SPTCA_DROME
ID SPTCA_DROME Reviewed; 2415 AA.
AC P13395; Q26340; Q3KN50; Q8SZW7; Q9W085;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Spectrin alpha chain;
GN Name=alpha-Spec; Synonyms=SPEC-A; ORFNames=CG1977;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2808524; DOI=10.1083/jcb.109.5.2197;
RA Dubreuil R.R., Byers T.J., Sillman A.L., Bar-Zvi D., Goldstein L.S.B.,
RA Branton D.;
RT "The complete sequence of Drosophila alpha-spectrin: conservation of
RT structural domains between alpha-spectrins and alpha-actinin.";
RL J. Cell Biol. 109:2197-2205(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150 AND 2192-2415, AND FUNCTION.
RX PubMed=8276898; DOI=10.1083/jcb.123.6.1797;
RA Lee J.K., Coyne R.S., Dubreuil R.R., Goldstein L.S.B., Branton D.;
RT "Cell shape and interaction defects in alpha-spectrin mutants of Drosophila
RT melanogaster.";
RL J. Cell Biol. 123:1797-1809(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1539-2415.
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP FUNCTION.
RX PubMed=3680372; DOI=10.1083/jcb.105.5.2095;
RA Dubreuil R., Byers T.J., Branton D., Goldstein L.S.B., Kiehart D.P.;
RT "Drosophilia spectrin. I. Characterization of the purified protein.";
RL J. Cell Biol. 105:2095-2102(1987).
RN [8]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11076973; DOI=10.1083/jcb.151.4.905;
RA Sisson J.C., Field C., Ventura R., Royou A., Sullivan W.;
RT "Lava lamp, a novel peripheral Golgi protein, is required for Drosophila
RT melanogaster cellularization.";
RL J. Cell Biol. 151:905-918(2000).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=2497103; DOI=10.1083/jcb.108.5.1697;
RA Pesacreta T.C., Byers T.J., Dubreuil R., Kiehart D.P., Branton D.;
RT "Drosophila spectrin: the membrane skeleton during embryogenesis.";
RL J. Cell Biol. 108:1697-1709(1989).
RN [10]
RP GENE STRUCTURE.
RX PubMed=14667407; DOI=10.1016/s1534-5807(03)00358-7;
RA Pielage J., Stork T., Bunse I., Klaembt C.;
RT "The Drosophila cell survival gene discs lost encodes a cytoplasmic
RT Codanin-1-like protein, not a homolog of tight junction PDZ protein Patj.";
RL Dev. Cell 5:841-851(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1032 AND SER-1034, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [13]
RP INTERACTION WITH TEN-M.
RX PubMed=22426000; DOI=10.1038/nature10923;
RA Mosca T.J., Hong W., Dani V.S., Favaloro V., Luo L.;
RT "Trans-synaptic Teneurin signalling in neuromuscular synapse organization
RT and target choice.";
RL Nature 484:237-241(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1391-1497.
RX PubMed=8266097; DOI=10.1126/science.8266097;
RA Yan Y., Winograd E., Viel A., Cronin T., Harrison S.C., Branton D.;
RT "Crystal structure of the repetitive segments of spectrin.";
RL Science 262:2027-2030(1993).
CC -!- FUNCTION: Spectrin is the major constituent of the cytoskeletal network
CC underlying the erythrocyte plasma membrane. It associates with band 4.1
CC and actin to form the cytoskeletal superstructure of the erythrocyte
CC plasma membrane. Essential for larval survival and development.
CC Stabilizes cell to cell interactions that are critical for the
CC maintenance of cell shape and subcellular organization within embryonic
CC tissues. Lva and spectrin may form a Golgi-based scaffold that mediates
CC interaction of Golgi bodies with microtubules and facilitates Golgi-
CC derived membrane secretion required for the formation of furrows during
CC cellularization. {ECO:0000269|PubMed:11076973,
CC ECO:0000269|PubMed:3680372, ECO:0000269|PubMed:8276898}.
CC -!- SUBUNIT: Native spectrin molecule is a tetramer composed of two
CC antiparallel heterodimers joined head to head so that each end of the
CC native molecule includes the C-terminus of the alpha subunit and the N-
CC terminus of the beta subunit. Interacts with calmodulin in a calcium-
CC dependent manner, interacts with F-actin and also interacts with Lva.
