RP3A_RAT
ID RP3A_RAT Reviewed; 684 AA.
AC P47709;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Rabphilin-3A;
DE AltName: Full=Exophilin-1;
GN Name=Rph3a;
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].
RX PubMed=7946335; DOI=10.1016/0896-6273(94)90254-2;
RA Li C., Takei K., Geppert M., Daniell L., Stenius K., Chapman E.R., Jahn R.,
RA de Camilli P., Suedhof T.C.;
RT "Synaptic targeting of rabphilin-3A, a synaptic vesicle Ca2+/phospholipid-
RT binding protein, depends on rab3A/3C.";
RL Neuron 13:885-898(1994).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=8060298; DOI=10.1006/bbrc.1994.2063;
RA Mizoguchi A., Yano Y., Hamaguchi H., Yanagida H., Ide C., Zahraoui A.,
RA Shirataki H., Sasaki T., Takai Y.;
RT "Localization of Rabphilin-3A on the synaptic vesicle.";
RL Biochem. Biophys. Res. Commun. 202:1235-1243(1994).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAB3A.
RX PubMed=8617225; DOI=10.1002/j.1460-2075.1996.tb00529.x;
RA Stahl B., Chou J.H., Li C., Suedhof T.C., Jahn R.;
RT "Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism
RT analogous to raf recruitment by ras.";
RL EMBO J. 15:1799-1809(1996).
RN [4]
RP FUNCTION, AND INTERACTION WITH SNAP25 AND RAB27A.
RX PubMed=16203731; DOI=10.1074/jbc.m507173200;
RA Tsuboi T., Fukuda M.;
RT "The C2B domain of rabphilin directly interacts with SNAP-25 and regulates
RT the docking step of dense core vesicle exocytosis in PC12 cells.";
RL J. Biol. Chem. 280:39253-39259(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682 AND SER-683, AND
RP IDENTIFICATION BY MASS 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).
RN [6]
RP FUNCTION, INTERACTION WITH GRIN2A AND DLG4, AND SUBCELLULAR LOCATION.
RX PubMed=26679993; DOI=10.1038/ncomms10181;
RA Stanic J., Carta M., Eberini I., Pelucchi S., Marcello E., Genazzani A.A.,
RA Racca C., Mulle C., Di Luca M., Gardoni F.;
RT "Rabphilin 3A retains NMDA receptors at synaptic sites through interaction
RT with GluN2A/PSD-95 complex.";
RL Nat. Commun. 6:10181-10181(2015).
RN [7]
RP INTERACTION WITH CAND1, AND FUNCTION.
RX PubMed=29367474; DOI=10.1507/endocrj.ej17-0399;
RA Nakashima K., Takeuchi S., Iwama S., Kiyota A., Yasuda Y., Iwata N.,
RA Enomoto A., Arima H., Sugimura Y.;
RT "Cullin-associated NEDD8-dissociated protein 1, a novel interactor of
RT rabphilin-3A, deubiquitylates rabphilin-3A and regulates arginine
RT vasopressin secretion in PC12 cells.";
RL Endocr. J. 65:325-334(2018).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 41-170 IN COMPLEX WITH RAB3A.
RC TISSUE=Brain;
RX PubMed=10025402; DOI=10.1016/s0092-8674(00)80549-8;
RA Ostermeier C., Brunger A.T.;
RT "Structural basis of Rab effector specificity: crystal structure of the
RT small G protein Rab3A complexed with the effector domain of rabphilin-3A.";
RL Cell 96:363-374(1999).
RN [9]
RP STRUCTURE BY NMR OF 541-680.
RX PubMed=10559882; DOI=10.1038/10076;
RA Ubach J., Garcia J., Nittler M.P., Sudhof T.C., Rizo J.;
RT "Structure of the Janus-faced C2B domain of rabphilin.";
RL Nat. Cell Biol. 1:106-112(1999).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 519-684 IN COMPLEX WITH CALCIUM
RP IONS, DOMAIN, SUBCELLULAR LOCATION, AND CALCIUM-BINDING.
