SY65_DROME
ID SY65_DROME Reviewed; 474 AA.
AC P21521; A4V023; M9PB17; M9PE99; Q7KU16; Q86NN2; Q8MRR8; Q9VQG7; Q9VQG8;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Synaptotagmin 1;
DE AltName: Full=p65;
GN Name=Syt1; Synonyms=syt; ORFNames=CG3139;
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] (ISOFORM A), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1840599; DOI=10.1016/s0021-9258(18)52479-0;
RA Perin M.S., Johnston P.A., Oezcelik T., Jahn R., Francke U., Suedhof T.C.;
RT "Structural and functional conservation of synaptotagmin (p65) in
RT Drosophila and humans.";
RL J. Biol. Chem. 266:615-622(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING OF POSITION
RP 383 AND 405.
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM B), AND RNA EDITING OF
RP POSITION 367.
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-380 (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
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 [6]
RP INTERACTION WITH STNA AND STNB.
RX PubMed=11069931; DOI=10.1523/jneurosci.20-22-08254.2000;
RA Phillips A.M., Smith M., Ramaswami M., Kelly L.E.;
RT "The products of the Drosophila stoned locus interact with synaptic
RT vesicles via synaptotagmin.";
RL J. Neurosci. 20:8254-8261(2000).
RN [7]
RP RNA EDITING OF POSITIONS 367; 379; 383 AND 405.
RX PubMed=12907802; DOI=10.1126/science.1086763;
RA Hoopengardner B., Bhalla T., Staber C., Reenan R.;
RT "Nervous system targets of RNA editing identified by comparative
RT genomics.";
RL Science 301:832-836(2003).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH NWK AND SYN.
RX PubMed=29568072; DOI=10.1038/emm.2017.303;
RA Hur J.H., Lee S.H., Kim A.Y., Koh Y.H.;
RT "Regulation of synaptic architecture and synaptic vesicle pools by Nervous
RT wreck at Drosophila Type 1b glutamatergic synapses.";
RL Exp. Mol. Med. 50:E462-E462(2018).
CC -!- FUNCTION: May have a regulatory role in the membrane interactions
CC during trafficking of synaptic vesicles at the active zone of the
CC synapse. It binds acidic phospholipids with a specificity that requires
CC the presence of both an acidic head group and a diacyl backbone.
CC {ECO:0000269|PubMed:1840599}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
CC domains. {ECO:0000250};
CC -!- SUBUNIT: Homodimer or homotrimer (Potential). Identified in a complex
CC with Syn and nwk (PubMed:29568072). Interacts with StnA and StnB via
CC its second C2 domain. This interaction may mediate its retrieval from
CC the plasma membrane, thereby facilitating the internalization of
CC multiple synaptic vesicles from the plasma membrane.
CC {ECO:0000269|PubMed:11069931, ECO:0000269|PubMed:29568072,
CC ECO:0000305}.
CC -!- INTERACTION:
CC P21521; Q24211: stnA; NbExp=2; IntAct=EBI-484504, EBI-604915;
CC P21521; Q24212: stnB; NbExp=5; IntAct=EBI-484504, EBI-604879;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:1840599}; Single-pass membrane
CC protein {ECO:0000269|PubMed:1840599}. Synapse
CC {ECO:0000269|PubMed:1840599}. Note=Synaptic vesicles in neurons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=A;
CC IsoId=P21521-1; Sequence=Displayed;
CC Name=B; Synonyms=C, I;
CC IsoId=P21521-2; Sequence=VSP_011862;
CC Name=E;
CC IsoId=P21521-4; Sequence=VSP_054631;
CC Name=G;
CC IsoId=P21521-5; Sequence=VSP_054630, VSP_054632;
CC Name=F;
CC IsoId=P21521-6; Sequence=VSP_054628, VSP_054629;
CC -!- RNA EDITING: Modified_positions=367 {ECO:0000269|PubMed:12907802,
CC ECO:0000269|Ref.4}, 379 {ECO:0000269|PubMed:12907802}, 383
CC {ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:12907802}, 405
CC {ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:12907802};
CC Note=Partially edited.;
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM50109.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAM50109.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M55048; AAA28925.1; -; mRNA.
DR EMBL; AE014134; AAF51205.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51206.2; -; Genomic_DNA.
DR EMBL; AE014134; AAS64625.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10415.1; -; Genomic_DNA.
DR EMBL; AE014134; AGB92502.1; -; Genomic_DNA.
DR EMBL; AE014134; AGB92503.1; -; Genomic_DNA.
DR EMBL; BT004498; AAO42662.1; -; mRNA.
DR EMBL; AY119455; AAM50109.1; ALT_SEQ; mRNA.
DR PIR; B39052; BMFFSY.
DR RefSeq; NP_001259965.1; NM_001273036.1. [P21521-6]
DR RefSeq; NP_001259966.1; NM_001273037.1.
DR RefSeq; NP_001285568.1; NM_001298639.1. [P21521-2]
DR RefSeq; NP_523460.2; NM_078736.3. [P21521-1]
DR RefSeq; NP_722838.1; NM_164501.2. [P21521-2]
DR RefSeq; NP_722839.1; NM_164502.2. [P21521-2]
DR RefSeq; NP_995619.2; NM_205897.2. [P21521-4]
DR AlphaFoldDB; P21521; -.
