RPGF6_HUMAN
ID RPGF6_HUMAN Reviewed; 1601 AA.
AC Q8TEU7; A3KN82; A5PLL6; B7ZML2; E9PDV7; Q8NI21; Q8TEU6; Q96PC1;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Rap guanine nucleotide exchange factor 6;
DE AltName: Full=PDZ domain-containing guanine nucleotide exchange factor 2;
DE Short=PDZ-GEF2;
DE AltName: Full=RA-GEF-2;
GN Name=RAPGEF6; Synonyms=PDZGEF2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAL79915.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND VARIANT
RP ARG-1452.
RX PubMed=12581858; DOI=10.1016/s0167-4889(02)00365-8;
RA Kuiperij H.B., de Rooij J., Rehmann H., van Triest M., Wittinghofer A.,
RA Bos J.L., Zwartkruis F.J.T.;
RT "Characterisation of PDZ-GEFs, a family of guanine nucleotide exchange
RT factors specific for Rap1 and Rap2.";
RL Biochim. Biophys. Acta 1593:141-149(2003).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, AND VARIANT ARG-1452.
RA Banville D., Murthy K., Shen S., Clark K., Fortin Y.;
RT "A PDZ domain containing guanine exchange factor (GEF) interacts with the
RT second PDZ domain of human PTP1e.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND VARIANT ARG-1452.
RC TISSUE=Fetal brain {ECO:0000269|PubMed:11524421};
RX PubMed=11524421; DOI=10.1074/jbc.m105760200;
RA Gao X., Satoh T., Liao Y., Song C., Hu C.-D., Kariya K., Kataoka T.;
RT "Identification and characterization of RA-GEF-2, a Rap guanine nucleotide
RT exchange factor that serves as a downstream target of M-Ras.";
RL J. Biol. Chem. 276:42219-42225(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
RC TISSUE=Brain;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8] {ECO:0000305}
RP STRUCTURE BY NMR OF 265-386.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the cNMP-binding domain of human Rap guanine
RT nucleotide exchange factor 6.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for Rap1A, Rap2A and
CC M-Ras GTPases. Does not interact with cAMP.
CC {ECO:0000269|PubMed:11524421, ECO:0000269|PubMed:12581858}.
CC -!- SUBUNIT: Interacts with the second PDZ domain of human PTP1e.
CC {ECO:0000269|Ref.2, ECO:0000305}.
CC -!- INTERACTION:
CC Q8TEU7; Q12923: PTPN13; NbExp=4; IntAct=EBI-2693017, EBI-355227;
CC Q8TEU7; P46937: YAP1; NbExp=2; IntAct=EBI-2693017, EBI-1044059;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11524421}. Cell
CC membrane {ECO:0000269|PubMed:11524421}. Note=Upon binding to M-Ras, it
CC translocates to the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=PDZ-GEF2A {ECO:0000269|PubMed:12581858};
CC IsoId=Q8TEU7-1; Sequence=Displayed;
CC Name=2; Synonyms=PDZ-GEF2B {ECO:0000269|PubMed:12581858};
CC IsoId=Q8TEU7-2; Sequence=VSP_050610, VSP_050611;
CC Name=3;
CC IsoId=Q8TEU7-3; Sequence=VSP_050607, VSP_050608, VSP_050609;
CC Name=4;
CC IsoId=Q8TEU7-4; Sequence=VSP_050608;
CC Name=5;
CC IsoId=Q8TEU7-5; Sequence=VSP_050608, VSP_050609;
CC Name=6;
CC IsoId=Q8TEU7-6; Sequence=VSP_045027;
CC -!- TISSUE SPECIFICITY: Isoform 3 has highest expression levels in the
CC brain, heart, liver, lung and placenta and is barely detectable in
CC skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:11524421}.
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DR EMBL; AF478468; AAL79915.1; -; mRNA.
DR EMBL; AF478469; AAL79916.1; -; mRNA.
DR EMBL; AF478567; AAM21637.1; -; mRNA.
DR EMBL; AF394782; AAK83368.1; -; mRNA.
DR EMBL; AC004227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC133703; AAI33704.1; -; mRNA.
DR EMBL; BC142964; AAI42965.1; -; mRNA.
DR EMBL; BC144627; AAI44628.1; -; mRNA.
