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Adenylate cyclase type 9 (EC 4.6.1.1) (ATP pyrophosphate-lyase 9) (Adenylate cyclase type IX) (ACIX) (Adenylyl cyclase 9) (AC9)

 ADCY9_HUMAN             Reviewed;        1353 AA.
O60503; A7E2V5; A7E2X2; D3DUD1; O60273; Q4ZHT9; Q4ZIR5; Q9BWT4;
Q9UGP2;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
13-DEC-2002, sequence version 4.
28-MAR-2018, entry version 162.
RecName: Full=Adenylate cyclase type 9 {ECO:0000303|PubMed:9628827};
EC=4.6.1.1 {ECO:0000269|PubMed:10987815, ECO:0000269|PubMed:12972952, ECO:0000269|PubMed:15879435, ECO:0000269|PubMed:9628827};
AltName: Full=ATP pyrophosphate-lyase 9;
AltName: Full=Adenylate cyclase type IX {ECO:0000303|PubMed:10987815};
Short=ACIX {ECO:0000303|PubMed:10987815};
AltName: Full=Adenylyl cyclase 9;
Short=AC9 {ECO:0000303|PubMed:15879435};
Name=ADCY9; Synonyms=KIAA0520;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, ENZYME
REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=9628827; DOI=10.1006/geno.1998.5293;
Hacker B.M., Tomlinson J.E., Wayman G.A., Sultana R., Chan G.,
Villacres E., Disteche C., Storm D.R.;
"Cloning, chromosomal mapping, and regulatory properties of the human
type 9 adenylyl cyclase (ADCY9).";
Genomics 50:97-104(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
SPECIFICITY, AND VARIANT MET-772.
PubMed=12972952; DOI=10.1097/00008571-200309000-00002;
Small K.M., Brown K.M., Theiss C.T., Seman C.A., Weiss S.T.,
Liggett S.B.;
"An Ile to Met polymorphism in the catalytic domain of adenylyl
cyclase type 9 confers reduced beta2-adrenergic receptor
stimulation.";
Pharmacogenetics 13:535-541(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, AND VARIANT MET-772.
PubMed=15879435; DOI=10.1093/hmg/ddi175;
Tantisira K.G., Small K.M., Litonjua A.A., Weiss S.T., Liggett S.B.;
"Molecular properties and pharmacogenetics of a polymorphism of
adenylyl cyclase type 9 in asthma: interaction between beta-agonist
and corticosteroid pathways.";
Hum. Mol. Genet. 14:1671-1677(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT
SER-1154.
PubMed=10987815; DOI=10.1046/j.1471-4159.2000.0751358.x;
Paterson J.M., Smith S.M., Simpson J., Grace O.C., Sosunov A.A.,
Bell J.E., Antoni F.A.;
"Characterisation of human adenylyl cyclase IX reveals inhibition by
Ca(2+)/Calcineurin and differential mRNA plyadenylation.";
J. Neurochem. 75:1358-1367(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Toyota T., Yamada K., Meerabux J., Hattori E., Saito K.,
Yoshitsugu K., Shimizu H., Nankai M., Toru M., Detera-Wadleigh S.D.,
Yoshikawa T.;
"Mutation screening, case control study and transmission
disequilibrium analysis of adenylate cyclase type 9 (ADCY9) gene in
functional psychoses.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-1154.
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[7]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[8]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R., Ishikawa K.;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-1154.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1259, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1307, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1257 AND SER-1259, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Adenylyl cyclase that catalyzes the formation of the
signaling molecule cAMP in response to activation of G protein-
coupled receptors (PubMed:9628827, PubMed:12972952,
PubMed:15879435, PubMed:10987815). Contributes to signaling
cascades activated by CRH (corticotropin-releasing factor),
corticosteroids and beta-adrenergic receptors (PubMed:9628827).
{ECO:0000269|PubMed:10987815, ECO:0000269|PubMed:12972952,
ECO:0000269|PubMed:15879435, ECO:0000269|PubMed:9628827}.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
{ECO:0000269|PubMed:10987815, ECO:0000269|PubMed:12972952,
ECO:0000269|PubMed:15879435, ECO:0000269|PubMed:9628827}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P30803};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:P30803};
Note=Binds 2 magnesium ions per subunit. Is also active with
manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
-!- ENZYME REGULATION: Insensitive to calcium/calmodulin, forskolin
and somatostatin. Stimulated by beta-adrenergic receptor
activation (PubMed:9628827). Activity is down-regulated by
calcium/calcineurin (PubMed:10987815).
