ANK3_RAT
ID ANK3_RAT Reviewed; 2622 AA.
AC O70511; Q574D7; Q574D8; Q574D9; Q574E0; Q574E2; Q8VDA0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Ankyrin-3;
DE Short=ANK-3;
DE AltName: Full=Ankyrin-G;
GN Name=Ank3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=9744885; DOI=10.1083/jcb.142.6.1571;
RA Zhang X., Bennett V.;
RT "Restriction of 480/270-kD ankyrin G to axon proximal segments requires
RT multiple ankyrin G-specific domains.";
RL J. Cell Biol. 142:1571-1581(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX PubMed=11796721; DOI=10.1074/jbc.m111299200;
RA Gagelin C., Constantin B., Deprette C., Ludosky M.A., Recouvreur M.,
RA Cartaud J., Cognard C., Raymond G., Kordeli E.;
RT "Identification of Ank(G107), a muscle-specific ankyrin-G isoform.";
RL J. Biol. Chem. 277:12978-12987(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6 AND 7), SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX PubMed=15953600; DOI=10.1016/j.yexcr.2005.04.013;
RA Hopitzan A.A., Baines A.J., Ludosky M.A., Recouvreur M., Kordeli E.;
RT "Ankyrin-G in skeletal muscle: tissue-specific alternative splicing
RT contributes to the complexity of the sarcolemmal cytoskeleton.";
RL Exp. Cell Res. 309:86-98(2005).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=15579534; DOI=10.1073/pnas.0403711101;
RA Mohler P.J., Rivolta I., Napolitano C., LeMaillet G., Lambert S.,
RA Priori S.G., Bennett V.;
RT "Nav1.5 E1053K mutation causing Brugada syndrome blocks binding to ankyrin-
RT G and expression of Nav1.5 on the surface of cardiomyocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17533-17538(2004).
RN [5]
RP INTERACTION WITH PLEC AND FLNC, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21223964; DOI=10.1016/j.yexcr.2011.01.002;
RA Maiweilidan Y., Klauza I., Kordeli E.;
RT "Novel interactions of ankyrins-G at the costameres: the muscle-specific
RT Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C.";
RL Exp. Cell Res. 317:724-736(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631; SER-855; SER-869;
RP SER-875; SER-921; SER-924; SER-965; SER-967; SER-1121; SER-1458; SER-1984;
RP SER-2102; SER-2114; SER-2117; SER-2457 AND SER-2544, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-1679 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-851 (ISOFORMS 4 AND 5), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Membrane-cytoskeleton linker. May participate in the
CC maintenance/targeting of ion channels and cell adhesion molecules at
CC the nodes of Ranvier and axonal initial segments. In skeletal muscle,
CC required for costamere localization of DMD and betaDAG1 (By
CC similarity). Regulates KCNA1 channel activity in function of dietary
CC Mg(2+) levels, and thereby contributes to the regulation of renal
CC Mg(2+) reabsorption (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:G5E8K5}.
CC -!- SUBUNIT: May be a constituent of a NFASC/NRCAM/ankyrin G complex.
CC Interacts with RHBG. Directly interacts with DMD and betaDAG1; this
CC interaction does not interfere with DMD-binding and is required for DMD
CC and betaDAG1 retention at costameres. Interacts (via N-terminal ANK
CC repeats) with SCHIP1 isoform 7 (via C-terminus); this interaction is
CC required for the localization at axon initial segments (AISs) and nodes
CC of Ranvier (NRs) (By similarity). Interacts with PLEC and FLNC
CC (PubMed:21223964). Isoform 7 interacts with PLEC and FLNC through its
CC muscle-specific C-terminal sequence. Interacts with KCNA1; this
CC inhibits channel activity (By similarity). Interacts (via ANK repeats)
CC with IQCJ-SCHIP1; required for IQCJ-SCHIP1 localization at axon initial
CC segments (AIS) and nodes of Ranvier (By similarity). Interacts with
CC SCHIP1 (By similarity). Interacts with SCN5A (By similarity).
CC {ECO:0000250|UniProtKB:G5E8K5, ECO:0000250|UniProtKB:Q12955,
CC ECO:0000269|PubMed:21223964}.
