AT2A2_PIG
ID AT2A2_PIG Reviewed; 1042 AA.
AC P11607; P11606; P79426; P79427;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 2;
DE Short=SERCA2;
DE Short=SR Ca(2+)-ATPase 2;
DE EC=7.2.2.10 {ECO:0000269|PubMed:30777856};
DE AltName: Full=Calcium pump 2;
DE AltName: Full=Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform;
DE AltName: Full=Endoplasmic reticulum class 1/2 Ca(2+) ATPase;
GN Name=ATP2A2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Stomach smooth muscle;
RX PubMed=2527496; DOI=10.1042/bj2600757;
RA Eggermont J.A., Wuytack F., de Jaegere S., Nelles L., Casteels R.;
RT "Evidence for two isoforms of the endoplasmic-reticulum Ca2+ pump in pig
RT smooth muscle.";
RL Biochem. J. 260:757-761(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 842-1042 (ISOFORMS 1 AND 2).
RX PubMed=2015309; DOI=10.1016/0167-4781(91)90143-a;
RA Eggermont J.A., Wuytack F., Casteels R.;
RT "Characterization of the 3' end of the pig sarcoplasmic/endoplasmic-
RT reticulum Ca2+ pump gene 2.";
RL Biochim. Biophys. Acta 1088:448-451(1991).
RN [3]
RP TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=2158303;
RA Eggermont J.A., Wuytack F., Casteels R.;
RT "Characterization of the mRNAs encoding the gene 2
RT sarcoplasmic/endoplasmic-reticulum Ca2+ pump in pig smooth muscle.";
RL Biochem. J. 266:901-907(1990).
RN [4] {ECO:0007744|PDB:5MPM, ECO:0007744|PDB:6HXB}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-993 IN COMPLEXES WITH CALCIUM
RP IONS AND ATP ANALOGS, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, TOPOLOGY, AND DISULFIDE BOND.
RX PubMed=30777856; DOI=10.15252/embj.2018100020;
RA Sitsel A., De Raeymaecker J., Drachmann N.D., Derua R., Smaardijk S.,
RA Andersen J.L., Vandecaetsbeek I., Chen J., De Maeyer M., Waelkens E.,
RA Olesen C., Vangheluwe P., Nissen P.;
RT "Structures of the heart specific SERCA2a Ca2+-ATPase.";
RL EMBO J. 38:0-0(2019).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the translocation of calcium from the cytosol to the
CC sarcoplasmic reticulum lumen. Involved in autophagy in response to
CC starvation. Upon interaction with VMP1 and activation, controls ER-
CC isolation membrane contacts for autophagosome formation. Also modulates
CC ER contacts with lipid droplets, mitochondria and endosomes.
CC {ECO:0000250|UniProtKB:P16615}.
CC -!- FUNCTION: [Isoform 2]: Involved in the regulation of the
CC contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated
CC Ca(2+) signaling pathways via its interaction with TMEM64 which is
CC critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS
CC generation necessary for proper osteoclast generation. Association
CC between TMEM64 and SERCA2 in the ER leads to cytosolic Ca(2+) spiking
CC for activation of NFATC1 and production of mitochondrial ROS, thereby
CC triggering Ca(2+) signaling cascades that promote osteoclast
CC differentiation and activation. {ECO:0000250|UniProtKB:O55143}.
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 Evidence={ECO:0000269|PubMed:30777856};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000305|PubMed:30777856};
CC -!- ACTIVITY REGULATION: Has different conformational states with
CC differential Ca2+ affinity. The E1 conformational state (active form)
CC shows high Ca(2+) affinity, while the E2 state exhibits low Ca(2+)
CC affinity. Reversibly inhibited by phospholamban (PLN) at low calcium
CC concentrations. Inhibited by sarcolipin (SLN) and myoregulin (MRLN).
CC The inhibition is blocked by VMP1 (By similarity). Enhanced by DWORF;
CC DWORF increases activity by displacing sarcolipin (SLN), phospholamban
CC (PLN) and myoregulin (MRLN) (By similarity). Stabilizes SERCA2 in its
CC E2 state (By similarity). {ECO:0000250|UniProtKB:O55143,
CC ECO:0000250|UniProtKB:P04191, ECO:0000250|UniProtKB:P16615,
CC ECO:0000250|UniProtKB:Q8R429}.