{ECO:0000269|PubMed:10987815, ECO:0000269|PubMed:9628827}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10987815,
ECO:0000269|PubMed:9628827}; Multi-pass membrane protein
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Detected in skeletal muscle, pancreas, lung,
heart, kidney, liver, brain and placenta (PubMed:9628827,
PubMed:10987815). Expressed in multiple cells of the lung, with
expression highest in airway smooth muscle (PubMed:12972952).
{ECO:0000269|PubMed:10987815, ECO:0000269|PubMed:12972952,
ECO:0000269|PubMed:9628827}.
-!- 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}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
-!- SEQUENCE CAUTION:
Sequence=AAC24201.1; Type=Frameshift; Positions=1252; Evidence={ECO:0000305};
Sequence=BAA25446.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF036927; AAC24201.1; ALT_FRAME; mRNA.
EMBL; DQ008441; AAY27880.1; -; mRNA.
EMBL; DQ005545; AAY21237.1; -; mRNA.
EMBL; AJ133123; CAB65084.1; -; mRNA.
EMBL; AY028959; AAK29464.1; -; Genomic_DNA.
EMBL; AY028949; AAK29464.1; JOINED; Genomic_DNA.
EMBL; AY028950; AAK29464.1; JOINED; Genomic_DNA.
EMBL; AY028951; AAK29464.1; JOINED; Genomic_DNA.
EMBL; AY028952; AAK29464.1; JOINED; Genomic_DNA.
EMBL; AY028953; AAK29464.1; JOINED; Genomic_DNA.
EMBL; AY028954; AAK29464.1; JOINED; Genomic_DNA.
EMBL; AY028955; AAK29464.1; JOINED; Genomic_DNA.
EMBL; AY028956; AAK29464.1; JOINED; Genomic_DNA.
EMBL; AY028957; AAK29464.1; JOINED; Genomic_DNA.
EMBL; AB011092; BAA25446.3; ALT_INIT; mRNA.
EMBL; CH471112; EAW85331.1; -; Genomic_DNA.
EMBL; CH471112; EAW85332.1; -; Genomic_DNA.
EMBL; BC136657; AAI36658.1; -; mRNA.
EMBL; BC136658; AAI36659.1; -; mRNA.
EMBL; BC151207; AAI51208.1; -; mRNA.
EMBL; BC151229; AAI51230.1; -; mRNA.
CCDS; CCDS32382.1; -.
RefSeq; NP_001107.2; NM_001116.3.
UniGene; Hs.391860; -.
UniGene; Hs.610484; -.
ProteinModelPortal; O60503; -.
SMR; O60503; -.
BioGrid; 106628; 43.
IntAct; O60503; 3.
MINT; O60503; -.
STRING; 9606.ENSP00000294016; -.
ChEMBL; CHEMBL2655; -.
iPTMnet; O60503; -.
PhosphoSitePlus; O60503; -.
BioMuta; ADCY9; -.
EPD; O60503; -.
MaxQB; O60503; -.
PaxDb; O60503; -.
PeptideAtlas; O60503; -.
PRIDE; O60503; -.
Ensembl; ENST00000294016; ENSP00000294016; ENSG00000162104.
GeneID; 115; -.
KEGG; hsa:115; -.
UCSC; uc002cvx.4; human.
CTD; 115; -.
DisGeNET; 115; -.
EuPathDB; HostDB:ENSG00000162104.9; -.
GeneCards; ADCY9; -.
HGNC; HGNC:240; ADCY9.
HPA; HPA041328; -.
HPA; HPA044225; -.
MIM; 603302; gene.
neXtProt; NX_O60503; -.
OpenTargets; ENSG00000162104; -.
PharmGKB; PA30; -.
eggNOG; KOG3618; Eukaryota.
eggNOG; COG2114; LUCA.
GeneTree; ENSGT00760000119042; -.
HOVERGEN; HBG050459; -.
InParanoid; O60503; -.
KO; K08049; -.
OMA; LNQSAIS; -.
OrthoDB; EOG091G0285; -.
PhylomeDB; O60503; -.
TreeFam; TF313845; -.
Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation.
Reactome; R-HSA-163615; PKA activation.
Reactome; R-HSA-164378; PKA activation in glucagon signalling.
Reactome; R-HSA-170660; Adenylate cyclase activating pathway.