CC Interacts with Ten-m. {ECO:0000269|PubMed:11076973,
CC ECO:0000269|PubMed:22426000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11076973}. Golgi apparatus
CC {ECO:0000269|PubMed:11076973}. Note=Near the inner surface of the
CC plasma membrane of nearly all cells. Lva-alpha-spectrin complexes are
CC found at the Golgi.
CC -!- TISSUE SPECIFICITY: A substantial pool of maternal protein in the egg
CC undergoes dynamic changes in distribution early in embryogenesis. In
CC gastrulated embryo, the highest level of protein is found in the
CC respiratory tract cells and the lowest in parts of the forming gut.
CC {ECO:0000269|PubMed:2497103}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC -!- MISCELLANEOUS: Its transcript shares the first untranslated exon with
CC the dlt transcript, suggesting a common regulation.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39886.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABA81823.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M26400; AAA28907.1; -; mRNA.
DR EMBL; AE014296; AAF47569.1; -; Genomic_DNA.
DR EMBL; BT023889; ABA81823.1; ALT_FRAME; mRNA.
DR EMBL; S67762; AAB29441.2; -; Genomic_DNA.
DR EMBL; S67765; AAB29442.1; -; Genomic_DNA.
DR EMBL; AY069741; AAL39886.1; ALT_INIT; mRNA.
DR PIR; A33733; A33733.
DR RefSeq; NP_476739.1; NM_057391.4.
DR PDB; 2SPC; X-ray; 1.80 A; A/B=1391-1497.
DR PDBsum; 2SPC; -.
DR AlphaFoldDB; P13395; -.
DR SMR; P13395; -.
DR BioGRID; 63763; 46.
DR DIP; DIP-17516N; -.
DR IntAct; P13395; 2.
DR STRING; 7227.FBpp0305100; -.
DR iPTMnet; P13395; -.
DR PaxDb; P13395; -.
DR PRIDE; P13395; -.
DR EnsemblMetazoa; FBtr0072789; FBpp0072672; FBgn0250789.
DR GeneID; 38231; -.
DR KEGG; dme:Dmel_CG1977; -.
DR CTD; 38231; -.
DR FlyBase; FBgn0250789; alpha-Spec.
DR VEuPathDB; VectorBase:FBgn0250789; -.
DR eggNOG; KOG0040; Eukaryota.
DR GeneTree; ENSGT00940000156662; -.
DR HOGENOM; CLU_000847_0_0_1; -.
DR InParanoid; P13395; -.
DR OMA; QQFNRTV; -.
DR PhylomeDB; P13395; -.
DR Reactome; R-DME-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-DME-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-DME-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DME-9013420; RHOU GTPase cycle.
DR Reactome; R-DME-9013424; RHOV GTPase cycle.
DR SignaLink; P13395; -.
DR BioGRID-ORCS; 38231; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; P13395; -.
DR GenomeRNAi; 38231; -.
DR PRO; PR:P13395; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0250789; Expressed in eye disc (Drosophila) and 47 other tissues.
DR ExpressionAtlas; P13395; baseline and differential.
DR Genevisible; P13395; DM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0045169; C:fusome; IDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0045170; C:spectrosome; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IDA:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0016199; P:axon midline choice point recognition; IGI:FlyBase.
DR GO; GO:0007417; P:central nervous system development; IMP:FlyBase.
DR GO; GO:0045478; P:fusome organization; TAS:FlyBase.
DR GO; GO:0030727; P:germarium-derived female germ-line cyst formation; IMP:FlyBase.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
DR GO; GO:0042062; P:long-term strengthening of neuromuscular junction; IMP:FlyBase.
DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; IDA:FlyBase.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:FlyBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0007308; P:oocyte construction; IMP:FlyBase.
DR GO; GO:0007009; P:plasma membrane organization; TAS:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0050807; P:regulation of synapse organization; IMP:FlyBase.
DR CDD; cd00051; EFh; 1.
DR CDD; cd11808; SH3_Alpha_Spectrin; 1.
DR CDD; cd00176; SPEC; 13.
