSPRPPPSEDLFYETYYSLSQQYPLLLLLLGIVLCALAALL -> MSR
FT                   GTRESACCMLTSWASRGWPASVPLRSWCSCSMSSLASSTRLP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055816"
FT   VAR_SEQ         46..352
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055817"
FT   VAR_SEQ         720..726
FT                   /note="YSMHCCT -> VSVPTCP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055818"
FT   VAR_SEQ         727..1077
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055819"
FT   CONFLICT        571
FT                   /note="E -> G (in Ref. 2; BAB71270)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1077 AA;  119794 MW;  24C0D5AE495CFD50 CRC64;
     MARLFSPRPP PSEDLFYETY YSLSQQYPLL LLLLGIVLCA LAALLAVAWA SGRELTSDPS
     FLTTVLCALG GFSLLLGLAS REQRLQRWTR PLSGLVWVAL LALGHAFLFT GGVVSAWDQV
     SYFLFVIFTA YAMLPLGMRD AAVAGLASSL SHLLVLGLYL GPQPDSRPAL LPQLAANAVL
     FLCGNVAGVY HKALMERALR ATFREALSSL HSRRRLDTEK KHQEHLLLSI LPAYLAREMK
     AEIMARLQAG QGSRPESTNN FHSLYVKRHQ GVSVLYADIV GFTRLASECS PKELVLMLNE
     LFGKFDQIAK EHECMRIKIL GDCYYCVSGL PLSLPDHAIN CVRMGLDMCR AIRKLRAATG
     VDINMRVGVH SGSVLCGVIG LQKWQYDVWS HDVTLANHME AGGVPGRVHI TGATLALLAG
     AYAVEDAGME HRDPYLRELG EPTYLVIDPR AEEEDEKGTA GGLLSSLEGL KMRPSLLMTR
     YLESWGAAKP FAHLSHGDSP VSTSTPLPEK TLASFSTQWS LDRSRTPRGL DDELDTGDAK
     FFQVIEQLNS QKQWKQSKDF NPLTLYFREK EMEKEYRLSA IPAFKYYEAC TFLVFLSNFI
     IQMLVTNRPP ALAITYSITF LLFLLILFVC FSEDLMRCVL KGPKMLHWLP ALSGLVATRP
     GLRIALGTAT ILLVFAMAIT SLFFFPTSSD CPFQAPNVSS MISNLSWELP GSLPLISVPY
     SMHCCTLGFL SCSLFLHMSF ELKLLLLLLW LAASCSLFLH SHAWLSECLI VRLYLGPLDS
     RPGVLKEPKL MGAISFFIFF FTLLVLARQN EYYCRLDFLW KKKLRQEREE TETMENLTRL
     LLENVLPAHV APQFIGQNRR NEDLYHQSYE CVCVLFASVP DFKEFYSESN INHEGLECLR
     LLNEIIADFD ELLSKPKFSG VEKIKTIGST YMAATGLNAT SGQDAQQDAE RSCSHLGTMV
     EFAVALGSKL DVINKHSFNN FRLRVGLNHG PVVAGVIGAQ KPQYDIWGNT VNVASRMEST
     GVLGKIQVTE ETAWALQSLG YTCYSRGVIK VKGKGQLCTY FLNTDLTRTG PPSATLG
//