ADCY5_CANLF
ID ADCY5_CANLF Reviewed; 1265 AA.
AC P30803;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Adenylate cyclase type 5;
DE EC=4.6.1.1 {ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:1618857, ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:8428899};
DE AltName: Full=ATP pyrophosphate-lyase 5;
DE AltName: Full=Adenylate cyclase type V;
DE AltName: Full=Adenylyl cyclase 5;
DE AltName: Full=Ca(2+)-inhibitable adenylyl cyclase;
GN Name=ADCY5;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RC TISSUE=Heart muscle;
RX PubMed=1618857; DOI=10.1016/s0021-9258(18)42247-8;
RA Ishikawa Y., Katsushika S., Chen L., Halnon N.J., Kawabe J., Homcy C.J.;
RT "Isolation and characterization of a novel cardiac adenylylcyclase cDNA.";
RL J. Biol. Chem. 267:13553-13557(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, ACTIVITY REGULATION, DOMAIN, AND TISSUE SPECIFICITY.
RC TISSUE=Heart muscle;
RX PubMed=8428899; DOI=10.1016/s0021-9258(18)53766-2;
RA Katsushika S., Kawabe J., Homcy C.J., Ishikawa Y.;
RT "In vivo generation of an adenylylcyclase isoform with a half-molecule
RT motif.";
RL J. Biol. Chem. 268:2273-2276(1993).
RN [3]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Tomlinson J., Okumura S., Ishikawa Y.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 445-661 OF CHIMERA WITH ADCY5 IN
RP COMPLEX WITH GNAS, INTERACTION WITH GNAS, AND DOMAIN.
RX PubMed=9417641; DOI=10.1126/science.278.5345.1907;
RA Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.;
RT "Crystal structure of the catalytic domains of adenylyl cyclase in a
RT complex with Gsalpha.GTPgammaS.";
RL Science 278:1907-1916(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 445-661 OF CHIMERA WITH ADCY5 IN
RP COMPLEX WITH ATP ANALOGS; MAGNESIUM; MANGANESE AND GNAS, INTERACTION WITH
RP GNAS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, MUTAGENESIS OF ASP-477 AND
RP ASP-521, AND DOMAIN.
RX PubMed=10427002; DOI=10.1126/science.285.5428.756;
RA Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G.,
RA Sprang S.R.;
RT "Two-metal-ion catalysis in adenylyl cyclase.";
RL Science 285:756-760(1999).
RN [6] {ECO:0007744|PDB:1CS4, ECO:0007744|PDB:1CUL}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 445-661 OF CHIMERA WITH ADCY5 IN
RP COMPLEX WITH GNAS; ATP ANALOG AND MAGNESIUM, CATALYTIC ACTIVITY, FUNCTION,
RP COFACTOR, SUBCELLULAR LOCATION, INTERACTION WITH GNAS, AND DOMAIN.
RX PubMed=11087399; DOI=10.1021/bi0015562;
RA Tesmer J.J., Dessauer C.W., Sunahara R.K., Murray L.D., Johnson R.A.,
RA Gilman A.G., Sprang S.R.;
RT "Molecular basis for P-site inhibition of adenylyl cyclase.";
RL Biochemistry 39:14464-14471(2000).
RN [7] {ECO:0007744|PDB:1TL7, ECO:0007744|PDB:1U0H}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 445-661 OF CHIMERA WITH ADCY5 IN
RP COMPLEX WITH GNAS; MAGNESIUM AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY,
RP INTERACTION WITH GNAS, AND DOMAIN.
RX PubMed=15591060; DOI=10.1074/jbc.m409076200;
RA Mou T.C., Gille A., Fancy D.A., Seifert R., Sprang S.R.;
RT "Structural basis for the inhibition of mammalian membrane adenylyl cyclase
RT by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate.";
RL J. Biol. Chem. 280:7253-7261(2005).
RN [8] {ECO:0007744|PDB:2GVD, ECO:0007744|PDB:2GVZ}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 444-661 OF CHIMERA WITH ADCY5 IN
RP COMPLEX WITH GNAS; MANGANESE AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, INTERACTION WITH GNAS, AND DOMAIN.
RX PubMed=16766715; DOI=10.1124/mol.106.026427;
RA Mou T.C., Gille A., Suryanarayana S., Richter M., Seifert R., Sprang S.R.;
RT "Broad specificity of mammalian adenylyl cyclase for interaction with
RT 2',3'-substituted purine- and pyrimidine nucleotide inhibitors.";
RL Mol. Pharmacol. 70:878-886(2006).
