ADCY1_HUMAN
ID ADCY1_HUMAN Reviewed; 1119 AA.
AC Q08828; A4D2L8; Q75MI1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Adenylate cyclase type 1;
DE EC=4.6.1.1 {ECO:0000250|UniProtKB:P19754};
DE AltName: Full=ATP pyrophosphate-lyase 1;
DE AltName: Full=Adenylate cyclase type I;
DE AltName: Full=Adenylyl cyclase 1;
DE AltName: Full=Ca(2+)/calmodulin-activated adenylyl cyclase;
GN Name=ADCY1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 281-1119, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=8314585; DOI=10.1006/geno.1993.1213;
RA Villacres E.C., Xia Z., Bookbinder L.H., Edelhoff S., Disteche C.M.,
RA Storm D.R.;
RT "Cloning, chromosomal mapping, and expression of human fetal brain type I
RT adenylyl cyclase.";
RL Genomics 16:473-478(1993).
RN [4]
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 [5]
RP INVOLVEMENT IN DFNB44.
RX PubMed=24482543; DOI=10.1093/hmg/ddu042;
RA Santos-Cortez R.L., Lee K., Giese A.P., Ansar M., Amin-Ud-Din M., Rehn K.,
RA Wang X., Aziz A., Chiu I., Hussain Ali R., Smith J.D., Shendure J.,
RA Bamshad M., Nickerson D.A., Ahmed Z.M., Ahmad W., Riazuddin S., Leal S.M.;
RT "Adenylate cyclase 1 (ADCY1) mutations cause recessive hearing impairment
RT in humans and defects in hair cell function and hearing in zebrafish.";
RL Hum. Mol. Genet. 23:3289-3298(2014).
CC -!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP in
CC response to G-protein signaling. Mediates responses to increased
CC cellular Ca(2+)/calmodulin levels (By similarity). May be involved in
CC regulatory processes in the central nervous system. May play a role in
CC memory and learning. Plays a role in the regulation of the circadian
CC rhythm of daytime contrast sensitivity probably by modulating the
CC rhythmic synthesis of cyclic AMP in the retina (By similarity).
CC {ECO:0000250|UniProtKB:O88444, ECO:0000250|UniProtKB:P19754}.
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:P19754};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P19754};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P19754};
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 calcium/calmodulin. Activated by
CC forskolin. Activated by the G protein alpha subunit GNAS. Inhibited by
CC the G protein beta and gamma subunit complex. Inhibited by the ATP
CC analogs adenosine, 2'-deoxyadenosine and 2'-deoxy-3'-AMP.
CC {ECO:0000250|UniProtKB:P19754}.
CC -!- SUBUNIT: Interacts with CALM. {ECO:0000250|UniProtKB:P19754}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P19754}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P19754}. Cell membrane
CC {ECO:0000269|PubMed:11549699}; Multi-pass membrane protein
CC {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O88444}. Membrane raft
CC {ECO:0000250|UniProtKB:P19754}. Note=Expressed in the cytoplasm of
CC supporting cells and hair cells of the cochlea vestibule, as well as to
CC the cochlear hair cell nuclei and stereocilia.
CC {ECO:0000250|UniProtKB:O88444}.
CC -!- TISSUE SPECIFICITY: Detected in zona glomerulosa and zona fasciculata
CC in the adrenal gland (at protein level) (PubMed:11549699). Brain,
CC retina and adrenal medulla. {ECO:0000269|PubMed:11549699,
CC ECO:0000269|PubMed:8314585}.
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:0000250|UniProtKB:P30803}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P19754}.
CC -!- DISEASE: Deafness, autosomal recessive, 44 (DFNB44) [MIM:610154]: A
CC form of non-syndromic deafness characterized by prelingual profound
CC hearing loss affecting all frequencies. {ECO:0000269|PubMed:24482543}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AC069008; AAS07467.1; -; Genomic_DNA.
DR EMBL; AC091439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236960; EAL23741.1; -; Genomic_DNA.
DR EMBL; L05500; AAA02907.1; -; mRNA.
DR CCDS; CCDS34631.1; -.
DR PIR; A47007; A47007.
DR RefSeq; NP_066939.1; NM_021116.2.
DR AlphaFoldDB; Q08828; -.
DR SMR; Q08828; -.
DR BioGRID; 106621; 4.
DR IntAct; Q08828; 2.
DR MINT; Q08828; -.
DR STRING; 9606.ENSP00000297323; -.
DR BindingDB; Q08828; -.
DR ChEMBL; CHEMBL2899; -.
DR DrugBank; DB00131; Adenosine phosphate.
DR DrugBank; DB00171; ATP.
DR DrugBank; DB09121; Aurothioglucose.
DR DrugBank; DB00424; Hyoscyamine.
DR DrugBank; DB13749; Magnesium gluconate.
DR DrugCentral; Q08828; -.
DR GuidetoPHARMACOLOGY; 1278; -.
DR GlyGen; Q08828; 1 site.
DR iPTMnet; Q08828; -.
DR PhosphoSitePlus; Q08828; -.
DR BioMuta; ADCY1; -.
DR DMDM; 62512172; -.
DR MassIVE; Q08828; -.
DR PaxDb; Q08828; -.
DR PeptideAtlas; Q08828; -.
DR PRIDE; Q08828; -.
DR ProteomicsDB; 58648; -.
DR Antibodypedia; 4335; 251 antibodies from 29 providers.
DR DNASU; 107; -.
DR Ensembl; ENST00000297323.12; ENSP00000297323.7; ENSG00000164742.16.
DR GeneID; 107; -.
DR KEGG; hsa:107; -.
DR MANE-Select; ENST00000297323.12; ENSP00000297323.7; NM_021116.4; NP_066939.1.