CC -!- SUBUNIT: Interacts with sarcolipin (SLN); the interaction inhibits
CC ATP2A2 Ca(2+) affinity. Interacts with phospholamban (PLN); the
CC interaction inhibits ATP2A2 Ca(2+) affinity (By similarity). Interacts
CC with myoregulin (MRLN) (By similarity). Interacts with DWORF (By
CC similarity). Interacts with HAX1 (By similarity). Interacts with S100A8
CC and S100A9 (By similarity). Interacts with SLC35G1 and STIM1. Interacts
CC with TMEM203 (By similarity). Interacts with TMEM64 and PDIA3 (By
CC similarity). Interacts with TMX2 (By similarity). Interacts with VMP1;
CC VMP1 competes with PLN and SLN to prevent them from forming an
CC inhibitory complex with ATP2A2. Interacts with ULK1 (By similarity).
CC Interacts with S100A1 in a Ca(2+)-dependent manner (By similarity).
CC Interacts with TUNAR (By similarity). {ECO:0000250|UniProtKB:O55143,
CC ECO:0000250|UniProtKB:P04191, ECO:0000250|UniProtKB:P16615,
CC ECO:0000250|UniProtKB:Q8R429}.
CC -!- SUBUNIT: [Isoform 1]: Interacts with TRAM2 (via C-terminus).
CC {ECO:0000250|UniProtKB:P16615}.
CC -!- INTERACTION:
CC P11607; P27824: CANX; Xeno; NbExp=2; IntAct=EBI-8004986, EBI-355947;
CC P11607; P41143: OPRD1; Xeno; NbExp=2; IntAct=EBI-8004986, EBI-2624456;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:30777856}. Sarcoplasmic reticulum membrane
CC {ECO:0000269|PubMed:30777856}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:30777856}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ATP2A2B, SERCA2b;
CC IsoId=P11607-1; Sequence=Displayed;
CC Name=2; Synonyms=ATP2A2A, SERCA2a;
CC IsoId=P11607-2; Sequence=VSP_000360;
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Detected in heart left ventricle (at
CC protein level) (PubMed:30777856). Isoform 2 is highly expressed in
CC heart and slow twitch skeletal muscle. Isoform 1 is widely expressed.
CC {ECO:0000269|PubMed:2158303, ECO:0000269|PubMed:30777856}.
CC -!- DOMAIN: Ca(2+) and ATP binding cause major rearrangements of the
CC cytoplasmic and transmembrane domains. According to the E1-E2 model,
CC Ca(2+) binding to the cytosolic domain of the pump in the high-affinity
CC E1 conformation is followed by the ATP-dependent phosphorylation of the
CC active site Asp, giving rise to E1P. A conformational change of the
CC phosphoenzyme gives rise to the low-affinity E2P state that exposes the
CC Ca(2+) ions to the lumenal side and promotes Ca(2+) release.
CC Dephosphorylation of the active site Asp mediates the subsequent return
CC to the E1 conformation. {ECO:0000250|UniProtKB:P04191}.
CC -!- DOMAIN: PLN and SLN both have a single transmembrane helix; both occupy
CC a similar binding site that is situated between the ATP2A2
CC transmembrane helices. {ECO:0000250|UniProtKB:P04191}.
CC -!- PTM: Nitrated under oxidative stress. Nitration on the two tyrosine
CC residues inhibits catalytic activity. {ECO:0000250|UniProtKB:P16615}.
CC -!- PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia,
CC leading to its inactivation. {ECO:0000250|UniProtKB:O55143}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
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DR EMBL; X15074; CAA33170.1; -; mRNA.
DR EMBL; X15073; CAA33169.1; -; mRNA.
DR EMBL; X53754; CAA37783.1; -; Genomic_DNA.
DR EMBL; X53754; CAA37784.1; -; Genomic_DNA.
DR PIR; S04651; S04651.
DR PIR; S04652; S04652.
DR RefSeq; NP_999030.1; NM_213865.1. [P11607-1]
DR PDB; 5MPM; X-ray; 3.30 A; A=1-993.