RX PubMed=17166855; DOI=10.1074/jbc.m606746200;
RA Montaville P., Schlicker C., Leonov A., Zweckstetter M., Sheldrick G.M.,
RA Becker S.;
RT "The C2A-C2B linker defines the high affinity Ca(2+) binding mode of
RT rabphilin-3A.";
RL J. Biol. Chem. 282:5015-5025(2007).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 378-510 IN COMPLEX WITH CALCIUM.
RX PubMed=24302762; DOI=10.1073/pnas.1316179110;
RA Guillen J., Ferrer-Orta C., Buxaderas M., Perez-Sanchez D.,
RA Guerrero-Valero M., Luengo-Gil G., Pous J., Guerra P.,
RA Gomez-Fernandez J.C., Verdaguer N., Corbalan-Garcia S.;
RT "Structural insights into the Ca2+ and PI(4,5)P2 binding modes of the C2
RT domains of rabphilin 3A and synaptotagmin 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20503-20508(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 536-680, AND INTERACTION WITH
RP SNAP25.
RX PubMed=28634303; DOI=10.1073/pnas.1702542114;
RA Ferrer-Orta C., Perez-Sanchez M.D., Coronado-Parra T., Silva C.,
RA Lopez-Martinez D., Baltanas-Copado J., Gomez-Fernandez J.C.,
RA Corbalan-Garcia S., Verdaguer N.;
RT "Structural characterization of the Rabphilin-3A-SNAP25 interaction.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E5343-E5351(2017).
CC -!- FUNCTION: Plays an essential role in docking and fusion steps of
CC regulated exocytosis (PubMed:8617225, PubMed:16203731). At the
CC presynaptic level, RPH3A is recruited by RAB3A to the synaptic vesicle
CC membrane in a GTP-dependent manner where it modulates synaptic vesicle
CC trafficking and calcium-triggered neurotransmitter release
CC (PubMed:8617225). In the post-synaptic compartment, forms a ternary
CC complex with GRIN2A and DLG4 and regulates NMDA receptor stability
CC (PubMed:26679993). Also plays a role in the exocytosis of arginine
CC vasopressin hormone (PubMed:29367474). {ECO:0000269|PubMed:16203731,
CC ECO:0000269|PubMed:26679993, ECO:0000269|PubMed:29367474,
CC ECO:0000269|PubMed:8617225}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts with RAB3B, RAB3C, RAB3D, RAB8A, RAB27A and RAB27B
CC (By similarity). Interacts with RAB3A; this interaction recruits RPH3A
CC to synaptic vesicules (PubMed:8617225, PubMed:10025402). Interacts (via
CC C2B domain) with SNAP25 (PubMed:16203731, PubMed:28634303). Interacts
CC with deubiquitinating enzyme CAND1; this interaction results in the
CC deubiquitination of RPH3A (PubMed:29367474). Interacts with GRIN2A and
CC DLG4; this ternary complex regulates NMDA receptor composition at
CC postsynaptic membranes (PubMed:26679993). Interacts with SNCA (By
CC similarity). {ECO:0000250|UniProtKB:P47708,
CC ECO:0000250|UniProtKB:Q9Y2J0, ECO:0000269|PubMed:10025402,
CC ECO:0000269|PubMed:16203731, ECO:0000269|PubMed:26679993,
CC ECO:0000269|PubMed:28634303, ECO:0000269|PubMed:29367474,
CC ECO:0000269|PubMed:8617225}.
CC -!- INTERACTION:
CC P47709; P63012: Rab3a; NbExp=2; IntAct=EBI-1027524, EBI-440126;
CC P47709; P60881: Snap25; NbExp=4; IntAct=EBI-1027524, EBI-1027214;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:8060298,
CC ECO:0000269|PubMed:8617225}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:26679993}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:26679993}. Membrane {ECO:0000269|PubMed:17166855};
CC Peripheral membrane protein {ECO:0000269|PubMed:17166855}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain.
CC -!- DOMAIN: Binds calcium via the C2 domains. The calcium-bound C2 domains
CC mediate interactions with phospholipid bilayers.
CC {ECO:0000269|PubMed:17166855}.
CC -!- PTM: Ubiquitinated. Deubiquitinated by CAND1 to prevent its
CC degradation. {ECO:0000269|PubMed:29367474}.
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DR EMBL; U12571; AAA62662.1; -; mRNA.
DR PIR; I58166; I58166.
