RP3A_MOUSE
ID RP3A_MOUSE Reviewed; 681 AA.
AC P47708;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Rabphilin-3A;
DE AltName: Full=Exophilin-1;
GN Name=Rph3a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Inagaki N.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-606.
RC STRAIN=C57BL/6J;
RX PubMed=7822236; DOI=10.1093/oxfordjournals.jbchem.a124512;
RA Inagaki N., Mizuta M., Seino S.;
RT "Cloning of a mouse Rabphilin-3A expressed in hormone-secreting cells.";
RL J. Biochem. 116:239-242(1994).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=10407024; DOI=10.1523/jneurosci.19-14-05834.1999;
RA Schlueter O.M., Schnell E., Verhage M., Tzonopoulos T., Nicoll R.A.,
RA Janz R., Malenka R.C., Geppert M., Suedhof T.C.;
RT "Rabphilin knock-out mice reveal that rabphilin is not required for rab3
RT function in regulating neurotransmitter release.";
RL J. Neurosci. 19:5834-5846(1999).
RN [5]
RP INTERACTION WITH RAB3A; RAB3B; RAB3C; RAB3D; RAB8A; RAB27A AND RAB27B.
RX PubMed=12578829; DOI=10.1074/jbc.m212341200;
RA Fukuda M.;
RT "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2.
RT Identification of a critical determinant of Rab3A/Rab27A recognition by
RT Rim2.";
RL J. Biol. Chem. 278:15373-15380(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-223, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [9]
RP STRUCTURE BY NMR OF 368-507 IN COMPLEX WITH CALCIUM IONS, CALCIUM-BINDING
RP DOMAIN, SUBCELLULAR LOCATION, AND LIPID-BINDING.
RX PubMed=18945677; DOI=10.1074/jbc.m804094200;
RA Coudevylle N., Montaville P., Leonov A., Zweckstetter M., Becker S.;
RT "Structural determinants for Ca2+ and phosphatidylinositol 4,5-bisphosphate
RT binding by the C2A domain of rabphilin-3A.";
RL J. Biol. Chem. 283:35918-35928(2008).
CC -!- FUNCTION: Plays an essential role in docking and fusion steps of
CC regulated exocytosis (By similarity). At the presynaptic level, RPH3A
CC is recruited by RAB3A to the synaptic vesicle membrane in a GTP-
CC dependent manner where it modulates synaptic vesicle trafficking and
CC calcium-triggered neurotransmitter release (By similarity). In the
CC post-synaptic compartment, forms a ternary complex with GRIN2A and DLG4
CC and regulates NMDA receptor stability. Also plays a role in the
CC exocytosis of arginine vasopressin hormone (By similarity).
CC {ECO:0000250|UniProtKB:P47709}.
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 (PubMed:12578829). Interacts with RAB3A; this interaction recruits
CC RPH3A to synaptic vesicules (By similarity). Interacts (via C2B domain)
CC with SNAP25 (By similarity). Interacts with deubiquitinating enzyme
CC CAND1; this interaction results in the deubiquitination of RPH3A (By
CC similarity). Interacts with GRIN2A and DLG4; this ternary complex
CC regulates NMDA receptor composition at postsynaptic membranes (By
CC similarity). Interacts with SNCA (By similarity).
CC {ECO:0000250|UniProtKB:P47709, ECO:0000250|UniProtKB:Q9Y2J0,
CC ECO:0000269|PubMed:12578829}.
CC -!- INTERACTION:
CC P47708; Q9ERI2: Rab27a; NbExp=2; IntAct=EBI-398376, EBI-398172;
CC P47708; P63011: Rab3a; NbExp=2; IntAct=EBI-398376, EBI-398393;
CC P47708; P55258: Rab8a; NbExp=2; IntAct=EBI-398376, EBI-398411;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:P47709}. Cell projection,
CC dendritic spine {ECO:0000250|UniProtKB:P47709}. Postsynaptic cell
CC membrane {ECO:0000250|UniProtKB:P47709}. Membrane
CC {ECO:0000250|UniProtKB:P47709}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P47709}.
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 -!- PTM: Ubiquitinated. Deubiquitinated by CAND1 to prevent its
CC degradation. {ECO:0000250|UniProtKB:P47709}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are viable and fertile
CC and do not display any physiological impairment. Additionally, synaptic
CC properties seem unaffected. {ECO:0000269|PubMed:10407024}.
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DR EMBL; BC042585; AAH42585.1; -; mRNA.
DR EMBL; BC050883; AAH50883.1; -; mRNA.
DR EMBL; D29965; BAA06231.2; -; mRNA.
DR CCDS; CCDS39246.1; -.
DR PIR; JX0338; JX0338.
DR RefSeq; NP_001289273.1; NM_001302344.1.
DR RefSeq; NP_001289274.1; NM_001302345.1.
DR RefSeq; NP_035416.1; NM_011286.3.
DR PDB; 2K3H; NMR; -; A=368-507.
DR PDBsum; 2K3H; -.
DR AlphaFoldDB; P47708; -.
DR SMR; P47708; -.
DR BioGRID; 202964; 17.
DR IntAct; P47708; 6.
DR STRING; 10090.ENSMUSP00000078198; -.
DR iPTMnet; P47708; -.
DR PhosphoSitePlus; P47708; -.
DR SwissPalm; P47708; -.
DR MaxQB; P47708; -.
DR PaxDb; P47708; -.
DR PeptideAtlas; P47708; -.
DR PRIDE; P47708; -.
DR ProteomicsDB; 300433; -.