DR InterPro; IPR035825; Alpha_Spectrin_SH3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 20.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 20.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin capping; Actin-binding; Calcium; Calmodulin-binding;
KW Cell shape; Cytoplasm; Cytoskeleton; Golgi apparatus; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..2415
FT /note="Spectrin alpha chain"
FT /id="PRO_0000073467"
FT REPEAT 48..150
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 154..254
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 258..362
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 366..464
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 471..574
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 577..679
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 683..784
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 788..890
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 894..963
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT DOMAIN 970..1029
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1079..1177
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1181..1284
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1287..1391
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1394..1496
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
FT REPEAT 1500..1604
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT REPEAT 1608..1710
FT /note="Spectrin 15"
FT /evidence="ECO:0000255"
FT REPEAT 1714..1816
FT /note="Spectrin 16"
FT /evidence="ECO:0000255"
FT REPEAT 1820..1921
FT /note="Spectrin 17"
FT /evidence="ECO:0000255"
FT REPEAT 1926..2028
FT /note="Spectrin 18"
FT /evidence="ECO:0000255"
FT REPEAT 2040..2141
FT /note="Spectrin 19"
FT /evidence="ECO:0000255"
FT REPEAT 2154..2252
FT /note="Spectrin 20"
FT /evidence="ECO:0000255"
FT DOMAIN 2265..2300
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 2308..2343
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 2332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 1032
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT CONFLICT 110
FT /note="Q -> D (in Ref. 5; AAB29441)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="N -> I (in Ref. 4; ABA81823)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="D -> G (in Ref. 4; ABA81823)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="Q -> L (in Ref. 4; ABA81823)"
FT /evidence="ECO:0000305"
FT CONFLICT 1555
FT /note="Q -> H (in Ref. 6; AAL39886)"
FT /evidence="ECO:0000305"
FT CONFLICT 1562
FT /note="G -> E (in Ref. 4; ABA81823)"
FT /evidence="ECO:0000305"
FT CONFLICT 1668
FT /note="Q -> R (in Ref. 1; AAA28907)"
FT /evidence="ECO:0000305"
FT CONFLICT 1908
FT /note="N -> S (in Ref. 4; ABA81823)"
FT /evidence="ECO:0000305"
FT CONFLICT 2203
FT /note="D -> G (in Ref. 4; ABA81823)"
FT /evidence="ECO:0000305"
