ATC1_DROME
ID ATC1_DROME Reviewed; 1020 AA.
AC P22700; A4UZU0; Q2MGN2; Q95TX1; Q9W1G2; Q9W1G3;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type;
DE EC=7.2.2.10;
DE AltName: Full=Calcium ATPase at 60A;
DE AltName: Full=Calcium pump;
DE AltName: Full=Sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase {ECO:0000312|FlyBase:FBgn0263006};
GN Name=SERCA {ECO:0000312|FlyBase:FBgn0263006};
GN Synonyms=Ca-P60A {ECO:0000312|FlyBase:FBgn0263006};
GN ORFNames=CG3725 {ECO:0000312|FlyBase:FBgn0263006};
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).
RX PubMed=2148477; DOI=10.1016/s0006-291x(05)80867-8;
RA Magyar A., Varadi A.;
RT "Molecular cloning and chromosomal localization of a sarco/endoplasmic
RT reticulum-type Ca2(+)-ATPase of Drosophila melanogaster.";
RL Biochem. Biophys. Res. Commun. 173:872-877(1990).
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, 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).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 357-513.
RX PubMed=2557235; DOI=10.1016/0014-5793(89)81653-9;
RA Varadi A., Gilmore-Heber M., Benz E.J. Jr.;
RT "Amplification of the phosphorylation site-ATP-binding site cDNA fragment
RT of the Na+,K(+)-ATPase and the Ca2(+)-ATPase of Drosophila melanogaster by
RT polymerase chain reaction.";
RL FEBS Lett. 258:203-207(1989).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND IDENTIFICATION BY
RP 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 [7]
RP INTERACTION WITH SCLA AND SCLB, AND SUBCELLULAR LOCATION.
RX PubMed=23970561; DOI=10.1126/science.1238802;
RA Magny E.G., Pueyo J.I., Pearl F.M., Cespedes M.A., Niven J.E., Bishop S.A.,
RA Couso J.P.;
RT "Conserved regulation of cardiac calcium uptake by peptides encoded in
RT small open reading frames.";
RL Science 341:1116-1120(2013).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of calcium.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC -!- SUBUNIT: Interacts with SclA and SclB. {ECO:0000269|PubMed:23970561}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23970561}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23970561}. Sarcoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23970561}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23970561}. Note=Colocalizes with SclA and SclB at
CC the sarcoplasmic reticulum and the diad, a structure composed of a
CC single t-tubule paired with a terminal cisterna of the sarcoplasmic
CC reticulum. {ECO:0000269|PubMed:23970561}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=C, D, E, F, G, H;
CC IsoId=P22700-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P22700-2; Sequence=VSP_010297;
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000305}.
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DR EMBL; M62892; AAB00735.1; -; mRNA.
DR EMBL; AE013599; AAF47101.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF47102.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF47103.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68278.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68279.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68280.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68281.1; -; Genomic_DNA.
DR EMBL; AY058465; AAL13694.1; -; mRNA.
DR EMBL; X17472; CAA35505.1; -; mRNA.
DR PIR; A36691; A36691.
DR RefSeq; NP_476832.1; NM_057484.3. [P22700-2]
DR RefSeq; NP_726381.1; NM_166633.2. [P22700-1]
DR RefSeq; NP_726382.1; NM_166634.2. [P22700-1]
DR RefSeq; NP_726383.1; NM_166635.2. [P22700-1]
DR RefSeq; NP_726384.1; NM_166636.2. [P22700-1]
DR RefSeq; NP_726385.1; NM_166637.2. [P22700-1]
DR RefSeq; NP_726386.1; NM_166638.2. [P22700-1]
DR RefSeq; NP_726387.1; NM_166639.2. [P22700-1]
DR AlphaFoldDB; P22700; -.
DR SMR; P22700; -.
DR BioGRID; 72161; 128.
DR DIP; DIP-20129N; -.
DR IntAct; P22700; 6.
DR STRING; 7227.FBpp0072125; -.
DR iPTMnet; P22700; -.
DR PaxDb; P22700; -.
DR PRIDE; P22700; -.
DR DNASU; 49297; -.
DR EnsemblMetazoa; FBtr0072211; FBpp0072120; FBgn0263006. [P22700-1]
DR EnsemblMetazoa; FBtr0072212; FBpp0072121; FBgn0263006. [P22700-1]
DR EnsemblMetazoa; FBtr0072213; FBpp0072122; FBgn0263006. [P22700-1]
DR EnsemblMetazoa; FBtr0072214; FBpp0072123; FBgn0263006. [P22700-1]
DR EnsemblMetazoa; FBtr0072215; FBpp0072124; FBgn0263006. [P22700-2]
DR EnsemblMetazoa; FBtr0072216; FBpp0072125; FBgn0263006. [P22700-1]
DR EnsemblMetazoa; FBtr0072217; FBpp0072126; FBgn0263006. [P22700-1]
DR EnsemblMetazoa; FBtr0072218; FBpp0072127; FBgn0263006. [P22700-1]
DR GeneID; 49297; -.
DR KEGG; dme:Dmel_CG3725; -.
DR CTD; 49297; -.
DR FlyBase; FBgn0263006; SERCA.
DR VEuPathDB; VectorBase:FBgn0263006; -.