DR Antibodypedia; 996; 276 antibodies from 33 providers.
DR DNASU; 19894; -.
DR Ensembl; ENSMUST00000079204; ENSMUSP00000078198; ENSMUSG00000029608.
DR Ensembl; ENSMUST00000202326; ENSMUSP00000144291; ENSMUSG00000029608.
DR Ensembl; ENSMUST00000202406; ENSMUSP00000143917; ENSMUSG00000029608.
DR GeneID; 19894; -.
DR KEGG; mmu:19894; -.
DR UCSC; uc008zil.2; mouse.
DR CTD; 22895; -.
DR MGI; MGI:102788; Rph3a.
DR VEuPathDB; HostDB:ENSMUSG00000029608; -.
DR eggNOG; KOG1013; Eukaryota.
DR GeneTree; ENSGT00940000157468; -.
DR HOGENOM; CLU_011461_2_0_1; -.
DR InParanoid; P47708; -.
DR OMA; TREIWLC; -.
DR OrthoDB; 374694at2759; -.
DR PhylomeDB; P47708; -.
DR TreeFam; TF351844; -.
DR BioGRID-ORCS; 19894; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Rph3a; mouse.
DR EvolutionaryTrace; P47708; -.
DR PRO; PR:P47708; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P47708; protein.
DR Bgee; ENSMUSG00000029608; Expressed in primary visual cortex and 84 other tissues.
DR ExpressionAtlas; P47708; baseline and differential.
DR Genevisible; P47708; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098981; C:cholinergic synapse; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISS:ParkinsonsUK-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030141; C:secretory granule; ISS:ParkinsonsUK-UCL.
DR GO; GO:0045202; C:synapse; ISS:ParkinsonsUK-UCL.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0042301; F:phosphate ion binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0008430; F:selenium binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0097061; P:dendritic spine organization; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IGI:MGI.
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..681
FT /note="Rabphilin-3A"
FT /id="PRO_0000190228"
FT DOMAIN 40..157
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 379..501
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 537..670
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..375
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 278..302
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 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18945677,
FT ECO:0007744|PDB:2K3H"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18945677,
FT ECO:0007744|PDB:2K3H"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18945677,
FT ECO:0007744|PDB:2K3H"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18945677,
FT ECO:0007744|PDB:2K3H"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18945677,
FT ECO:0007744|PDB:2K3H"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18945677,
FT ECO:0007744|PDB:2K3H"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18945677,
FT ECO:0007744|PDB:2K3H"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18945677,
FT ECO:0007744|PDB:2K3H"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18945677,
FT ECO:0007744|PDB:2K3H"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18945677,
FT ECO:0007744|PDB:2K3H"
FT BINDING 526
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 568
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 568
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 574
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 628
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 628
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 629
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 630
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 630
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT BINDING 636
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT MOD_RES 223
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47709"
FT STRAND 382..390
FT /evidence="ECO:0007829|PDB:2K3H"
FT TURN 391..394
FT /evidence="ECO:0007829|PDB:2K3H"
FT STRAND 395..404
FT /evidence="ECO:0007829|PDB:2K3H"
FT STRAND 417..426
FT /evidence="ECO:0007829|PDB:2K3H"
FT TURN 428..430
FT /evidence="ECO:0007829|PDB:2K3H"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:2K3H"
FT STRAND 445..453
FT /evidence="ECO:0007829|PDB:2K3H"
FT HELIX 457..460
FT /evidence="ECO:0007829|PDB:2K3H"
FT STRAND 464..472
FT /evidence="ECO:0007829|PDB:2K3H"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:2K3H"
FT STRAND 478..487
FT /evidence="ECO:0007829|PDB:2K3H"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:2K3H"
FT STRAND 495..502
FT /evidence="ECO:0007829|PDB:2K3H"
SQ SEQUENCE 681 AA; 75489 MW; D09F8D8D2CBB271E CRC64;
MTDTVVNRWM YPGDGPLQSN DKEQLQAGWS VHPGAQTDRQ RKQEELTDEE KEIINRVIAR
AEKMEAMEQE RIGRLVDRLE TMRKNVAGDG VNRCILCGEQ LGMLGSACVV CEDCKKNVCT
KCGVETSNNR PHPVWLCKIC LEQREVWKRS GAWFFKGFPK QVLPQPMPIK KTKPQQPAGE
PATQEQPTPE SRHPARAPAR GDMEDRRPPG QKPGPDLTSA PGRGSHGPPT RRASEARMST
AARDSEGWDH AHGGGTGDTS RSPAGLRRAN SVQAARPAPA PVPSPAPPQP VQPGPPGGSR
ATPGPGRFPE QSTEAPPSDP GYPGAVAPAR EERTGPAGGF QAAPHTAAPY SQAAPARQPP
PAEEEEEEAN SYDSDEATTL GALEFSLLYD QDNSNLQCTI IRAKGLKPMD SNGLADPYVK
LHLLPGASKS NKLRTKTLRN TRNPVWNETL QYHGITEEDM QRKTLRISVC DEDKFGHNEF
IGETRFSLKK LKANQRKNFN ICLERVIPMK RAGTTGSARG MALYEEEQVE RIGDIEERGK
ILVSLMYSTQ QGGLIVGIIR CVHLAAMDAN GYSDPFVKLW LKPDMGKKAK HKTQIKKKTL
NPEFNEEFFY DIKHSDLAKK SLDISVWDYD IGKSNDYIGG CQLGISAKGE RLKHWYECLK
NKDKKIERWH QLQNENHVSS D