DR SMR; P21521; -.
DR BioGRID; 59696; 17.
DR IntAct; P21521; 3.
DR STRING; 7227.FBpp0077410; -.
DR PaxDb; P21521; -.
DR PRIDE; P21521; -.
DR EnsemblMetazoa; FBtr0077726; FBpp0077410; FBgn0004242. [P21521-1]
DR EnsemblMetazoa; FBtr0077727; FBpp0077411; FBgn0004242. [P21521-2]
DR EnsemblMetazoa; FBtr0077728; FBpp0077412; FBgn0004242. [P21521-2]
DR EnsemblMetazoa; FBtr0332218; FBpp0304523; FBgn0004242. [P21521-4]
DR EnsemblMetazoa; FBtr0332219; FBpp0304524; FBgn0004242. [P21521-6]
DR EnsemblMetazoa; FBtr0332220; FBpp0304525; FBgn0004242. [P21521-5]
DR EnsemblMetazoa; FBtr0345331; FBpp0311487; FBgn0004242. [P21521-2]
DR GeneID; 33473; -.
DR KEGG; dme:Dmel_CG3139; -.
DR UCSC; CG3139-RC; d. melanogaster.
DR CTD; 6857; -.
DR FlyBase; FBgn0004242; Syt1.
DR VEuPathDB; VectorBase:FBgn0004242; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000168041; -.
DR InParanoid; P21521; -.
DR OMA; PMATMEN; -.
DR PhylomeDB; P21521; -.
DR Reactome; R-DME-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-DME-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-DME-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-DME-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-DME-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DME-888590; GABA synthesis, release, reuptake and degradation.
DR BioGRID-ORCS; 33473; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33473; -.
DR PRO; PR:P21521; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004242; Expressed in brain and 22 other tissues.
DR ExpressionAtlas; P21521; baseline and differential.
DR Genevisible; P21521; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0031045; C:dense core granule; IBA:GO_Central.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; NAS:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IDA:FlyBase.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:FlyBase.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:FlyBase.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0000149; F:SNARE binding; IPI:FlyBase.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IMP:FlyBase.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IDA:FlyBase.
DR GO; GO:0150007; P:clathrin-dependent synaptic vesicle endocytosis; IDA:FlyBase.
DR GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:FlyBase.
DR GO; GO:0031340; P:positive regulation of vesicle fusion; IDA:FlyBase.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR GO; GO:1900073; P:regulation of neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IMP:FlyBase.
DR GO; GO:0060024; P:rhythmic synaptic transmission; IDA:FlyBase.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:FlyBase.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISS:FlyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:FlyBase.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR015428; Synaptotagmin1.
DR PANTHER; PTHR10024:SF239; PTHR10024:SF239; 1.
DR Pfam; PF00168; C2; 2.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cytoplasmic vesicle; Membrane;
KW Metal-binding; Reference proteome; Repeat; RNA editing; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..474
FT /note="Synaptotagmin 1"
FT /id="PRO_0000183986"
FT TOPO_DOM 1..107
FT /note="Vesicular"
FT TRANSMEM 108..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..474
FT /note="Cytoplasmic"
FT DOMAIN 192..312
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 325..458
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..434
FT /note="Phospholipid binding"
FT /evidence="ECO:0000305"
FT COMPBIAS 28..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT VAR_SEQ 168..169
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_011862"
FT VAR_SEQ 169..170
FT /note="QP -> SV (in isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_054628"
FT VAR_SEQ 171..474
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_054629"
FT VAR_SEQ 324..331
FT /note="EKLGDICF -> VVLREVNI (in isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_054630"
FT VAR_SEQ 324..325
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_054631"
FT VAR_SEQ 332..474
FT /note="Missing (in isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_054632"
FT VARIANT 367
FT /note="I -> V (in RNA edited version)"
FT VARIANT 379
FT /note="K -> R (in RNA edited version)"
FT VARIANT 383
FT /note="I -> V (in RNA edited version)"
FT VARIANT 405
FT /note="I -> M (in RNA edited version)"
FT CONFLICT 26
FT /note="D -> E (in Ref. 1; AAA28925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 53260 MW; 76F3A34EEABE875B CRC64;
MPPNAKSETD AKPEAEPAPA SEPAADLESV DQKLEETHHS KFREVDRQEQ EVLAEKAAEA
ASQRIAQVES TTRSATTEAQ ESTTTAVPVI KKIEHVGEVV TEVIAERTGL PTWGVVAIII
LVFLVVFGII FFCVRRFLKK RRTKDGKGKK GVDMKSVQLL GSAYKEKVQP DMEELTENAE
EGDEEDKQSE QKLGRLNFKL EYDFNSNSLA VTVIQAEELP ALDMGGTSDP YVKVYLLPDK
KKKFETKVHR KTLSPVFNET FTFKSLPYAD AMNKTLVFAI FDFDRFSKHD QIGEVKVPLC
TIDLAQTIEE WRDLVSVEGE GGQEKLGDIC FSLRYVPTAG KLTVVILEAK NLKKMDVGGL
SDPYVKIAIM QNGKRLKKKK TSIKKCTLNP YYNESFSFEV PFEQIQKICL VVTVVDYDRI
GTSEPIGRCI LGCMGTGTEL RHWSDMLASP RRPIAQWHTL KDPEETDEIL KNMK
