ADCY4_HUMAN
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 03-AUG-2022, entry version 173.
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 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; Q8NFM4; -.
DR PeptideAtlas; Q8NFM4; -.
DR PRIDE; Q8NFM4; -.
DR ProteomicsDB; 68278; -.
DR ProteomicsDB; 73323; -. [Q8NFM4-1]
DR Antibodypedia; 3908; 239 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 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; 363718at2759; -.
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 1063 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 91 other tissues.
DR ExpressionAtlas; Q8NFM4; baseline and differential.
DR Genevisible; Q8NFM4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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; -; 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; 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
