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Adenylate cyclase type 6 (EC 4.6.1.1) (ATP pyrophosphate-lyase 6) (Adenylate cyclase type VI) (Adenylyl cyclase 6) (AC6) (Ca(2 )-inhibitable adenylyl cyclase)

 ADCY6_MOUSE             Reviewed;        1165 AA.
Q01341;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
25-OCT-2017, entry version 157.
RecName: Full=Adenylate cyclase type 6;
EC=4.6.1.1 {ECO:0000269|PubMed:1379717, ECO:0000269|PubMed:18071070, ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:20864687, ECO:0000269|PubMed:23753526, ECO:0000269|PubMed:24363043};
AltName: Full=ATP pyrophosphate-lyase 6;
AltName: Full=Adenylate cyclase type VI;
AltName: Full=Adenylyl cyclase 6 {ECO:0000303|PubMed:18071070, ECO:0000303|PubMed:20466003};
Short=AC6 {ECO:0000303|PubMed:18071070, ECO:0000303|PubMed:20466003};
AltName: Full=Ca(2+)-inhibitable adenylyl cyclase;
Name=Adcy6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, ENZYME
REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=1379717; DOI=10.1073/pnas.89.15.6716;
Yoshimura M., Cooper D.M.F.;
"Cloning and expression of a Ca(2+)-inhibitable adenylyl cyclase from
NCB-20 cells.";
Proc. Natl. Acad. Sci. U.S.A. 89:6716-6720(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-1165.
PubMed=1332848; DOI=10.1210/endo.131.6.1332848;
Premont R.T., Jacobowitz O., Iyengar R.;
"Lowered responsiveness of the catalyst of adenylyl cyclase to
stimulation by GS in heterologous desensitization: a role for
adenosine 3',5'-monophosphate-dependent phosphorylation.";
Endocrinology 131:2774-2784(1992).
[3]
DISRUPTION PHENOTYPE, FUNCTION, ENZYME REGULATION, CATALYTIC ACTIVITY,
AND TISSUE SPECIFICITY.
PubMed=18071070; DOI=10.1161/CIRCULATIONAHA.107.730069;
Tang T., Gao M.H., Lai N.C., Firth A.L., Takahashi T., Guo T.,
Yuan J.X., Roth D.M., Hammond H.K.;
"Adenylyl cyclase type 6 deletion decreases left ventricular function
via impaired calcium handling.";
Circulation 117:61-69(2008).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=20371630; DOI=10.1096/fj.09-148007;
Kwon R.Y., Temiyasathit S., Tummala P., Quah C.C., Jacobs C.R.;
"Primary cilium-dependent mechanosensing is mediated by adenylyl
cyclase 6 and cyclic AMP in bone cells.";
FASEB J. 24:2859-2868(2010).
[6]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, CATALYTIC
ACTIVITY, ENZYME REGULATION, AND TISSUE SPECIFICITY.
PubMed=20466003; DOI=10.1016/j.febslet.2010.05.004;
Chien C.L., Wu Y.S., Lai H.L., Chen Y.H., Jiang S.T., Shih C.M.,
Lin S.S., Chang C., Chern Y.;
"Impaired water reabsorption in mice deficient in the type VI adenylyl
cyclase (AC6).";
FEBS Lett. 584:2883-2890(2010).
[7]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=20359598; DOI=10.1016/j.jacc.2009.11.066;
Tang T., Lai N.C., Hammond H.K., Roth D.M., Yang Y., Guo T., Gao M.H.;
"Adenylyl cyclase 6 deletion reduces left ventricular hypertrophy,
dilation, dysfunction, and fibrosis in pressure-overloaded female
mice.";
J. Am. Coll. Cardiol. 55:1476-1486(2010).
[8]
DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, AND ENZYME
REGULATION.
PubMed=20864687; DOI=10.1681/ASN.2010040409;
Rieg T., Tang T., Murray F., Schroth J., Insel P.A., Fenton R.A.,
Hammond H.K., Vallon V.;
"Adenylate cyclase 6 determines cAMP formation and aquaporin-2
phosphorylation and trafficking in inner medulla.";
J. Am. Soc. Nephrol. 21:2059-2068(2010).
[9]
SUBCELLULAR LOCATION, AND INTERACTION WITH AKAP5; ADCY5; PDE4C AND
PKD2.
PubMed=21670265; DOI=10.1073/pnas.1016214108;
Choi Y.H., Suzuki A., Hajarnis S., Ma Z., Chapin H.C., Caplan M.J.,
Pontoglio M., Somlo S., Igarashi P.;
"Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-
kinase anchoring protein complex that is disrupted in cystic kidney
diseases.";
Proc. Natl. Acad. Sci. U.S.A. 108:10679-10684(2011).