CC -!- INTERACTION:
CC O70511-7; Q14315: FLNC; Xeno; NbExp=2; IntAct=EBI-9663485, EBI-489954;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q12955}. Cell projection, axon
CC {ECO:0000269|PubMed:9744885}. Cell membrane
CC {ECO:0000269|PubMed:21223964}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:15953600, ECO:0000269|PubMed:21223964}.
CC Postsynaptic cell membrane {ECO:0000269|PubMed:11796721}. Lysosome
CC {ECO:0000250|UniProtKB:G5E8K5}. Cell membrane, sarcolemma, T-tubule
CC {ECO:0000269|PubMed:15579534}. Note=When transfected in root dorsal
CC ganglia, predominantly located in the axolemma of the axon proximal
CC segments (PubMed:9744885). Also associated with the plasma membrane in
CC neuron cell bodies, although at a lower level than in the axon proximal
CC segment (PubMed:9744885). Isoform 1 is restricted to the axolemma of
CC the axon proximal segment. Isoforms containing the muscle-specific 76
CC amino-acid insertion localize to the sarcolemma and on the postsynaptic
CC membrane of neuromuscular junctions (PubMed:11796721).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=AnkG270;
CC IsoId=O70511-1; Sequence=Displayed;
CC Name=2; Synonyms=AnkG217;
CC IsoId=O70511-2; Sequence=VSP_055005, VSP_055006, VSP_055007,
CC VSP_055008, VSP_055009, VSP_055011;
CC Name=3; Synonyms=AnkG197;
CC IsoId=O70511-3; Sequence=VSP_055005, VSP_055006, VSP_055007,
CC VSP_055008, VSP_055010, VSP_055012;
CC Name=4; Synonyms=Ank130;
CC IsoId=O70511-4; Sequence=VSP_055004, VSP_055008, VSP_055009,
CC VSP_055013;
CC Name=5; Synonyms=AnkG128;
CC IsoId=O70511-5; Sequence=VSP_055004, VSP_055008, VSP_055009,
CC VSP_055011;
CC Name=6; Synonyms=AnkG109;
CC IsoId=O70511-6; Sequence=VSP_055004, VSP_055008, VSP_055010,
CC VSP_055013;
CC Name=7; Synonyms=AnkG107;
CC IsoId=O70511-7; Sequence=VSP_055004, VSP_055008, VSP_055010,
CC VSP_055011;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in brain and testis,
CC followed by skin, kidney, liver and spleen. Isoforms 2, 3, 4, 5, 6 and
CC 7 may be specifically expressed in muscle tissues, including heart and
CC skeletal muscle (extensor digitorum longus) (at protein level)
CC (PubMed:11796721). {ECO:0000269|PubMed:11796721,
CC ECO:0000269|PubMed:15953600, ECO:0000269|PubMed:21223964}.
CC -!- MISCELLANEOUS: [Isoform 2]: The 76 amino-acid long sequence from Asp-
CC 1888 to Val-1963 is encoded by a muscle-specific exon. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: The 76 amino-acid long sequence from Asp-
CC 1710 to Val-1785 is encoded by a muscle-specific exon. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: The 76 amino-acid long sequence from Asp-
CC 1077 to Val-1152 is encoded by a muscle-specific exon. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: The 76 amino-acid long sequence from Asp-
CC 1060 to Val-1135 is encoded by a muscle-specific exon. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: The 76 amino-acid long sequence from Asp-
CC 881 to Val-956 is encoded by a muscle-specific exon. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: The 76 amino-acid long sequence from Asp-
CC 864 to Val-939 is encoded by a muscle-specific exon. {ECO:0000305}.
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DR EMBL; AF102552; AAC78143.1; -; mRNA.
DR EMBL; AJ428573; CAD21705.1; -; mRNA.
DR EMBL; AJ812019; CAH19219.1; -; mRNA.
DR EMBL; AJ812021; CAH19221.1; -; mRNA.
DR EMBL; AJ812022; CAH19222.1; -; mRNA.
DR EMBL; AJ812023; CAH19223.1; -; mRNA.