RN [9] {ECO:0007744|PDB:3C14, ECO:0007744|PDB:3C15, ECO:0007744|PDB:3C16, ECO:0007744|PDB:3MAA}
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 444-661 OF CHIMERA WITH ADCY5 IN
RP COMPLEX WITH GNAS; ATP AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, INTERACTION WITH GNAS, AND DOMAIN.
RX PubMed=19243146; DOI=10.1021/bi802122k;
RA Mou T.C., Masada N., Cooper D.M., Sprang S.R.;
RT "Structural basis for inhibition of mammalian adenylyl cyclase by
RT calcium.";
RL Biochemistry 48:3387-3397(2009).
CC -!- FUNCTION: [Isoform 1]: Catalyzes the formation of the signaling
CC molecule cAMP in response to G-protein signaling (PubMed:1618857,
CC PubMed:8428899, PubMed:10427002, PubMed:11087399, PubMed:15591060,
CC PubMed:16766715, PubMed:19243146). Mediates signaling downstream of
CC ADRB1. Regulates the increase of free cytosolic Ca(2+) in response to
CC increased blood glucose levels and contributes to the regulation of
CC Ca(2+)-dependent insulin secretion (By similarity).
CC {ECO:0000250|UniProtKB:O95622, ECO:0000269|PubMed:10427002,
CC ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060,
CC ECO:0000269|PubMed:1618857, ECO:0000269|PubMed:16766715,
CC ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:8428899}.
CC -!- FUNCTION: [Isoform 2]: Lacks catalytic activity by itself, but can
CC associate with isoform 1 to form active adenylyl cyclase.
CC {ECO:0000269|PubMed:8428899}.
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:10427002, ECO:0000269|PubMed:11087399,
CC ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:1618857,
CC ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:19243146,
CC ECO:0000269|PubMed:8428899};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:16766715,
CC ECO:0000269|PubMed:19243146};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:16766715};
CC Note=Binds 2 magnesium ions per subunit (PubMed:16766715,
CC PubMed:19243146). Is also active with manganese (in vitro)
CC (PubMed:11087399, PubMed:16766715). {ECO:0000269|PubMed:10427002,
CC ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:16766715,
CC ECO:0000305|PubMed:19243146};
CC -!- ACTIVITY REGULATION: Activated by forskolin (PubMed:1618857,
CC PubMed:8428899). Activated by GNAS. Activity is further increased by
CC interaction with the G-protein beta and gamma subunit complex formed by
CC GNB1 and GNG2 (By similarity). Is not activated by calmodulin.
CC Inhibited by adenosine and ATP analogs. Inhibited by calcium ions,
CC already at micromolar concentrations (PubMed:1618857). Phosphorylation
CC by RAF1 results in its activation (By similarity).
CC {ECO:0000250|UniProtKB:O95622, ECO:0000269|PubMed:1618857,
CC ECO:0000269|PubMed:8428899}.
CC -!- SUBUNIT: Interacts with GNAS (PubMed:9417641, PubMed:10427002,
CC PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146).
CC Interacts with GNB1 and GNG2 (By similarity). Part of a complex
CC containing AKAP5, ADCY6, PDE4C and PKD2 (By similarity). Interacts with
CC RAF1 (By similarity). {ECO:0000250|UniProtKB:O95622,
CC ECO:0000250|UniProtKB:P84309, ECO:0000269|PubMed:10427002,
CC ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060,
CC ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:19243146,
CC ECO:0000269|PubMed:9417641}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1618857,
CC ECO:0000269|PubMed:8428899}; Multi-pass membrane protein {ECO:0000305}.
CC Cell projection, cilium {ECO:0000250|UniProtKB:P84309}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=V;
CC IsoId=P30803-1; Sequence=Displayed;
CC Name=2; Synonyms=V-alpha;
CC IsoId=P30803-2; Sequence=VSP_000242, VSP_000243;
CC -!- TISSUE SPECIFICITY: Isoform 1 is detected in heart, and at lower levels
CC in brain (PubMed:1618857). Isoform 2 is detected in heart
CC (PubMed:8428899). {ECO:0000269|PubMed:1618857,
CC ECO:0000269|PubMed:8428899}.
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:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399,
CC ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:16766715,
CC ECO:0000269|PubMed:19243146}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; M88649; AAC32726.1; -; mRNA.
DR EMBL; M97886; AAA30827.1; ALT_SEQ; mRNA.