DR UCSC; uc003tne.5; human.
DR CTD; 107; -.
DR DisGeNET; 107; -.
DR GeneCards; ADCY1; -.
DR HGNC; HGNC:232; ADCY1.
DR HPA; ENSG00000164742; Group enriched (brain, liver, retina).
DR MalaCards; ADCY1; -.
DR MIM; 103072; gene.
DR MIM; 610154; phenotype.
DR neXtProt; NX_Q08828; -.
DR OpenTargets; ENSG00000164742; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA24560; -.
DR VEuPathDB; HostDB:ENSG00000164742; -.
DR eggNOG; KOG3619; Eukaryota.
DR GeneTree; ENSGT00940000154872; -.
DR HOGENOM; CLU_001072_2_1_1; -.
DR InParanoid; Q08828; -.
DR OMA; ERRMCPY; -.
DR OrthoDB; 594476at2759; -.
DR PhylomeDB; Q08828; -.
DR TreeFam; TF313845; -.
DR BRENDA; 4.6.1.1; 2681.
DR PathwayCommons; Q08828; -.
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-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
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; Q08828; -.
DR SIGNOR; Q08828; -.
DR BioGRID-ORCS; 107; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; ADCY1; human.
DR GeneWiki; ADCY1; -.
DR GenomeRNAi; 107; -.
DR Pharos; Q08828; Tchem.
DR PRO; PR:Q08828; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q08828; protein.
DR Bgee; ENSG00000164742; Expressed in middle temporal gyrus and 150 other tissues.
DR ExpressionAtlas; Q08828; baseline and differential.
DR Genevisible; Q08828; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008294; F:calcium- and calmodulin-responsive adenylate cyclase activity; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin 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:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006171; P:cAMP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR GO; GO:0150076; P:neuroinflammatory response; ISS:UniProtKB.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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; IPR029787; Nucleotide_cyclase.
DR Pfam; PF16214; AC_N; 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 ATP-binding; Biological rhythms; Calmodulin-binding; cAMP biosynthesis;
KW Cell membrane; Cytoplasm; Deafness; Glycoprotein; Lyase; Magnesium;
KW Manganese; Membrane; Metal-binding; Non-syndromic deafness;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1119
FT /note="Adenylate cyclase type 1"
FT /id="PRO_0000195682"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 674..694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 753..773
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 775..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..1119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..520
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250"
FT REGION 1024..1047
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250"
FT BINDING 308..313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 308
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 308
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 309
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 350..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 352
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 352
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 396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 920
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 997..999
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1004..1008
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1044
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88444"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 456
FT /note="P -> L (in dbSNP:rs12721473)"
FT /id="VAR_029186"
FT VARIANT 940
FT /note="A -> T (in dbSNP:rs45444695)"
FT /id="VAR_029187"
FT VARIANT 984
FT /note="V -> M (in dbSNP:rs2293106)"
FT /id="VAR_048246"
SQ SEQUENCE 1119 AA; 123440 MW; E8DDC8FCB58743D7 CRC64;
MAGAPRGGGG GGGGAGEPGG AERAAGTSRR RGLRACDEEF ACPELEALFR GYTLRLEQAA
TLKALAVLSL LAGALALAEL LGAPGPAPGL AKGSHPVHCV LFLALLVVTN VRSLQVPQLQ
QVGQLALLFS LTFALLCCPF ALGGPARGSA GAAGGPATAE QGVWQLLLVT FVSYALLPVR
SLLAIGFGLV VAASHLLVTA TLVPAKRPRL WRTLGANALL FVGVNMYGVF VRILTERSQR
KAFLQARSCI EDRLRLEDEN EKQERLLMSL LPRNVAMEMK EDFLKPPERI FHKIYIQRHD
NVSILFADIV GFTGLASQCT AQELVKLLNE LFGKFDELAT ENHCRRIKIL GDCYYCVSGL
TQPKTDHAHC CVEMGLDMID TITSVAEATE VDLNMRVGLH TGRVLCGVLG LRKWQYDVWS
NDVTLANVME AAGLPGKVHI TKTTLACLNG DYEVEPGYGH ERNSFLKTHN IETFFIVPSH
RRKIFPGLIL SDIKPAKRMK FKTVCYLLVQ LMHCRKMFKA EIPFSNVMTC EDDDKRRALR
TASEKLRNRS SFSTNVVYTT PGTRVNRYIS RLLEARQTEL EMADLNFFTL KYKHVEREQK
YHQLQDEYFT SAVVLTLILA ALFGLVYLLI FPQSVVVLLL LVFCICFLVA CVLYLHITRV
QCFPGCLTIQ IRTVLCIFIV VLIYSVAQGC VVGCLPWAWS SKPNSSLVVL SSGGQRTALP
TLPCESTHHA LLCCLVGTLP LAIFFRVSSL PKMILLSGLT TSYILVLELS GYTRTGGGAV
SGRSYEPIVA ILLFSCALAL HARQVDIRLR LDYLWAAQAE EEREDMEKVK LDNRRILFNL
LPAHVAQHFL MSNPRNMDLY YQSYSQVGVM FASIPNFNDF YIELDGNNMG VECLRLLNEI
IADFDELMEK DFYKDIEKIK TIGSTYMAAV GLAPTSGTKA KKSISSHLST LADFAIEMFD
VLDEINYQSY NDFVLRVGIN VGPVVAGVIG ARRPQYDIWG NTVNVASRMD STGVQGRIQV
TEEVHRLLRR CPYHFVCRGK VSVKGKGEML TYFLEGRTDG NGSQIRSLGL DRKMCPFGRA
GLQGRRPPVC PMPGVSVRAG LPPHSPGQYL PSAAAGKEA