[10]
DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION,
AND TISSUE SPECIFICITY.
PubMed=23753526; DOI=10.1113/jphysiol.2012.249698;
Sabbatini M.E., D'Alecy L., Lentz S.I., Tang T., Williams J.A.;
"Adenylyl cyclase 6 mediates the action of cyclic AMP-dependent
secretagogues in mouse pancreatic exocrine cells via protein kinase A
pathway activation.";
J. Physiol. (Lond.) 591:3693-3707(2013).
[11]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=24277577; DOI=10.1096/fj.13-240432;
Lee K.L., Hoey D.A., Spasic M., Tang T., Hammond H.K., Jacobs C.R.;
"Adenylyl cyclase 6 mediates loading-induced bone adaptation in
vivo.";
FASEB J. 28:1157-1165(2014).
[12]
DISRUPTION PHENOTYPE.
PubMed=24158982; DOI=10.1681/ASN.2013010077;
Rees S., Kittikulsuth W., Roos K., Strait K.A., Van Hoek A.,
Kohan D.E.;
"Adenylyl cyclase 6 deficiency ameliorates polycystic kidney
disease.";
J. Am. Soc. Nephrol. 25:232-237(2014).
[13]
DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, AND ENZYME
REGULATION.
PubMed=24854272; DOI=10.1681/ASN.2013101102;
Fenton R.A., Murray F., Dominguez Rieg J.A., Tang T., Levi M.,
Rieg T.;
"Renal phosphate wasting in the absence of adenylyl cyclase 6.";
J. Am. Soc. Nephrol. 25:2822-2834(2014).
[14]
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=24363043; DOI=10.1007/s00210-013-0950-4;
Bogard A.S., Birg A.V., Ostrom R.S.;
"Non-raft adenylyl cyclase 2 defines a cAMP signaling compartment that
selectively regulates IL-6 expression in airway smooth muscle cells:
differential regulation of gene expression by AC isoforms.";
Naunyn Schmiedebergs Arch. Pharmacol. 387:329-339(2014).
-!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP
downstream of G protein-coupled receptors (PubMed:18071070,
PubMed:24363043). Functions in signaling cascades downstream of
beta-adrenergic receptors in the heart and in vascular smooth
muscle cells (PubMed:18071070). Functions in signaling cascades
downstream of the vasopressin receptor in the kidney and has a
role in renal water reabsorption (PubMed:20466003,
PubMed:20864687). Functions in signaling cascades downstream of
PTH1R and plays a role in regulating renal phosphate excretion
(PubMed:24854272). Functions in signaling cascades downstream of
the VIP and SCT receptors in pancreas and contributes to the
regulation of pancreatic amylase and fluid secretion
(PubMed:23753526). Signaling mediates cAMP-dependent activation of
protein kinase PKA and promotes increased phosphorylation of
various proteins, including AKT (PubMed:18071070,
PubMed:23753526). Plays a role in regulating cardiac sarcoplasmic
reticulum Ca(2+) uptake and storage, and is required for normal
heart ventricular contractibility (PubMed:18071070). May
contribute to normal heart function (PubMed:18071070,
PubMed:20359598). Mediates vasodilatation after activation of
beta-adrenergic receptors by isoproterenol (By similarity).
Contributes to bone cell responses to mechanical stimuli
(PubMed:20371630, PubMed:24277577). {ECO:0000250|UniProtKB:O43306,
ECO:0000269|PubMed:1379717, ECO:0000269|PubMed:18071070,
ECO:0000269|PubMed:20359598, ECO:0000269|PubMed:20371630,
ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:20864687,
ECO:0000269|PubMed:23753526, ECO:0000269|PubMed:24277577,
ECO:0000269|PubMed:24363043, ECO:0000269|PubMed:24854272}.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
{ECO:0000269|PubMed:1379717, ECO:0000269|PubMed:18071070,
ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:20864687,
ECO:0000269|PubMed:23753526, ECO:0000269|PubMed:24363043,
ECO:0000269|PubMed:24854272}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:O43306};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:O43306};
Note=Binds 2 magnesium ions per subunit. Is also active with
manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
-!- ENZYME REGULATION: Activated by forskolin (PubMed:18071070,
PubMed:20466003, PubMed:20864687, PubMed:23753526,
PubMed:24363043). Inhibited by calcium ions, already at micromolar
concentrations (PubMed:1379717, PubMed:18071070). Inhibited by
adenosine, AMP and their analogs (By similarity). Activated by
GNAS. Is further activated by the complex formed by GNB1 and GNG2
(By similarity). Phosphorylation by RAF1 results in its activation
(By similarity). {ECO:0000250|UniProtKB:P30804,
ECO:0000250|UniProtKB:Q03343, ECO:0000269|PubMed:1379717,
ECO:0000269|PubMed:18071070, ECO:0000269|PubMed:20466003,
ECO:0000269|PubMed:20864687, ECO:0000269|PubMed:23753526,
ECO:0000269|PubMed:24363043}.