DR PIR; A42904; A42904.
DR PIR; A45195; A45195.
DR RefSeq; NP_001161932.1; NM_001168460.1. [P30803-1]
DR PDB; 1AZS; X-ray; 2.30 A; A=442-656.
DR PDB; 1CJK; X-ray; 3.00 A; A=445-661.
DR PDB; 1CJT; X-ray; 2.80 A; A=445-661.
DR PDB; 1CJU; X-ray; 2.80 A; A=445-661.
DR PDB; 1CJV; X-ray; 3.00 A; A=445-661.
DR PDB; 1CS4; X-ray; 2.50 A; A=442-661.
DR PDB; 1CUL; X-ray; 2.40 A; A=445-661.
DR PDB; 1TL7; X-ray; 2.80 A; A=445-661.
DR PDB; 1U0H; X-ray; 2.90 A; A=442-661.
DR PDB; 2GVD; X-ray; 2.90 A; A=444-661.
DR PDB; 2GVZ; X-ray; 3.27 A; A=444-661.
DR PDB; 3C14; X-ray; 2.68 A; A=444-661.
DR PDB; 3C15; X-ray; 2.78 A; A=444-661.
DR PDB; 3C16; X-ray; 2.87 A; A=444-661.
DR PDB; 3G82; X-ray; 3.11 A; A=444-661.
DR PDB; 3MAA; X-ray; 3.00 A; A=444-661.
DR PDBsum; 1AZS; -.
DR PDBsum; 1CJK; -.
DR PDBsum; 1CJT; -.
DR PDBsum; 1CJU; -.
DR PDBsum; 1CJV; -.
DR PDBsum; 1CS4; -.
DR PDBsum; 1CUL; -.
DR PDBsum; 1TL7; -.
DR PDBsum; 1U0H; -.
DR PDBsum; 2GVD; -.
DR PDBsum; 2GVZ; -.
DR PDBsum; 3C14; -.
DR PDBsum; 3C15; -.
DR PDBsum; 3C16; -.
DR PDBsum; 3G82; -.
DR PDBsum; 3MAA; -.
DR AlphaFoldDB; P30803; -.
DR SMR; P30803; -.
DR DIP; DIP-179N; -.
DR IntAct; P30803; 1.
DR STRING; 9612.ENSCAFP00000017783; -.
DR PaxDb; P30803; -.
DR GeneID; 403859; -.
DR KEGG; cfa:403859; -.
DR CTD; 111; -.
DR eggNOG; KOG3619; Eukaryota.
DR InParanoid; P30803; -.
DR OrthoDB; 215180at2759; -.
DR EvolutionaryTrace; P30803; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004016; F:adenylate cyclase activity; ISS: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; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR CDD; cd07302; CHD; 1.
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; 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 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 3D-structure; Alternative splicing; ATP-binding; cAMP biosynthesis;
KW Cell membrane; Cell projection; Cilium; Glycoprotein; Lyase; Magnesium;
KW Membrane; Metal-binding; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1265
FT /note="Adenylate cyclase type 5"
FT /id="PRO_0000195693"
FT TOPO_DOM 1..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..765
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000305"
FT TRANSMEM 766..786
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 792..812
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 839..859
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 908..928
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 930..950
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 988..1008
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1009..1265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000305"
FT DOMAIN 472..599
FT /note="Guanylate cyclase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DOMAIN 1075..1214
FT /note="Guanylate cyclase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 477..482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:10427002,
FT ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:16766715,
FT ECO:0000305|PubMed:19243146"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10427002,
FT ECO:0007744|PDB:1CJU, ECO:0007744|PDB:1CJV,
FT ECO:0007744|PDB:1CS4, ECO:0007744|PDB:1CUL,
FT ECO:0007744|PDB:1U0H, ECO:0007744|PDB:3C15"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:10427002"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:10427002"
FT BINDING 519..521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:10427002,
FT ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:16766715,
FT ECO:0000305|PubMed:19243146"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10427002,
FT ECO:0007744|PDB:1CJU, ECO:0007744|PDB:1CJV,
FT ECO:0007744|PDB:1CS4, ECO:0007744|PDB:1CUL,
FT ECO:0007744|PDB:1U0H, ECO:0007744|PDB:3C15"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:10427002"
FT BINDING 565
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:10427002,
FT ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:16766715,
FT ECO:0000305|PubMed:19243146"
FT BINDING 1127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1201..1203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1208..1212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT MOD_RES 16
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P84309"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84309"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84309"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43306"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03343"
FT MOD_RES 1015
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q03343"
FT CARBOHYD 873
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 890
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 976
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 653..677
FT /note="KEEKAMIAKMNRQRTNSIGHNPPHW -> VRRGGGGPRPGGADSPGWWGASA
FT GP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8428899"
FT /id="VSP_000242"
FT VAR_SEQ 678..1265
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8428899"
FT /id="VSP_000243"
FT MUTAGEN 477
FT /note="D->A,N: Almost abolishes enzyme activity. Abolishes
FT enzyme activity; when associated with A-521 or N-521."