DR CCDS; CCDS34225.1; -. [Q8TEU7-1]
DR CCDS; CCDS54897.1; -. [Q8TEU7-6]
DR CCDS; CCDS54898.1; -. [Q8TEU7-2]
DR CCDS; CCDS54899.1; -. [Q8TEU7-5]
DR CCDS; CCDS54900.1; -. [Q8TEU7-4]
DR CCDS; CCDS54901.1; -. [Q8TEU7-3]
DR RefSeq; NP_001157858.1; NM_001164386.1. [Q8TEU7-4]
DR RefSeq; NP_001157859.1; NM_001164387.1. [Q8TEU7-3]
DR RefSeq; NP_001157860.1; NM_001164388.1. [Q8TEU7-5]
DR RefSeq; NP_001157861.1; NM_001164389.1. [Q8TEU7-2]
DR RefSeq; NP_001157862.1; NM_001164390.1. [Q8TEU7-6]
DR RefSeq; NP_057424.3; NM_016340.5. [Q8TEU7-1]
DR PDB; 2D93; NMR; -; A=265-385.
DR PDB; 3LNY; X-ray; 1.30 A; B=1596-1601.
DR PDBsum; 2D93; -.
DR PDBsum; 3LNY; -.
DR AlphaFoldDB; Q8TEU7; -.
DR SMR; Q8TEU7; -.
DR BioGRID; 119705; 54.
DR ELM; Q8TEU7; -.
DR IntAct; Q8TEU7; 23.
DR MINT; Q8TEU7; -.
DR STRING; 9606.ENSP00000296859; -.
DR iPTMnet; Q8TEU7; -.
DR PhosphoSitePlus; Q8TEU7; -.
DR BioMuta; RAPGEF6; -.
DR DMDM; 313104174; -.
DR EPD; Q8TEU7; -.
DR jPOST; Q8TEU7; -.
DR MassIVE; Q8TEU7; -.
DR MaxQB; Q8TEU7; -.
DR PaxDb; Q8TEU7; -.
DR PeptideAtlas; Q8TEU7; -.
DR PRIDE; Q8TEU7; -.
DR ProteomicsDB; 19757; -.
DR ProteomicsDB; 74497; -. [Q8TEU7-1]
DR ProteomicsDB; 74498; -. [Q8TEU7-2]
DR ProteomicsDB; 74499; -. [Q8TEU7-3]
DR ProteomicsDB; 74500; -. [Q8TEU7-4]
DR ProteomicsDB; 74501; -. [Q8TEU7-5]
DR Antibodypedia; 25867; 129 antibodies from 22 providers.
DR DNASU; 51735; -.
DR Ensembl; ENST00000296859.10; ENSP00000296859.6; ENSG00000158987.22. [Q8TEU7-4]
DR Ensembl; ENST00000308008.10; ENSP00000311419.6; ENSG00000158987.22. [Q8TEU7-2]
DR Ensembl; ENST00000507093.5; ENSP00000426081.2; ENSG00000158987.22. [Q8TEU7-3]
DR Ensembl; ENST00000509018.6; ENSP00000421684.1; ENSG00000158987.22. [Q8TEU7-1]
DR Ensembl; ENST00000510071.5; ENSP00000425389.1; ENSG00000158987.22. [Q8TEU7-6]
DR Ensembl; ENST00000627212.2; ENSP00000487439.1; ENSG00000158987.22. [Q8TEU7-5]
DR GeneID; 51735; -.
DR KEGG; hsa:51735; -.
DR MANE-Select; ENST00000509018.6; ENSP00000421684.1; NM_016340.6; NP_057424.3.
DR UCSC; uc003kvn.2; human. [Q8TEU7-1]
DR CTD; 51735; -.
DR DisGeNET; 51735; -.
DR GeneCards; RAPGEF6; -.
DR HGNC; HGNC:20655; RAPGEF6.
DR HPA; ENSG00000158987; Tissue enhanced (brain).
DR MIM; 610499; gene.
DR neXtProt; NX_Q8TEU7; -.
DR OpenTargets; ENSG00000158987; -.
DR PharmGKB; PA134885793; -.
DR VEuPathDB; HostDB:ENSG00000158987; -.
DR eggNOG; KOG3542; Eukaryota.
DR GeneTree; ENSGT00940000158124; -.
DR InParanoid; Q8TEU7; -.
DR OMA; PAYGTCE; -.
DR PhylomeDB; Q8TEU7; -.
DR TreeFam; TF313184; -.
DR PathwayCommons; Q8TEU7; -.
DR SignaLink; Q8TEU7; -.
DR SIGNOR; Q8TEU7; -.
DR BioGRID-ORCS; 51735; 17 hits in 1075 CRISPR screens.
DR ChiTaRS; RAPGEF6; human.
DR EvolutionaryTrace; Q8TEU7; -.
DR GeneWiki; RAPGEF6; -.
DR GenomeRNAi; 51735; -.