DR RefSeq; NP_598202.1; NM_133518.1.
DR PDB; 1ZBD; X-ray; 2.60 A; B=41-170.
DR PDB; 2CHD; X-ray; 1.92 A; A=371-510.
DR PDB; 2CM5; X-ray; 1.28 A; A=519-684.
DR PDB; 2CM6; X-ray; 1.85 A; A/B=519-684.
DR PDB; 3RPB; NMR; -; A=541-680.
DR PDB; 4LT7; X-ray; 2.50 A; A=378-510.
DR PDB; 4NP9; X-ray; 1.92 A; A=378-510.
DR PDB; 4NS0; X-ray; 1.80 A; A=378-510.
DR PDB; 5LO8; X-ray; 2.50 A; A/B=536-680.
DR PDB; 5LOB; X-ray; 3.30 A; A/B/C=536-680.
DR PDB; 5LOW; X-ray; 2.80 A; A/B/C/H/I/J=536-680.
DR PDBsum; 1ZBD; -.
DR PDBsum; 2CHD; -.
DR PDBsum; 2CM5; -.
DR PDBsum; 2CM6; -.
DR PDBsum; 3RPB; -.
DR PDBsum; 4LT7; -.
DR PDBsum; 4NP9; -.
DR PDBsum; 4NS0; -.
DR PDBsum; 5LO8; -.
DR PDBsum; 5LOB; -.
DR PDBsum; 5LOW; -.
DR AlphaFoldDB; P47709; -.
DR SMR; P47709; -.
DR BioGRID; 251056; 5.
DR IntAct; P47709; 6.
DR MINT; P47709; -.
DR STRING; 10116.ENSRNOP00000001844; -.
DR iPTMnet; P47709; -.
DR PhosphoSitePlus; P47709; -.
DR PaxDb; P47709; -.
DR PRIDE; P47709; -.
DR GeneID; 171039; -.
DR KEGG; rno:171039; -.
DR UCSC; RGD:620073; rat.
DR CTD; 22895; -.
DR RGD; 620073; Rph3a.
DR eggNOG; KOG1013; Eukaryota.
DR InParanoid; P47709; -.
DR OrthoDB; 374694at2759; -.
DR PhylomeDB; P47709; -.
DR EvolutionaryTrace; P47709; -.
DR PRO; PR:P47709; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:RGD.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IDA:RGD.
DR GO; GO:0042301; F:phosphate ion binding; IDA:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:RGD.
DR GO; GO:0005543; F:phospholipid binding; TAS:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0008430; F:selenium binding; IDA:RGD.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0097061; P:dendritic spine organization; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:UniProtKB.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; ISO:RGD.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR043566; Rabphilin/DOC2/Noc2.
DR InterPro; IPR028698; RPH3A.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45729; PTHR45729; 1.
DR PANTHER; PTHR45729:SF3; PTHR45729:SF3; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Lipid-binding; Membrane; Metal-binding; Methylation; Phosphoprotein;
KW Postsynaptic cell membrane; Protein transport; Reference proteome; Repeat;
KW Synapse; Transport; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..684
FT /note="Rabphilin-3A"
FT /id="PRO_0000190229"
FT DOMAIN 40..157
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 382..504
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 540..673
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 88..145
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24302762,
FT ECO:0007744|PDB:4LT7"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:24302762,
FT ECO:0007744|PDB:4LT7"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 482
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT BINDING 529
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17166855,
FT ECO:0007744|PDB:2CM5"
FT BINDING 571
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17166855,
FT ECO:0007744|PDB:2CM5, ECO:0007744|PDB:2CM6"
FT BINDING 571
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:17166855,
FT ECO:0007744|PDB:2CM5, ECO:0007744|PDB:2CM6"
FT BINDING 577
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17166855,
FT ECO:0007744|PDB:2CM5, ECO:0007744|PDB:2CM6"
FT BINDING 631
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17166855,
FT ECO:0007744|PDB:2CM5, ECO:0007744|PDB:2CM6"
FT BINDING 631
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:17166855,
FT ECO:0007744|PDB:2CM5"
FT BINDING 632
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17166855,
FT ECO:0007744|PDB:2CM5, ECO:0007744|PDB:2CM6"