-!- SUBUNIT: Part of a complex containing AKAP5, ADCY5, PDE4C and PKD2
(PubMed:21670265). Interacts with RAF1. Interacts (via cytoplasmic
N-terminus) with GNAS, GNB1 and GNG2 (By similarity).
{ECO:0000250|UniProtKB:O43306, ECO:0000269|PubMed:21670265}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1379717,
ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:21670265}; Multi-
pass membrane protein {ECO:0000269|PubMed:21670265}. Cell
projection, cilium {ECO:0000269|PubMed:20371630,
ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:21670265}.
-!- TISSUE SPECIFICITY: Detected in kidney tubules (PubMed:20466003).
Detected in primary bone cells with osteocyte morphology
(PubMed:24277577). Detected in heart (at protein level)
(PubMed:18071070). Highly expressed in heart (PubMed:1379717,
PubMed:18071070). Detected in kidney, pancreas acini and ducts
(PubMed:23753526). Weakly detectable in brain, intestine, lung and
spleen (PubMed:1379717). {ECO:0000269|PubMed:1379717,
ECO:0000269|PubMed:18071070, ECO:0000269|PubMed:20466003,
ECO:0000269|PubMed:23753526, ECO:0000269|PubMed:24277577}.
-!- DOMAIN: The protein contains two modules with six transmembrane
helices each; both are required for catalytic activity. Isolated
N-terminal or C-terminal guanylate cyclase domains have no
catalytic activity, but when they are brought together, enzyme
activity is restored. The active site is at the interface of the
two domains. Both contribute substrate-binding residues, but the
catalytic metal ions are bound exclusively via the N-terminal
guanylate cyclase domain. {ECO:0000250|UniProtKB:P26769}.
-!- PTM: Phosphorylation by RAF1 increases enzyme activity.
Phosphorylation by PKA on Ser-659 inhibits the GNAS-mediated
increase in catalytic activity. Phosphorylation by PKC on Ser-553,
Ser-659 and Thr-916 inhibits catalytic activity.
{ECO:0000250|UniProtKB:Q03343}.
-!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected
Mendelian rate, present no obvious phenotype and are fertile
(PubMed:18071070, PubMed:20466003, PubMed:23753526,
PubMed:24277577). Their hearts display a decrease in left
ventricular pressure, both at the basal level and after activation
of beta-adrenergic receptors (PubMed:18071070). Besides, their
hearts show defects in sarcoplasmic Ca(2+) uptake and storage, and
decreased levels of protein phosphorylation (PubMed:18071070).
Male mice show increased mortality after transversal aortic
constriction (PubMed:20359598). In contrast, female mice do not
show increased mortality after transversal aortic constriction,
and develop less heart hypertrophy and fibrosis than wild-type
(PubMed:20359598). Compared to wild-type, mutant mice drink more
and produce greater volumes of urine with decreased osmolarity,
but there is no difference in the total quantity of excreted
urinary solutes and no difference in blood plasma composition
(PubMed:20466003, PubMed:20864687). The impaired urinary water
homeostasis is due to retention of AQP2 in intracellular vesicles
and decreased AQP2 levels at the cell membrane (PubMed:20466003).
Mutant mice display increased urinary inorganic phosphate
excretion, but normal plasma phosphate levels (PubMed:24854272).
Mutant mice display increased plasma levels of PTH and FGF23, the
two principal regulators of urinary phosphate excretion
(PubMed:24854272). Mutant mice display no obvious skeleton
defects, but display less bone formation after load stress than
wild-type (PubMed:24277577). Mutant mice lacking both Adcy6 and
Pkd1 survive longer and have less severe polycystic kidney disease
than mice lacking only Pkd1 (PubMed:24158982).
{ECO:0000269|PubMed:18071070, ECO:0000269|PubMed:20359598,
ECO:0000269|PubMed:20466003, ECO:0000269|PubMed:20864687,
ECO:0000269|PubMed:23753526, ECO:0000269|PubMed:24158982,
ECO:0000269|PubMed:24277577, ECO:0000269|PubMed:24854272}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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EMBL; M93422; AAA37174.1; -; mRNA.