FT HELIX 1393..1422
FT /evidence="ECO:0007829|PDB:2SPC"
FT HELIX 1428..1494
FT /evidence="ECO:0007829|PDB:2SPC"
SQ SEQUENCE 2415 AA; 278303 MW; F1F72FB990EB0A37 CRC64;
MENFTPKEVK ILETVEDIQE RREQVLSRYN DFKIETRQKR EKLEDSRRFQ YFKRDADELE
SWIHEKLQAA SEESYRDPTN LQAKIQKHQA FEAEVSAHSN AIVSLDNTGQ EMINQQHFAS
ESIQVRLDEL HKLWELLLSR LAEKGLKLQQ ALVLVQFLRQ CEEVMFWIKD KETFVTADEF
GQDLEHVEVL QRKFDEFQKD MASQEYRVTE VNQLADKLVQ DGHPERDTIT KRKEELNEAW
QRLKQLAIVR QEKLFGAHEI QRFNRDADET VAWIAEKDVV LSSDDYGRDL ASVQALQRKH
EGVERDLAAL EDKVSTLGAE AQRLCSIHAD HSDQIRDKQA EIANYWQSLT TKARERKQKL
DESYYLHRFL ADFRDLVSWI NGMKAIISAD ELAKDVAGAE ALLERHQEHK GEIDAREDSF
KLTTESGQKL LEREHYAAAE IQEKLAALEN DKSSLLSLWE DRRILYEQCM DLQLFYRDTE
QADTWMAKQE AFLANEDLGD SLDSVEALIK KHEDFEKSLA AQEEKIKALD IFATKLIDGQ
HYAADDVAQR RQMLLARRAA LQEKSSKRRQ LLEDSNRYQQ FERDCDETKG WISEKLKFAT
DDSYLDPTNL NGKMQKHQNF EHELNANKSR IEDITNVGTE LIEKQHYAAD QINTRMQEIV
VLWETLVQAS DKKGTKLNEA CQQQQFNRTI EDIELWLSEI EGQLLSEDHG KDLTSVQNLQ
KKHALLEADV MAHQDRIESI KVAANKFIES GHFDADNIRN KEGNLSARYA ALAAPMGERK
QHLLDSLQVQ QLFRDLEDEA AWIREKEPIA ASTNRGRDLI GVQNLIKKHQ AVLAEINNHE
ARLLNVISSG ENMLKDQPFA SDDIRQRLEA LQEQWNTLKE KSSQRKQDLD DSLQAHQYFA
DANEAESWMR EKEPIATGSD YGKDEDSSEA LLKKHEALVS DLEAFGNTIQ ALQEQAKNCR
QQETPVVDIT GKECVVALYD YTEKSPREVS MKKGDVLTLL NSNNKDWWKV EVNDRQGFVP
AAYIKKIDAG LSASQQNLVD NHSIAKRQNQ INSQYDNLLA LARERQNKLN ETVKAYVLVR
EAADLAQWIR DKENHAQIAD VVGEDLEEVE VLQKKFDDFN DDLKANEVRL ANMNEIAVQL
TSLGQTEAAL KIQTQMQDLN EKWNNLQTLT AEKASQLGSA HEVQRFHRDI DETKDWIAEK
ANALNNDDLG KDLRSVQTLQ RKHEGVERDL AALRDKIRQL DETANRLMQS HPDTAEQTYA
KQKEINEMWD QIITKSTARK EKLLDSYDLQ RFLSDYRDLL AWINSMMSLV TSDELANDVT
GAEALIERHQ EHRTEIDARA GTFGAFEQFG NELLQANHYA SPEIKEKIED LAKAREDLEK
AWTERRLQLE QNLDLQLYMR DCELAESWMS AREAFLNADD DANAGGNVEA LIKKHEDFDK
AINGHEQKIA ALQTVADQLI AQNHYASNLV DEKRKQVLER WRHLKEGLIE KRSRLGDEQT
LQQFSRDADE IENWIAEKLQ LATEESYKDP ANIQSKHQKH QAFEAELAAN ADRIQSVLAM
GGNLIDKKQC SGSEDAVQKR LTQIADQWEY LTHKTTEKSL KLKEANKQRT YIAAVKDLDF
WLGEVESLLT TEDSGKDLAS VQNLMKKHQL VEADIVAHED RIKDMNNQAD SLVESGQFDT
AGIQEKRQSI NERYERICNL AAHRQARLNE ALTLHQFFRD IADEESWIKE KKLLVGSDDY
GRDLTGVQNL KKKHKRLEAE LGSHEPAIQA VQEAGEKLMD VSNLGVPEIE QRLKALNQAW
AELKNLAATR GQKLDESLTY QQFLAQVEEE EAWITEKQQL LSVEDYGDSM AAVQGLLKKH
DAFETDFTAH KDRCSLICDQ GSELVEAKNH HGESIAQRCQ QLRLKLDNLS ALAARRKGAL
LDNSAYLQFM WKADVVESWI DDKENYVRSD EFGRDLSTVQ TLLTKQETFD AGLNAFEQEG
IHNITALKDQ LINASHAQSP AILKRHGDVI ARWQKLRDAS NTRKDRLLAM QEQFRQIEEL
YLTFAKKASA FNSWFENAEE DLTDPVRCNS IEEIRALRDA HAQFQASLSS AEADFKALAA
LDQKIKSFNV GPNPYTWFTM EALEETWRNL QKIIEERDGE LAKEAKRQEE NDKLRKEFAK
HANLFHQWLT ETRTSMMEGS GSLEQQLEAL RVKATEVRAR RVDLKKIEEL GALLEEHLIL
DNRYTEHSTV GLAQQWDQLD QLSMRMQHNL EQQIQARNHS GVSEDSLKEF SMMFKHFDKD
KSGKLNHQEF KSCLRALGYD LPMVEEGQPD PEFEAILDVV DPNRDGYVSL QEYIAFMISK
ETENVQSYEE IENAFRAITA ADRPYVTKEE LYCNLTKDMA DYCVQRMKPF SEPRSGQPIK
DALDYIDFTR TLFQN