FT BINDING 633
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17166855,
FT ECO:0007744|PDB:2CM5, ECO:0007744|PDB:2CM6"
FT BINDING 633
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:17166855,
FT ECO:0007744|PDB:2CM5"
FT BINDING 639
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:17166855,
FT ECO:0007744|PDB:2CM5, ECO:0007744|PDB:2CM6"
FT MOD_RES 223
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47708"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT HELIX 50..84
FT /evidence="ECO:0007829|PDB:1ZBD"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1ZBD"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1ZBD"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1ZBD"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1ZBD"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1ZBD"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:1ZBD"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1ZBD"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1ZBD"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:1ZBD"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:1ZBD"
FT STRAND 385..393
FT /evidence="ECO:0007829|PDB:4NS0"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:4NS0"
FT STRAND 398..408
FT /evidence="ECO:0007829|PDB:4NS0"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:4LT7"
FT STRAND 420..428
FT /evidence="ECO:0007829|PDB:4NS0"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:4NS0"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:4NS0"
FT STRAND 448..457
FT /evidence="ECO:0007829|PDB:4NS0"
FT HELIX 460..465
FT /evidence="ECO:0007829|PDB:4NS0"
FT STRAND 467..475
FT /evidence="ECO:0007829|PDB:4NS0"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:4LT7"
FT STRAND 481..490
FT /evidence="ECO:0007829|PDB:4NS0"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:4NS0"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:4NS0"
FT HELIX 527..530
FT /evidence="ECO:0007829|PDB:2CM6"
FT STRAND 543..551
FT /evidence="ECO:0007829|PDB:2CM5"
FT TURN 552..555
FT /evidence="ECO:0007829|PDB:2CM5"
FT STRAND 556..566
FT /evidence="ECO:0007829|PDB:2CM5"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:5LOW"
FT STRAND 578..585
FT /evidence="ECO:0007829|PDB:2CM5"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:5LOB"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:2CM5"
FT STRAND 606..614
FT /evidence="ECO:0007829|PDB:2CM5"
FT HELIX 617..622
FT /evidence="ECO:0007829|PDB:2CM5"
FT STRAND 624..631
FT /evidence="ECO:0007829|PDB:2CM5"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:2CM5"
FT STRAND 639..647
FT /evidence="ECO:0007829|PDB:2CM5"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:5LO8"
FT HELIX 652..663
FT /evidence="ECO:0007829|PDB:2CM5"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:3RPB"
FT STRAND 669..674
FT /evidence="ECO:0007829|PDB:2CM5"
SQ SEQUENCE 684 AA; 75832 MW; 05838BC3C7A86444 CRC64;
MTDTVVNRWM YPGDGPLQSN DKEQLQAGWS VHPGAQTDRQ RKQEELTDEE KEIINRVIAR
AEKMETMEQE RIGRLVDRLE TMRKNVAGDG VNRCILCGEQ LGMLGSACVV CEDCKKNVCT
KCGVETSNNR PHPVWLCKIC LEQREVWKRS GAWFFKGFPK QVLPQPMPIK KTKPQQPAGE
PATQEQPTPE SRHPARAPAR GDMEDRRAPG QKPGPDLTSA PGRGSHGPPT RRASEARMST
TTRDSEGWDH GHGGGAGDTS RSPGGEQGLR RANSVQASRP APASMPSPAP PQPVQPGPPG
GSRAAPGPGR FPEQSTEAPP SDPGYPGAVA PAREERTGPT GGFQAAPHTA GPYSQAAPAR
QPPPAEEEEE EANSYDSDQA TTLGALEFSL LYDQDNSNLQ CTIIRAKGLK PMDSNGLADP
YVKLHLLPGA SKSNKLRTKT LRNTRNPVWN ETLQYHGITE EDMQRKTLRI SVCDEDKFGH
NEFIGETRFS LKKLKANQRK NFNICLERVI PMKRAGTTGS ARGMALYEEE QVERIGDIEE
RGKILVSLMY STQQGGLIVG IIRCVHLAAM DANGYSDPFV KLWLKPDMGK KAKHKTQIKK
KTLNPEFNEE FFYDIKHSDL AKKSLDISVW DYDIGKSNDY IGGCQLGISA KGERLKHWYE
CLKNKDKKIE RWHQLQNENH VSSD