DR EMBL; AJ812024; CAH19224.1; -; mRNA.
DR RefSeq; NP_001029156.1; NM_001033984.1. [O70511-1]
DR RefSeq; NP_113993.1; NM_031805.1. [O70511-2]
DR PDB; 5YIP; X-ray; 1.85 A; B=1985-2010.
DR PDB; 5YIQ; X-ray; 2.60 A; D=1985-2010.
DR PDB; 6A9X; X-ray; 2.20 A; A=1987-2010.
DR PDB; 6M3P; X-ray; 3.31 A; C/E=975-1465.
DR PDB; 6M3R; X-ray; 4.31 A; E=975-1465.
DR PDBsum; 5YIP; -.
DR PDBsum; 5YIQ; -.
DR PDBsum; 6A9X; -.
DR PDBsum; 6M3P; -.
DR PDBsum; 6M3R; -.
DR AlphaFoldDB; O70511; -.
DR SMR; O70511; -.
DR BioGRID; 262995; 9.
DR CORUM; O70511; -.
DR DIP; DIP-60342N; -.
DR IntAct; O70511; 9.
DR MINT; O70511; -.
DR STRING; 10116.ENSRNOP00000043687; -.
DR iPTMnet; O70511; -.
DR PhosphoSitePlus; O70511; -.
DR SwissPalm; O70511; -.
DR jPOST; O70511; -.
DR PaxDb; O70511; -.
DR PRIDE; O70511; -.
DR ABCD; O70511; 6 sequenced antibodies.
DR Ensembl; ENSRNOT00000085985; ENSRNOP00000072993; ENSRNOG00000053288. [O70511-3]
DR Ensembl; ENSRNOT00000090273; ENSRNOP00000071942; ENSRNOG00000053288. [O70511-2]
DR GeneID; 361833; -.
DR KEGG; rno:361833; -.
DR UCSC; RGD:620157; rat.
DR CTD; 288; -.
DR RGD; 620157; Ank3.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000154939; -.
DR OrthoDB; 1011028at2759; -.
DR PRO; PR:O70511; -.
DR Proteomes; UP000002494; Chromosome 20.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0043194; C:axon initial segment; IDA:BHF-UCL.
DR GO; GO:0009925; C:basal plasma membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0043034; C:costamere; TAS:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0033268; C:node of Ranvier; IDA:ARUK-UCL.
DR GO; GO:0033270; C:paranode region of axon; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
DR GO; GO:0014731; C:spectrin-associated cytoskeleton; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
DR GO; GO:0030018; C:Z disc; IDA:RGD.
DR GO; GO:0045296; F:cadherin binding; IPI:BHF-UCL.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:BHF-UCL.
DR GO; GO:0140031; F:phosphorylation-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL.
DR GO; GO:0030507; F:spectrin binding; IDA:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; IMP:RGD.
DR GO; GO:0045184; P:establishment of protein localization; ISO:RGD.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:RGD.
DR GO; GO:0010960; P:magnesium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0072660; P:maintenance of protein location in plasma membrane; ISO:RGD.
DR GO; GO:0071709; P:membrane assembly; IGI:BHF-UCL.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:RGD.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0007528; P:neuromuscular junction development; IEP:RGD.
DR GO; GO:0019228; P:neuronal action potential; ISO:RGD.
DR GO; GO:0007009; P:plasma membrane organization; ISO:RGD.
DR GO; GO:2001259; P:positive regulation of cation channel activity; IMP:BHF-UCL.
DR GO; GO:0010650; P:positive regulation of cell communication by electrical coupling; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0034112; P:positive regulation of homotypic cell-cell adhesion; IMP:RGD.
DR GO; GO:1900827; P:positive regulation of membrane depolarization during cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0045838; P:positive regulation of membrane potential; IMP:BHF-UCL.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:RGD.
DR GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; IMP:BHF-UCL.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:BHF-UCL.
DR GO; GO:0099612; P:protein localization to axon; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0043266; P:regulation of potassium ion transport; IDA:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR CDD; cd08803; Death_ank3; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR037971; Ank3_Death.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR040745; Ankyrin_UPA.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR000906; ZU5_dom.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 7.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF13637; Ank_4; 2.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF17809; UPA_2; 1.