EMBL; M96653; AAA37182.1; -; mRNA.
PIR; A49201; A49201.
RefSeq; NP_031431.2; NM_007405.2.
UniGene; Mm.157091; -.
ProteinModelPortal; Q01341; -.
SMR; Q01341; -.
STRING; 10090.ENSMUSP00000093939; -.
iPTMnet; Q01341; -.
PhosphoSitePlus; Q01341; -.
SwissPalm; Q01341; -.
MaxQB; Q01341; -.
PaxDb; Q01341; -.
PRIDE; Q01341; -.
DNASU; 11512; -.
GeneID; 11512; -.
KEGG; mmu:11512; -.
CTD; 112; -.
MGI; MGI:87917; Adcy6.
eggNOG; KOG3619; Eukaryota.
eggNOG; COG2114; LUCA.
HOGENOM; HOG000006941; -.
HOVERGEN; HBG050458; -.
InParanoid; Q01341; -.
KO; K08046; -.
PhylomeDB; Q01341; -.
BRENDA; 4.6.1.1; 3474.
ChiTaRS; Adcy6; mouse.
PRO; PR:Q01341; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_ADCY6; -.
GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISS:BHF-UCL.
GO; GO:0004016; F:adenylate cyclase activity; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008294; F:calcium- and calmodulin-responsive adenylate cyclase activity; IDA:MGI.
GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; ISS:BHF-UCL.
GO; GO:0097110; F:scaffold protein binding; IPI:MGI.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:0006171; P:cAMP biosynthetic process; IMP:UniProtKB.
GO; GO:0071870; P:cellular response to catecholamine stimulus; ISO:MGI.
GO; GO:1904322; P:cellular response to forskolin; IMP:UniProtKB.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:MGI.
GO; GO:1904117; P:cellular response to vasopressin; IMP:UniProtKB.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0007212; P:dopamine receptor signaling pathway; ISO:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:ParkinsonsUK-UCL.
GO; GO:0035811; P:negative regulation of urine volume; IMP:UniProtKB.
GO; GO:0097746; P:regulation of blood vessel diameter; ISO:MGI.
GO; GO:0003091; P:renal water homeostasis; IMP:UniProtKB.
Gene3D; 3.30.70.1230; -; 2.
InterPro; IPR001054; A/G_cyclase.
InterPro; IPR018297; A/G_cyclase_CS.
InterPro; IPR032628; AC_N.
InterPro; IPR030672; Adcy.
InterPro; IPR009398; Adcy_conserved_dom.
InterPro; IPR029787; Nucleotide_cyclase.
Pfam; PF16214; AC_N; 1.
Pfam; PF06327; DUF1053; 1.
Pfam; PF00211; Guanylate_cyc; 2.
PIRSF; PIRSF039050; Ade_cyc; 1.
SMART; SM00044; CYCc; 2.
SUPFAM; SSF55073; SSF55073; 2.
PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
1: Evidence at protein level;
ATP-binding; cAMP biosynthesis; Cell membrane; Cell projection;
Cilium; Complete proteome; Glycoprotein; Lyase; Magnesium; Manganese;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix.
CHAIN 1 1165 Adenylate cyclase type 6.
/FTId=PRO_0000195700.
TOPO_DOM 1 149 Cytoplasmic. {ECO:0000255}.
TRANSMEM 150 166 Helical. {ECO:0000255}.
TRANSMEM 179 195 Helical. {ECO:0000255}.
TRANSMEM 212 228 Helical. {ECO:0000255}.
TRANSMEM 237 253 Helical. {ECO:0000255}.
TRANSMEM 257 273 Helical. {ECO:0000255}.
TRANSMEM 287 303 Helical. {ECO:0000255}.
TOPO_DOM 304 670 Cytoplasmic. {ECO:0000255}.
TRANSMEM 671 688 Helical. {ECO:0000255}.
TRANSMEM 699 715 Helical. {ECO:0000255}.
TRANSMEM 740 756 Helical. {ECO:0000255}.
TOPO_DOM 757 816 Extracellular. {ECO:0000255}.
TRANSMEM 817 833 Helical. {ECO:0000255}.
TRANSMEM 836 852 Helical. {ECO:0000255}.
TRANSMEM 894 910 Helical. {ECO:0000255}.
TOPO_DOM 911 1165 Cytoplasmic. {ECO:0000255}.
NP_BIND 382 387 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 424 426 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 1102 1104 ATP. {ECO:0000250|UniProtKB:P26769}.