Reactome; R-HSA-170670; Adenylate cyclase inhibitory pathway.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-418597; G alpha (z) signalling events.
Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-HSA-5610787; Hedgehog 'off' state.
SIGNOR; O60503; -.
ChiTaRS; ADCY9; human.
GeneWiki; ADCY9; -.
GenomeRNAi; 115; -.
PRO; PR:O60503; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000162104; -.
CleanEx; HS_ADCY9; -.
ExpressionAtlas; O60503; baseline and differential.
Genevisible; O60503; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:Reactome.
GO; GO:0034199; P:activation of protein kinase A activity; TAS:Reactome.
GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IMP:UniProtKB.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0006171; P:cAMP biosynthetic process; IDA:UniProtKB.
GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 3.30.70.1230; -; 2.
InterPro; IPR001054; A/G_cyclase.
InterPro; IPR018297; A/G_cyclase_CS.
InterPro; IPR029787; Nucleotide_cyclase.
Pfam; PF00211; Guanylate_cyc; 2.
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; Complete proteome;
Glycoprotein; Lyase; Magnesium; Manganese; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Transmembrane; Transmembrane helix.
CHAIN 1 1353 Adenylate cyclase type 9.
/FTId=PRO_0000195708.
TOPO_DOM 1 117 Cytoplasmic. {ECO:0000255}.
TRANSMEM 118 138 Helical. {ECO:0000255}.
TOPO_DOM 139 141 Extracellular. {ECO:0000255}.
TRANSMEM 142 162 Helical. {ECO:0000255}.
TOPO_DOM 163 171 Cytoplasmic. {ECO:0000255}.
TRANSMEM 172 192 Helical. {ECO:0000255}.
TOPO_DOM 193 215 Extracellular. {ECO:0000255}.
TRANSMEM 216 235 Helical. {ECO:0000255}.
TOPO_DOM 236 241 Cytoplasmic. {ECO:0000255}.
TRANSMEM 242 259 Helical. {ECO:0000255}.
TOPO_DOM 260 280 Extracellular. {ECO:0000255}.
TRANSMEM 281 301 Helical. {ECO:0000255}.
TOPO_DOM 302 786 Cytoplasmic. {ECO:0000255}.
TRANSMEM 787 807 Helical. {ECO:0000255}.
TOPO_DOM 808 818 Extracellular. {ECO:0000255}.
TRANSMEM 819 839 Helical. {ECO:0000255}.
TOPO_DOM 840 867 Cytoplasmic. {ECO:0000255}.
TRANSMEM 868 888 Helical. {ECO:0000255}.
TOPO_DOM 889 891 Extracellular. {ECO:0000255}.
TRANSMEM 892 912 Helical. {ECO:0000255}.
TOPO_DOM 913 920 Cytoplasmic. {ECO:0000255}.
TRANSMEM 921 941 Helical. {ECO:0000255}.
TOPO_DOM 942 975 Extracellular. {ECO:0000255}.
TRANSMEM 976 996 Helical. {ECO:0000255}.
TOPO_DOM 997 1353 Cytoplasmic. {ECO:0000255}.
DOMAIN 394 521 Guanylate cyclase 1.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
DOMAIN 1058 1198 Guanylate cyclase 2.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
NP_BIND 399 404 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 441 443 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 1185 1187 ATP. {ECO:0000250|UniProtKB:P26769}.
NP_BIND 1192 1196 ATP. {ECO:0000250|UniProtKB:P26769}.
METAL 399 399 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 399 399 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 400 400 Magnesium 2; via carbonyl oxygen;
catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
METAL 443 443 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 443 443 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
BINDING 487 487 ATP. {ECO:0000250|UniProtKB:P30803}.
BINDING 1108 1108 ATP. {ECO:0000250|UniProtKB:P26769}.
BINDING 1232 1232 ATP. {ECO:0000250|UniProtKB:P26769}.
MOD_RES 610 610 Phosphoserine.
{ECO:0000250|UniProtKB:P51830}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000250|UniProtKB:P51830}.
MOD_RES 691 691 Phosphoserine.
{ECO:0000250|UniProtKB:P51830}.
MOD_RES 706 706 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1257 1257 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1259 1259 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1295 1295 Phosphoserine.
{ECO:0000250|UniProtKB:P51830}.