DR Pfam; PF00791; ZU5; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 22.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00218; ZU5; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF48403; SSF48403; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 21.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS51145; ZU5; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Lysosome; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Synapse.
FT CHAIN 1..2622
FT /note="Ankyrin-3"
FT /id="PRO_0000429632"
FT REPEAT 73..102
FT /note="ANK 1"
FT REPEAT 106..135
FT /note="ANK 2"
FT REPEAT 139..168
FT /note="ANK 3"
FT REPEAT 172..201
FT /note="ANK 4"
FT REPEAT 203..230
FT /note="ANK 5"
FT REPEAT 242..271
FT /note="ANK 6"
FT REPEAT 275..304
FT /note="ANK 7"
FT REPEAT 308..337
FT /note="ANK 8"
FT REPEAT 341..370
FT /note="ANK 9"
FT REPEAT 374..403
FT /note="ANK 10"
FT REPEAT 407..436
FT /note="ANK 11"
FT REPEAT 440..469
FT /note="ANK 12"
FT REPEAT 473..502
FT /note="ANK 13"
FT REPEAT 506..535
FT /note="ANK 14"
FT REPEAT 539..568
FT /note="ANK 15"
FT REPEAT 572..601
FT /note="ANK 16"
FT REPEAT 605..634
FT /note="ANK 17"
FT REPEAT 638..667
FT /note="ANK 18"
FT REPEAT 671..700
FT /note="ANK 19"
FT REPEAT 704..733
FT /note="ANK 20"
FT REPEAT 737..766
FT /note="ANK 21"
FT REPEAT 770..799
FT /note="ANK 22"
FT REPEAT 803..832
FT /note="ANK 23"
FT DOMAIN 992..1147
FT /note="ZU5 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 1149..1296
FT /note="ZU5 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 2336..2420
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1968..1992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2099..2147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2292..2312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2568..2622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2103..2120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2121..2137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2579..2622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12955"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 921
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G5E8K5"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G5E8K5"
FT MOD_RES 1621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G5E8K5"
FT MOD_RES 1624
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G5E8K5"
FT MOD_RES 1984
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12955"
FT MOD_RES 2544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..880
FT /note="MAHAASQLKKNRDLEINAEEETEKKKKHRKRSRDRKKKSDANASYLRAARAG
FT HLEKALDYIKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTAL
FT HIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSLAT
FT EDGFTPLAVALQQGHDQVVSLLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDTNAD
FT IESKMVVNRATESGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGN
FT ANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRAAPILSKTKNGLSPLH
FT MATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKAL
FT NGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGA
FT SPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQ
FT QLLQQGASPNAATTSGYTPLHLSAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKY
FT GKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTP
FT LHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLS
FT NKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQH
FT SAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQNNASPNELTVNGNTALAIARRLGYISV
FT VDTLKVVTEEIMTTTTITEKHKMNVPETMNEVLDMSDDEVGKASAPEKLSDGEYISDGE
FT EG -> MALPHS (in isoform 4, isoform 5, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:11796721,
FT ECO:0000303|PubMed:15953600"
FT /id="VSP_055004"
FT VAR_SEQ 1..36
FT /note="MAHAASQLKKNRDLEINAEEETEKKKKHRKRSRDRK -> MSEEAKEKTAKP
FT AHRKRKG (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15953600"
FT /id="VSP_055005"
FT VAR_SEQ 234..241
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15953600"
FT /id="VSP_055006"
FT VAR_SEQ 858..878
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15953600"
FT /id="VSP_055007"
FT VAR_SEQ 922..927
FT /note="LRSFSS -> PKISS (in isoform 2, isoform 3, isoform 4,
FT isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:11796721,
FT ECO:0000303|PubMed:15953600"
FT /id="VSP_055008"
FT VAR_SEQ 1466..2444
FT /note="KRYSYLTEPSMKTVERSSGTARSLPTTYSHKPFFSTRPYQSWTTTPITVPGP
FT AKSGSLSSSPSNTPSASPLKSIWSVSTPSPIKSTLGASTTSSVKSISDVASPIRSFRTI
FT SSPIRTVASPSPYNTQVASGTLGRVPTITEATPIKGVAPNSTLSSRTSPVTTAGSLLEK
FT SSITMTPPASPKANITMYSSSLPFKSIITSAAPLISSPLKSVVSPTKSAADVISTAKAA
FT MASTLSSPLKQMSGHAEVALVNGSVSPLKYPSSSALINGCKATATLQDKISTATNAVSS
FT VVSAAPDTVEKALSTTTAMPFSPLRSYVSAAAPSAFQSLRAPSASALYNSLGPSVGVTT
FT SSVTSSIITVPVYSVGNVLAEPALKKLPDSNSLTKSAAALLSPIKTLTTETRPQPHFNR
FT TSSPVKSSLFLASSALKPSVPSSLSSSQEILKDVAEMKEDLMRMTAILQTDVPEEKPFQ
FT TDLPREGRIDDEEPFKIVEKVKEDLVKVSEILKKDVCVESKGPPKSPKSDKGHSPEDDW
FT TEFSSEEIREARQAAASHAPSLPERVHGKANLTRVIDYLTNDIGSSSLTNLKYKFEEAK
FT KEGEERQKRILKPAMALQEHKLKMPPASMRPSTSEKELCKMADSFFGTDAILESPDDFS
FT QHDQDKSPLSDSGFETRSEKTPSAPQSAESTGPKPLFHEVPIPPVITETRTEVVHVIRS
FT YEPSTGEIPQSQPEDPVSPKPPPTFMELEPKPTALSIKEKVKAFQMKASSEEEDHSRVL
FT SKGMRVKEETHITTTTRMVYHSPPGSECASERIEETMSVHDIMKAFQSGRDPSKELAGL
FT FEHKSAMSPDVAKSAAETSAQHAEKDNQMKPKLERIIEVHIEKGPQSPCERTDIRMAIV
FT ADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTS
FT VLTKINRIDIVTLLEGPIFDYGNISGTRSFADENNVFHDPVD -> PQSPCERTDIRMA
FT IVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDAL
FT TSVLTKINRIDIVTLLEGPIFDYGNISGTRSFADENNVFHDPVDGHPSFQVELETPMGL
FT YCTPPTPFQQDDHFSDNSSIESPFRTPSRLSDGLMPSQGSIEHPAGGPPVVTAEDTSLE
FT DSKMDDSVTVTETADPLDVDESQLKDLCQSECAHCWASVPGVPSGGPQAEPLRAQTRKV
FT GVSSEQQEKGDSGPEEEMADDKVRSLFEDIQLEEVEAEEMTEDEGQAILNRVPRAELAM
FT SSLA (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15953600"
FT /id="VSP_055009"
FT VAR_SEQ 1466..2328
FT /note="Missing (in isoform 3, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:11796721,
FT ECO:0000303|PubMed:15953600"
FT /id="VSP_055010"
FT VAR_SEQ 2601
FT /note="K -> KDLRHSESDSSSEEERRVTTRVIRRRVIIKGEEAKTIPGESVTEEQF
FT TDEEGNLITRKITRKVIRRIGPQERKQDDV (in isoform 2, isoform 5 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:11796721,
FT ECO:0000303|PubMed:15953600"
FT /id="VSP_055011"
FT VAR_SEQ 2601