DR PDB; 6HXB; X-ray; 4.00 A; A=1-993.
DR PDBsum; 5MPM; -.
DR PDBsum; 6HXB; -.
DR AlphaFoldDB; P11607; -.
DR BMRB; P11607; -.
DR SMR; P11607; -.
DR BioGRID; 1149018; 1.
DR IntAct; P11607; 2.
DR MINT; P11607; -.
DR STRING; 9823.ENSSSCP00000019348; -.
DR PeptideAtlas; P11607; -.
DR PRIDE; P11607; -.
DR Ensembl; ENSSSCT00000045994; ENSSSCP00000037774; ENSSSCG00000034386. [P11607-1]
DR Ensembl; ENSSSCT00015008195; ENSSSCP00015003301; ENSSSCG00015006148. [P11607-1]
DR Ensembl; ENSSSCT00025020640; ENSSSCP00025008478; ENSSSCG00025015273. [P11607-1]
DR Ensembl; ENSSSCT00030063269; ENSSSCP00030028946; ENSSSCG00030045278. [P11607-1]
DR Ensembl; ENSSSCT00035043363; ENSSSCP00035017345; ENSSSCG00035032729. [P11607-1]
DR Ensembl; ENSSSCT00040006183; ENSSSCP00040002459; ENSSSCG00040004634. [P11607-1]
DR Ensembl; ENSSSCT00045030557; ENSSSCP00045021173; ENSSSCG00045017876. [P11607-1]
DR Ensembl; ENSSSCT00055035587; ENSSSCP00055028270; ENSSSCG00055017945. [P11607-1]
DR Ensembl; ENSSSCT00060108150; ENSSSCP00060048139; ENSSSCG00060078303. [P11607-1]
DR Ensembl; ENSSSCT00065011829; ENSSSCP00065004850; ENSSSCG00065008853. [P11607-1]
DR Ensembl; ENSSSCT00070027936; ENSSSCP00070023256; ENSSSCG00070014188. [P11607-1]
DR GeneID; 396875; -.
DR KEGG; ssc:396875; -.
DR CTD; 488; -.
DR GeneTree; ENSGT00940000159986; -.
DR InParanoid; P11607; -.
DR OMA; PLWNNMM; -.
DR OrthoDB; 100699at2759; -.
DR Reactome; R-SSC-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-SSC-5578775; Ion homeostasis.
DR Reactome; R-SSC-936837; Ion transport by P-type ATPases.
DR Proteomes; UP000008227; Chromosome 14.
DR Proteomes; UP000314985; Chromosome 14.
DR Bgee; ENSSSCG00000034386; Expressed in heart left ventricle and 42 other tissues.
DR ExpressionAtlas; P11607; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0097470; C:ribbon synapse; IEA:Ensembl.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR GO; GO:0086039; F:P-type calcium transporter activity involved in regulation of cardiac muscle cell membrane potential; ISS:UniProtKB.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0044548; F:S100 protein binding; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; ISS:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:1903515; P:calcium ion transport from cytosol to endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:0006984; P:ER-nucleus signaling pathway; IEA:Ensembl.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; ISS:UniProtKB.
DR GO; GO:0045822; P:negative regulation of heart contraction; IEA:Ensembl.
DR GO; GO:1900121; P:negative regulation of receptor binding; IEA:Ensembl.
DR GO; GO:0070050; P:neuron cellular homeostasis; IEA:Ensembl.
DR GO; GO:0140056; P:organelle localization by membrane tethering; ISS:UniProtKB.
DR GO; GO:0032470; P:positive regulation of endoplasmic reticulum calcium ion concentration; IEA:Ensembl.
DR GO; GO:1903233; P:regulation of calcium ion-dependent exocytosis of neurotransmitter; IEA:Ensembl.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IBA:GO_Central.
DR GO; GO:0002026; P:regulation of the force of heart contraction; IEA:Ensembl.
DR GO; GO:0070296; P:sarcoplasmic reticulum calcium ion transport; IEA:Ensembl.
DR GO; GO:0033292; P:T-tubule organization; IEA:Ensembl.
DR GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
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 PRINTS; PR00120; HATPASE.