MOD_RES 1307 1307 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 955 955 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 964 964 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 772 772 I -> M (common polymorphism; found in
37.5% of the Asian population, in 30% of
the Caucasian population and in 16.3% of
the African-American population; reduced
adenylyl cyclase activity in response to
stimulation of the beta-adregnergic
receptor by Mn(2+) agonists isoproteronol
and NaF; increased albuterol-stimulated
adenylyl cyclase activity in the presence
of corticosteroid; dbSNP:rs2230739).
{ECO:0000269|PubMed:12972952,
ECO:0000269|PubMed:15879435}.
/FTId=VAR_023750.
VARIANT 1154 1154 N -> S (in dbSNP:rs61731445).
{ECO:0000269|PubMed:10987815,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9628581}.
/FTId=VAR_070887.
CONFLICT 493 493 G -> R (in Ref. 4; CAB65084).
{ECO:0000305}.
CONFLICT 884 884 V -> A (in Ref. 4; CAB65084).
{ECO:0000305}.
CONFLICT 1308 1308 P -> R (in Ref. 4; CAB65084).
{ECO:0000305}.
SEQUENCE 1353 AA; 150701 MW; 4CBF051EA49B5B7B CRC64;
MASPPHQQLL HHHSTEVSCD SSGDSNSVRV KINPKQLSSN SHPKHCKYSI SSSCSSSGDS
GGVPRRVGGG GRLRRQKKLP QLFERASSRW WDPKFDSVNL EEACLERCFP QTQRRFRYAL
FYIGFACLLW SIYFAVHMRS RLIVMVAPAL CFLLVCVGFF LFTFTKLYAR HYAWTSLALT
LLVFALTLAA QFQVLTPVSG RGDSSNLTAT ARPTDTCLSQ VGSFSMCIEV LFLLYTVMHL
PLYLSLCLGV AYSVLFETFG YHFRDEACFP SPGAGALHWE LLSRGLLHGC IHAIGVHLFV
MSQVRSRSTF LKVGQSIMHG KDLEVEKALK ERMIHSVMPR IIADDLMKQG DEESENSVKR
HATSSPKNRK KKSSIQKAPI AFRPFKMQQI EEVSILFADI VGFTKMSANK SAHALVGLLN
DLFGRFDRLC EETKCEKIST LGDCYYCVAG CPEPRADHAY CCIEMGLGMI KAIEQFCQEK
KEMVNMRVGV HTGTVLCGIL GMRRFKFDVW SNDVNLANLM EQLGVAGKVH ISEATAKYLD
DRYEMEDGKV IERLGQSVVA DQLKGLKTYL ISGQRAKESR CSCAEALLSG FEVIDGSQVS
SGPRGQGTAS SGNVSDLAQT VKTFDNLKTC PSCGITFAPK SEAGAEGGAP QNGCQDEHKN
STKASGGPNP KTQNGLLSPP QEEKLTNSQT SLCEILQEKG RWAGVSLDQS ALLPLRFKNI
REKTDAHFVD VIKEDSLMKD YFFKPPINQF SLNFLDQELE RSYRTSYQEE VIKNSPVKTF
ASPTFSSLLD VFLSTTVFLT LSTTCFLKYE AATVPPPPAA LAVFSAALLL EVLSLAVSIR
MVFFLEDVMA CTKRLLEWIA GWLPRHCIGA ILVSLPALAV YSHVTSEYET NIHFPVFTGS
AALIAVVHYC NFCQLSSWMR SSLATVVGAG PLLLLYVSLC PDSSVLTSPL DAVQNFSSER
NPCNSSVPRD LRRPASLIGQ EVVLVFFLLL LLVWFLNREF EVSYRLHYHG DVEADLHRTK
IQSMRDQADW LLRNIIPYHV AEQLKVSQTY SKNHDSGGVI FASIVNFSEF YEENYEGGKE
CYRVLNELIG DFDELLSKPD YSSIEKIKTI GATYMAASGL NTAQAQDGSH PQEHLQILFE
FAKEMMRVVD DFNNNMLWFN FKLRVGFNHG PLTAGVIGTT KLLYDIWGDT VNIASRMDTT
GVECRIQVSE ESYRVLSKMG YDFDYRGTVN VKGKGQMKTY LYPKCTDHRV IPQHQLSISP
DIRVQVDGSI GRSPTDEIAN LVPSVQYVDK TSLGSDSSTQ AKDAHLSPKR PWKEPVKAEE
RGRFGKAIEK DDCDETGIEE ANELTKLNVS KSV


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