FT /note="K -> KQVKSPGEAFTRMTACCYKDLRHSESDSSSEEERRVTTRVIRRRVII
FT KGEEAKTIPGESVTEEQFTDEEGNLITRKITRKVIRRIGPQERKQDDV (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15953600"
FT /id="VSP_055012"
FT VAR_SEQ 2601
FT /note="K -> KVKSPGEAFTRMTACCYKDLRHSESDSSSEEERRVTTRVIRRRVIIK
FT GEEAKTIPGESVTEEQFTDEEGNLITRKITRKVIRRIGPQERKQDDV (in isoform
FT 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15953600"
FT /id="VSP_055013"
FT CONFLICT 246
FT /note="P -> S (in Ref. 1; AAC78143)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="A -> S (in Ref. 3; CAH19223/CAH19224)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="A -> P (in Ref. 1; AAC78143)"
FT /evidence="ECO:0000305"
FT STRAND 988..998
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1003..1010
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1014..1017
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1022..1024
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1026..1032
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1049..1059
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1063..1073
FT /evidence="ECO:0007829|PDB:6M3P"
FT TURN 1079..1082
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1083..1094
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1096..1098
FT /evidence="ECO:0007829|PDB:6M3P"
FT HELIX 1106..1110
FT /evidence="ECO:0007829|PDB:6M3P"
FT HELIX 1122..1128
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1130..1137
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1140..1148
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1151..1153
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1165..1169
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1171..1173
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1185..1190
FT /evidence="ECO:0007829|PDB:6M3P"
FT HELIX 1194..1199
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1210..1215
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1217..1229
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1250..1255
FT /evidence="ECO:0007829|PDB:6M3P"
FT HELIX 1269..1271
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1277..1287
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1290..1295
FT /evidence="ECO:0007829|PDB:6M3P"
FT TURN 1299..1301
FT /evidence="ECO:0007829|PDB:6M3P"
FT HELIX 1302..1313
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1317..1326
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1336..1343
FT /evidence="ECO:0007829|PDB:6M3P"
FT HELIX 1349..1353
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1357..1360
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1365..1368
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1371..1380
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1392..1394
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1401..1405
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1418..1424
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1437..1442
FT /evidence="ECO:0007829|PDB:6M3P"
FT STRAND 1989..1991
FT /evidence="ECO:0007829|PDB:5YIQ"
FT HELIX 1994..2003
FT /evidence="ECO:0007829|PDB:5YIP"