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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Calcium;
KW Calcium transport; Disulfide bond; Endoplasmic reticulum; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nitration; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Sarcoplasmic reticulum; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1042
FT /note="Sarcoplasmic/endoplasmic reticulum calcium ATPase 2"
FT /id="PRO_0000046198"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 49..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 70..89
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 111..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 254..273
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 274..295
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 296..313
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 314..756
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 757..776
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 777..786
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 787..807
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 808..827
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 828..850
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 851..896
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 897..916
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 917..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 930..948
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 949..963
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 964..984
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TOPO_DOM 985..1042
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 575..594
FT /note="Interaction with HAX1"
FT /evidence="ECO:0000250"
FT REGION 787..807
FT /note="Interaction with PLN"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT REGION 788..1042
FT /note="Interaction with TMEM64 and PDIA3"
FT /evidence="ECO:0000250|UniProtKB:O55143"
FT REGION 931..942
FT /note="Interaction with PLN"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT ACT_SITE 351
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30777856,
FT ECO:0007744|PDB:5MPM"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30777856,
FT ECO:0007744|PDB:5MPM"
FT BINDING 442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 559
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 624..626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 677
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 702
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:30777856,
FT ECO:0007744|PDB:5MPM"
FT BINDING 705
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 767
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 770
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 795
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 798
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 799
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 799
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:30777856,
FT ECO:0007744|PDB:6HXB"
FT BINDING 907
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55143"
FT MOD_RES 294
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16615"
FT MOD_RES 295
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16615"
FT MOD_RES 441
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64578"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55143"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16615"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16615"
FT DISULFID 875..887
FT /evidence="ECO:0000269|PubMed:30777856,
FT ECO:0007744|PDB:5MPM"
FT VAR_SEQ 994..1042
FT /note="GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS ->
FT AILE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2527496"
FT /id="VSP_000360"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:5MPM"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 60..75
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 89..109
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 248..274
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:5MPM"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 291..306
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 311..327
FT /evidence="ECO:0007829|PDB:5MPM"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 362..373
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 376..384
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 395..401
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 408..419
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:5MPM"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 440..452
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 466..478
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 479..488
FT /evidence="ECO:0007829|PDB:5MPM"
FT TURN 489..492
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 493..503
FT /evidence="ECO:0007829|PDB:5MPM"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 510..515
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 517..521
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 538..552
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 553..556
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 559..568
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 583..586
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 589..599
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 606..615
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 619..623
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 628..637
FT /evidence="ECO:0007829|PDB:5MPM"
FT TURN 648..650
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 654..659
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 662..671
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 674..677
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 680..692
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 697..701
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 707..712
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 713..719
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 724..728
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 730..736
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 740..780
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 788..806
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 815..817
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 830..856
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 866..870
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 872..874
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 889..891
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 893..913
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 915..919
FT /evidence="ECO:0007829|PDB:5MPM"
FT STRAND 921..924
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 926..928
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 930..948
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 952..956
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 964..973
FT /evidence="ECO:0007829|PDB:5MPM"
FT HELIX 975..989
FT /evidence="ECO:0007829|PDB:5MPM"
SQ SEQUENCE 1042 AA; 114792 MW; A68EC9E41494D532 CRC64;
MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL ELVIEQFEDL
LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA NAIVGVWQER NAENAIEALK
EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL
TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV
ATEQERTPLQ QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
MSVCRMFILD KVEGDTCSLN EFTITGSTYA PIGEVHKDDK PVKCHQYDGL VELATICALC
NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTELK GLSKIERANA CNSVIKQLMK
KEFTLEFSRD RKSMSVYCTP NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTPGV
KQKIMSVIRE WGSGSDTLRC LALATHDNPM RREEMNLEDS ANFIKYETNL TFVGCVGMLD
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK AFTGREFDEL
NPSAQREACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKSEIGIAMG
SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL
GFPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG
CYVGAATVGA AAWWFIAADG GPRVTFYQLS HFLQCKEDNP DFEGVDCAVF ESPYPMTMAL
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE PLPLIFQITP
LNLTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP ATKSCSFSAC TDGISWPFVL
LIMPLVIWVY STDTNFSDMF WS