NP_BIND 1109 1113 ATP. {ECO:0000250|UniProtKB:P26769}.
METAL 382 382 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 382 382 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 383 383 Magnesium 2; via carbonyl oxygen;
catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
METAL 426 426 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 426 426 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
BINDING 470 470 ATP. {ECO:0000250|UniProtKB:P30803}.
BINDING 1028 1028 ATP. {ECO:0000250|UniProtKB:P26769}.
BINDING 1149 1149 ATP. {ECO:0000250|UniProtKB:P26769}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000250|UniProtKB:O43306}.
MOD_RES 553 553 Phosphoserine.
{ECO:0000250|UniProtKB:Q03343}.
MOD_RES 573 573 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 659 659 Phosphoserine.
{ECO:0000250|UniProtKB:Q03343}.
MOD_RES 916 916 Phosphothreonine.
{ECO:0000250|UniProtKB:Q03343}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 790 790 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 875 875 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 47 47 K -> N (in Ref. 2; AAA37182).
{ECO:0000305}.
CONFLICT 76 76 G -> A (in Ref. 2; AAA37182).
{ECO:0000305}.
CONFLICT 508 509 GR -> RAG (in Ref. 2; AAA37182).
{ECO:0000305}.
CONFLICT 737 737 V -> G (in Ref. 2; AAA37182).
{ECO:0000305}.
CONFLICT 881 881 L -> Q (in Ref. 2; AAA37182).
{ECO:0000305}.
CONFLICT 990 990 V -> M (in Ref. 2; AAA37182).
{ECO:0000305}.
SEQUENCE 1165 AA; 130319 MW; 24EE1BB45DF1E87E CRC64;
MSWFSGLLVP KVDERKTAWG ERNGQKRPRH ANRASGFCAP RYMSCLKNAE PPSPTPAAHT
RCPWQDEAFI RRAGPGRGVE LGLRSVALGF DDTEVTTPMG TAEVAPDTSP RSGPSCWHRL
VQVFQSKQFR SAKLERLYQR YFFQMNQSSL TLLMAVLVLL MAVLLTFHAA PAQPQPAYVA
LLTCASVLFV VLMVVCNRHS FRQDSMWVVS YVVLGILAAV QVGGALAANP HSPSAGLWCP
VFFVYITYTL LPIRMRAAVL SGLGLSTLHL ILAWQLNSSD PFLWKQLGAN VVLFLCTNAI
GVCTHYPAEV SQRQAFQETR GYIQARLHLQ HENRQQERLL LSVLPQHVAM EMKEDINTKK
EDMMFHKIYI QKHDNVSILF ADIEGFTSLA SQCTAQELVM TLNELFARFD KLAAENHCLR
IKILGDCYYC VSGLPEARAD HAHCCVEMGV DMIEAISLVR EVTGVNVNMR VGIHSGRVHC
GVLGLRKWQF DVWSNDVTLA NHMEAGGGRR IHITRATLQY LNGDYEVEPG RGGERNAYLK
EQCIETFLIL GASQKRKEEK AMLAKLQRTR ANSMEGLMPR WVPDRAFSRT KDSKAFRQMG
IDDSSKDNRG AQDALNPEDE VDEFLGRAID ARSIDQLRKD HVRRFLLTFQ REDLEKKYSR
KVDPRFGAYV ACALLVFCFI CFIQLLVFPY STLILGIYAA IFLLLLVTVL ICAVCSCGSF
FPKALQRLSR NIVRSRVHST AVGIFSVLLV FISAIANMFT CNHTPIRTCA ARMLNLTPAD
VTACHLQQLN YSLGLDAPLC EGTAPTCSFP EYFVGNVLLS LLASSVFLHI SSIGKLAMTF
ILGFTYLVLL LLGPPAAIFD NYDLLLGVHG LASSNETFDG LDCPAVGRVA LKYMTPVILL
VFALALYLHA QQVESTARLD FLWKLQATGE KEEMEELQAY NRRLLHNILP KDVAAHFLAR
ERRNDELYYQ SCECVAVMFA SIANFSEFYV ELEANNEGVE CLRLLNEIIA DFDEIISEER
FRQLEKIKTI GSTYMAASGL NASTYDQVGR SHITALADYA MRLMEQMKHI NEHSFNNFQM
KIGLNMGPVV AGVIGARKPQ YDIWGNTVNV SSRMDSTGVP DRIQVTTDLY QVLAAKGYQL
ECRGVVKVKG KGEMTTYFLN GGPSS


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