FT MOD_RES O70511-2:1679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES O70511-4:851
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES O70511-5:851
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 2622 AA; 284443 MW; A17F304D792333F5 CRC64;
MAHAASQLKK NRDLEINAEE ETEKKKKHRK RSRDRKKKSD ANASYLRAAR AGHLEKALDY
IKNGVDVNIC NQNGLNALHL ASKEGHVEVV SELLQREANV DAATKKGNTA LHIASLAGQA
EVVKVLVTNG ANVNAQSQNG FTPLYMAAQE NHLEVVRFLL DNGASQSLAT EDGFTPLAVA
LQQGHDQVVS LLLENDTKGK VRLPALHIAA RKDDTKAAAL LLQNDTNADI ESKMVVNRAT
ESGFTPLHIA AHYGNINVAT LLLNRAAAVD FTARNDITPL HVASKRGNAN MVKLLLDRGA
KIDAKTRDGL TPLHCGARSG HEQVVEMLLD RAAPILSKTK NGLSPLHMAT QGDHLNCVQL
LLQHNVPVDD VTNDYLTALH VAAHCGHYKV AKVLLDKKAN PNAKALNGFT PLHIACKKNR
IRVMELLLKH GASIQAVTES GLTPIHVAAF MGHVNIVSQL MHHGASPNTT NVRGETALHM
AARSGQAEVV RYLVQDGAQV EAKAKDDQTP LHISARLGKA DIVQQLLQQG ASPNAATTSG
YTPLHLSARE GHEDVAAFLL DHGASLSITT KKGFTPLHVA AKYGKLEVAS LLLQKSASPD
AAGKSGLTPL HVAAHYDNQK VALLLLDQGA SPHAAAKNGY TPLHIAAKKN QMDIATSLLE
YGADANAVTR QGIASVHLAA QEGHVDMVSL LLSRNANVNL SNKSGLTPLH LAAQEDRVNV
AEVLVNQGAH VDAQTKMGYT PLHVGCHYGN IKIVNFLLQH SAKVNAKTKN GYTPLHQAAQ
QGHTHIINVL LQNNASPNEL TVNGNTALAI ARRLGYISVV DTLKVVTEEI MTTTTITEKH
KMNVPETMNE VLDMSDDEVG KASAPEKLSD GEYISDGEEG EDAITGDTDK YLGPQDLKEL
GDDSLPAEGY VGFSLGARSA SLRSFSSDRS YTLNRSSYAR DSMMIEELLV PSKEQHLPFT
REFDSDSLRH YSWAADTLDN VNLVSSPVHS GFLVSFMVDA RGGSMRGSRH HGMRIIIPPR
KCTAPTRITC RLVKRHKLAN PPPMVEGEGL ASRLVEMGPA GAQFLGPVIV EIPHFGSMRG
KERELIVLRS ENGETWKEHQ FDSKNEDLSE LLNGMDEELD SPEELGTKRI CRIITKDFPQ
YFAVVSRIKQ ESNQIGPEGG ILSSTTVPLV QASFPEGALT KRIRVGLQAQ PVPEETVKKI
LGNKATFSPI VTVEPRRRKF HKPITMTIPV PPPSGEGVSN GYKGDTTPSL RLLCSITGGT
SPAQWEDITG TTPLTFIKDC VSFTTNVSAR FWLADCHQVL ETVGLASQLY RELICVPYMA
KFVVFAKTND PVESSLRCFC MTDDRVDKTL EQQENFEEVA RSKDIEVLEG KPIYVDCYGN
LAPLTKGGQQ LVFNFYSFKE NRLPFSIKVR DTSQEPCGRL SFLKEPKTTK GLPQTAVCNL
NITLPAHKKA EKADRRQSFT SLALRKRYSY LTEPSMKTVE RSSGTARSLP TTYSHKPFFS
TRPYQSWTTT PITVPGPAKS GSLSSSPSNT PSASPLKSIW SVSTPSPIKS TLGASTTSSV
KSISDVASPI RSFRTISSPI RTVASPSPYN TQVASGTLGR VPTITEATPI KGVAPNSTLS
SRTSPVTTAG SLLEKSSITM TPPASPKANI TMYSSSLPFK SIITSAAPLI SSPLKSVVSP
TKSAADVIST AKAAMASTLS SPLKQMSGHA EVALVNGSVS PLKYPSSSAL INGCKATATL
QDKISTATNA VSSVVSAAPD TVEKALSTTT AMPFSPLRSY VSAAAPSAFQ SLRAPSASAL
YNSLGPSVGV TTSSVTSSII TVPVYSVGNV LAEPALKKLP DSNSLTKSAA ALLSPIKTLT
TETRPQPHFN RTSSPVKSSL FLASSALKPS VPSSLSSSQE ILKDVAEMKE DLMRMTAILQ
TDVPEEKPFQ TDLPREGRID DEEPFKIVEK VKEDLVKVSE ILKKDVCVES KGPPKSPKSD
KGHSPEDDWT EFSSEEIREA RQAAASHAPS LPERVHGKAN LTRVIDYLTN DIGSSSLTNL
KYKFEEAKKE GEERQKRILK PAMALQEHKL KMPPASMRPS TSEKELCKMA DSFFGTDAIL
ESPDDFSQHD QDKSPLSDSG FETRSEKTPS APQSAESTGP KPLFHEVPIP PVITETRTEV
VHVIRSYEPS TGEIPQSQPE DPVSPKPPPT FMELEPKPTA LSIKEKVKAF QMKASSEEED
HSRVLSKGMR VKEETHITTT TRMVYHSPPG SECASERIEE TMSVHDIMKA FQSGRDPSKE
LAGLFEHKSA MSPDVAKSAA ETSAQHAEKD NQMKPKLERI IEVHIEKGPQ SPCERTDIRM
AIVADHLGLS WTELARELNF SVDEINQIRV ENPNSLISQS FMLLKKWVTR DGKNATTDAL
TSVLTKINRI DIVTLLEGPI FDYGNISGTR SFADENNVFH DPVDGWQNET PSGSLESPAQ
ARRITGGLLD RLDDSSDQVR DPITSYLTGE AGKFEANGNH AEVIPEAKAK AYFPESQNDI
GKQSIKENLK PKTHGCGRAE EPVSPLTAYQ KSLEETSKLV IEDAPKPCVP VGMKKMTRTP
ADGKARLNLQ EEEGSARSEP KQGEGYKVKT KKEIRNVEKK AH