DR eggNOG; KOG0202; Eukaryota.
DR GeneTree; ENSGT00940000155668; -.
DR InParanoid; P22700; -.
DR PhylomeDB; P22700; -.
DR Reactome; R-DME-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-DME-5578775; Ion homeostasis.
DR Reactome; R-DME-936837; Ion transport by P-type ATPases.
DR SignaLink; P22700; -.
DR BioGRID-ORCS; 49297; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 49297; -.
DR PRO; PR:P22700; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0263006; Expressed in thoracico-abdominal ganglion (Drosophila) and 50 other tissues.
DR ExpressionAtlas; P22700; baseline and differential.
DR Genevisible; P22700; DM.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IMP:FlyBase.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:1990845; P:adaptive thermogenesis; IMP:FlyBase.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:1903515; P:calcium ion transport from cytosol to endoplasmic reticulum; IMP:FlyBase.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:FlyBase.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:FlyBase.
DR GO; GO:0007629; P:flight behavior; IGI:FlyBase.
DR GO; GO:0060047; P:heart contraction; IMP:FlyBase.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:FlyBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:1901896; P:positive regulation of ATPase-coupled calcium transmembrane transporter activity; IGI:FlyBase.
DR GO; GO:0010884; P:positive regulation of lipid storage; IMP:FlyBase.
DR GO; GO:0051282; P:regulation of sequestering of calcium ion; IMP:FlyBase.
DR GO; GO:0030322; P:stabilization of membrane potential; IGI:FlyBase.
DR GO; GO:0048863; P:stem cell differentiation; IMP:FlyBase.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005782; P-type_ATPase_IIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01116; ATPase-IIA1_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calcium; Calcium transport;
KW Endoplasmic reticulum; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Sarcoplasmic reticulum; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1020
FT /note="Calcium-transporting ATPase sarcoplasmic/endoplasmic
FT reticulum type"
FT /id="PRO_0000046208"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 49..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 70..89
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 90..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 111..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 254..273
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 274..295
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 296..313
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 314..757
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 758..777
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 778..787
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 788..808
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 809..828
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 829..851
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 852..897
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 898..917
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250"
FT TOPO_DOM 918..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 931..949
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250"
FT TOPO_DOM 950..964
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 965..985
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250"
FT TOPO_DOM 986..1020
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT ACT_SITE 351
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 703
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 707
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 768
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 771
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 796
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 799
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 800
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 800
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 908
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 994..1020
FT /note="GESPIYKMHGIVLMWAVFFGLLYAMML -> VPDVVVDRM (in isoform
FT A)"
FT /evidence="ECO:0000303|PubMed:2148477"
FT /id="VSP_010297"
FT CONFLICT 158
FT /note="K -> R (in Ref. 4; AAL13694)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="L -> V (in Ref. 1; AAB00735)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="T -> L (in Ref. 5; CAA35505)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="S -> P (in Ref. 4; AAL13694)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1020 AA; 111701 MW; 6A62D350BF316984 CRC64;
MEDGHSKTVE QSLNFFGTDP ERGLTLDQIK ANQKKYGPNE LPTEEGKSIW QLVLEQFDDL
LVKILLLAAI ISFVLALFEE HEETFTAFVE PLVILLILIA NAVVGVWQER NAESAIEALK
EYEPEMGKVV RQDKSGIQKV RAKEIVPGDL VEVSVGDKIP ADIRITHIYS TTLRIDQSIL
TGESVSVIKH TDAIPDPRAV NQDKKNILFS GTNVAAGKAR GVVIGTGLST AIGKIRTEMS
ETEEIKTPLQ QKLDEFGEQL SKVISVICVA VWAINIGHFN DPAHGGSWIK GAIYYFKIAV
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
MSVSRMFIFD KVEGNDSSFL EFEMTGSTYE PIGEVFLNGQ RIKAADYDTL QELSTICIMC
NDSAIDYNEF KQAFEKVGEA TETALIVLAE KLNSFSVNKS GLDRRSAAIA CRGEIETKWK
KEFTLEFSRD RKSMSSYCTP LKASRLGTGP KLFVKGAPEG VLERCTHARV GTTKVPLTSA
LKAKILALTG QYGTGRDTLR CLALAVADSP MKPDEMDLGD STKFYQYEVN LTFVGVVGML
DPPRKEVFDS IVRCRAAGIR VIVITGDNKA TAEAICRRIG VFAEDEDTTG KSYSGREFDD
LSPTEQKAAV ARSRLFSRVE PQHKSKIVEF LQSMNEISAM TGDGVNDAPA LKKAEIGIAM
GSGTAVAKSA AEMVLADDNF SSIVSAVEEG RAIYNNMKQF IRYLISSNIG EVVSIFLTAA
LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMEKP PRKADEGLIS GWLFFRYMAI
GFYVGAATVG AAAWWFVFSD EGPKLSYWQL THHLSCLGGG DEFKGVDCKI FSDPHAMTMA
LSVLVTIEML NAMNSLSENQ SLITMPPWCN LWLIGSMALS FTLHFVILYV DVLSTVFQVT
PLSAEEWITV MKFSIPVVLL DETLKFVARK IADGESPIYK MHGIVLMWAV FFGLLYAMML