FT /evidence="ECO:0000269|PubMed:10427002"
FT MUTAGEN 521
FT /note="D->A,N: Almost abolishes enzyme activity. Abolishes
FT enzyme activity; when associated with A-396 or N-396."
FT /evidence="ECO:0000269|PubMed:10427002"
FT STRAND 464..479
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 481..487
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 490..511
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 522..527
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 536..558
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 563..577
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 579..582
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 586..589
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 590..600
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:2GVZ"
FT STRAND 606..609
FT /evidence="ECO:0007829|PDB:1AZS"
FT TURN 612..619
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:1AZS"
FT HELIX 633..637
FT /evidence="ECO:0007829|PDB:1AZS"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:1AZS"
SQ SEQUENCE 1265 AA; 140319 MW; 414322F64153DFB4 CRC64;
MSGPRSASPP GCAATRGGPE HRAAWGEAEA RANGHPHAAG GATRGCSKKP GGAVTPQLQQ
QQQQQQHEQQ HEQQQHEQQQ HVQQQQRLAK RWRGDDDPPL GGDDPLAGGF GFSFRSRSAW
QERGGDDCGR GSRRRRRGAA GGGSSRAPPA GGGGGPAAAG GAEVRPRSVE LGLDERRGRG
RAEPEPEAEA GAPGGDRGAR DGDGPAGPGA CCRALLQIFR SKKFPSDKLE RLYQRYFFRL
NQSSLTMLMA VLVLVCLVML AFHAARPPLR LPHLAVLAAA VGVILVMAVL CNRAAFHQDH
MGLACYALIA VVLAVQVVGL LLPQPRSASE GIWWTVFFIY TIYTLLPVRM RAAVLSGVLL
SALHLAIALR ANAQDRFLLK QLVSNVLIFS CTNIVGVCTH YPAEVSQRQA FQETRECIQA
RLHSQRENQQ QERLLLSVLP RHVAMEMKAD INAKQEDMMF HKIYIQKHDN VSILFADIEG
FTSLASQCTA QELVMTLNEL FARFDKLAAE NHCLRIKILG DCYYCVSGLP EARADHAHCC
VEMGMDMIEA ISLVREVTGV NVNMRVGIHS GRVHCGVLGL RKWQFDVWSN DVTLANHMEA
GGKAGRIHIT KATLSYLNGD YEVEPGCGGE RNAYLKEHSI ETFLILRCTQ KRKEEKAMIA
KMNRQRTNSI GHNPPHWGAE RPFYNHLGGN QVSKEMKRMG FEDPKDKNAQ ESANPEDEVD
EFLGRAIDAR SIDRLRSEHV RKFLLTFREP DLEKKYSKQV DDRFGAYVAC ASLVFLFICF
VQITIVPHSV FMLSFYLTCF LLLTLVVFVS VIYSCVKLFP GPLQSLSRKI VRSKTNSTLV
GVFTITLVFL SAFVNMFMCN SEDLLGCLAD EHNISTSRVN ACHVAASAAN LSLGDEQGFC
GTPWPSCNFP EYFTYSVLLS LLACSVFLQI SCIGKLVLML AIELIYVLVV EVPRVTLFDN
ADLLVTANAI DFNNNNGTSQ CPEHATKVAL KVVTPIIISV FVLALYLHAQ QVESTARLDF
LWKLQATEEK EEMEELQAYN RRLLHNILPK DVAAHFLARE RRNDELYYQS CECVAVMFAS
IANFSEFYVE LEANNEGVEC LRVLNEIIAD FDEIISEDRF RQLEKIKTIG STYMAASGLN
DSTYDKVGKT HIKALADFAM KLMDQMKYIN EHSFNNFQMK IGLNIGPVVA GVIGARKPQY
DIWGNTVNVA SRMDSTGVPD RIQVTTDMYQ VLAANTYQLE CRGVVKVKGK GEMMTYFLNG
GPPLS
