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 02-SEP-2026, entry version 207. 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; Evidence={ECO:0000255|PROSITE- CC 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}. 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; 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_001302344.2. DR RefSeq; NP_001289274.1; NM_001302345.2. DR RefSeq; NP_035416.1; NM_011286.4. DR PDB; 2K3H; NMR; -; A=368-507. DR AlphaFoldDB; P47708; -. DR SMR; P47708; -. DR BioGRID; 202964; 22. DR FunCoup; P47708; 497. DR IntAct; P47708; 6. DR STRING; 10090.ENSMUSP00000078198; -. DR GlyGen; P47708; 4 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P47708; -. DR PhosphoSitePlus; P47708; -. DR SwissPalm; P47708; -. DR PaxDb; 10090-ENSMUSP00000078198; -. DR PeptideAtlas; P47708; -. DR ProteomicsDB; 300433; -. DR Antibodypedia; 996; 280 antibodies from 35 providers. DR DNASU; 19894; -. DR Ensembl; ENSMUST00000079204.9; ENSMUSP00000078198.6; ENSMUSG00000029608.11. DR Ensembl; ENSMUST00000202326.4; ENSMUSP00000144291.2; ENSMUSG00000029608.11. DR Ensembl; ENSMUST00000202406.4; ENSMUSP00000143917.2; ENSMUSG00000029608.11. DR GeneID; 19894; -. DR KEGG; mmu:19894; -. DR UCSC; uc008zil.2; mouse. DR AGR; MGI:102788; -. 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; IRYHTSE; -. DR OrthoDB; 270970at2759; -. DR PhylomeDB; P47708; -. DR BioGRID-ORCS; 19894; 1 hit in 77 CRISPR screens. DR CD-CODE; CE726F99; Postsynaptic density. 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 86 other cell types or tissues. DR ExpressionAtlas; P47708; baseline and differential. DR GO; GO:0098981; C:cholinergic synapse; ISO:GO_Central. DR GO; GO:0043197; C:dendritic spine; ISO:GO_Central. DR GO; GO:0019898; C:extrinsic component of membrane; ISS:ParkinsonsUK-UCL. DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; ISO:GO_Central. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0031594; C:neuromuscular junction; ISO:GO_Central. DR GO; GO:0043005; C:neuron projection; ISS:ParkinsonsUK-UCL. DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB. 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:GO_Central. 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:0099502; P:calcium-dependent activation of synaptic vesicle fusion; IBA:GO_Central. DR GO; GO:0097061; P:dendritic spine organization; ISO:GO_Central. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IBA:GO_Central. DR GO; GO:2000310; P:regulation of NMDA receptor activity; ISO:GO_Central. DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IGI:MGI. DR GO; GO:0016082; P:synaptic vesicle priming; IDA:SynGO. DR CDD; cd04035; C2A_Rabphilin_Doc2; 1. DR CDD; cd08384; C2B_Rabphilin_Doc2; 1. DR CDD; cd15762; FYVE_RP3A; 1. DR FunFam; 2.60.40.150:FF:000032; Double c2-like domain-containing; 1. DR FunFam; 2.60.40.150:FF:000023; Double C2-like domain-containing protein; 1. DR FunFam; 3.30.40.10:FF:000182; rabphilin-3A isoform X1; 1. DR Gene3D; 2.60.40.150; C2 domain; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR041282; FYVE_2. DR InterPro; IPR028698; FYVE_RPH3A. DR InterPro; IPR010911; Rab_BD. DR InterPro; IPR043566; Rabphilin/DOC2/Noc2. DR InterPro; IPR047022; Rabphilin_Doc2_C2A. 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; RABPHILIN, ISOFORM A; 1. DR PANTHER; PTHR45729:SF3; RABPHILIN-3A; 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; C2 domain (Calcium/lipid-binding domain, CaLB); 2. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR PROSITE; PS50004; C2; 2. DR PROSITE; PS50916; RABBD; 1. DR PROSITE; PS50178; ZF_FYVE; 1. DR PDBsum; 2K3H; -. 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 199..208 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 243..252 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 278..296 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 347..356 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 362..375 FT /note="Acidic 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 //