DR Pharos; Q8TEU7; Tbio.
DR PRO; PR:Q8TEU7; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8TEU7; protein.
DR Bgee; ENSG00000158987; Expressed in corpus callosum and 189 other tissues.
DR ExpressionAtlas; Q8TEU7; baseline and differential.
DR Genevisible; Q8TEU7; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030742; F:GTP-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0030033; P:microvillus assembly; IGI:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; NAS:UniProtKB.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1601
FT /note="Rap guanine nucleotide exchange factor 6"
FT /id="PRO_0000068876"
FT DOMAIN 412..526
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 530..615
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143,
FT ECO:0000305"
FT DOMAIN 749..835
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 860..1088
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1571..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 280..399
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 747
FT /note="D -> AVGFYY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11524421"
FT /id="VSP_050607"
FT VAR_SEQ 828..1601
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045027"
FT VAR_SEQ 1067
FT /note="R -> RKKRWRSLG (in isoform 3, isoform 4 and isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:11524421,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_050608"
FT VAR_SEQ 1249..1391
FT /note="GYTLIPSAKSDNLSDSSHSEISSRSSIVSNCSVDSMSAALQDERCSSQALAV
FT PESTGALEKTEHASGIGDHSQHGPGWTLLKPSLIKCLAVSSSVSNEEISQEHIIIEAAD
FT SGRGSWTSCSSSSHDNFQSLPNPKSWDFLNSY -> VGSIISDHSSKISGQSCPGIGGA
FT YLQKKILQITRSTAKRTDSTEKATEENRDRTSCENTTRKRMTSPFRRLRERMLSRERLV
FT NSQKEDTDHNQATESCEKVKDVGSNIKDEKGSAIFNSNSQGNSNTLNCFYTRFKSKRRK
FT TL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12581858"
FT /id="VSP_050610"
FT VAR_SEQ 1392..1601
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12581858"
FT /id="VSP_050611"
FT VAR_SEQ 1489..1593
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11524421,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_050609"
FT VARIANT 570
FT /note="S -> A (in dbSNP:rs3756293)"
FT /id="VAR_057168"
FT VARIANT 594
FT /note="A -> P (in dbSNP:rs34112735)"
FT /id="VAR_057169"
FT VARIANT 1353
FT /note="I -> V (in dbSNP:rs7717835)"
FT /id="VAR_057170"
FT VARIANT 1452
FT /note="Q -> R (in dbSNP:rs1291602)"
FT /evidence="ECO:0000269|PubMed:11524421,
FT ECO:0000269|PubMed:12581858, ECO:0000269|Ref.2"
FT /id="VAR_059793"
FT VARIANT 1559
FT /note="V -> E (in dbSNP:rs1064539)"
FT /id="VAR_057171"
FT CONFLICT 566
FT /note="K -> E (in Ref. 1; AAL79915/AAL79916)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="L -> P (in Ref. 1; AAL79915/AAL79916)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="E -> K (in Ref. 1; AAL79915/AAL79916)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="V -> A (in Ref. 1; AAL79915/AAL79916)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="P -> A (in Ref. 5; AAI42965)"
FT /evidence="ECO:0000305"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:2D93"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:2D93"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:2D93"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:2D93"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:2D93"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2D93"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:2D93"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:2D93"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:2D93"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2D93"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:2D93"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:2D93"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:2D93"
FT STRAND 357..372
FT /evidence="ECO:0007829|PDB:2D93"
FT HELIX 373..379
FT /evidence="ECO:0007829|PDB:2D93"
FT STRAND 1598..1601
FT /evidence="ECO:0007829|PDB:3LNY"
SQ SEQUENCE 1601 AA; 179423 MW; CF4C5407EB61EEE2 CRC64;
MNSPVDPGAR QALRKKPPER TPEDLNTIYS YLHGMEILSN LREHQLRLMS ARARYERYSG
NQVLFCSETI ARCWYILLSG SVLVKGSMVL PPCSFGKQFG GKRGCDCLVL EPSEMIVVEN
AKDNEDSILQ REIPARQSRR RFRKINYKGE RQTITDDVEV NSYLSLPADL TKMHLTENPH
PQVTHVSSSQ SGCSIASDSG SSSLSDIYQA TESEVGDVDL TRLPEGPVDS EDDEEEDEEI
DRTDPLQGRD LVRECLEKEP ADKTDDDIEQ LLEFMHQLPA FANMTMSVRR ELCSVMIFEV
VEQAGAIILE DGQELDSWYV ILNGTVEISH PDGKVENLFM GNSFGITPTL DKQYMHGIVR
TKVDDCQFVC IAQQDYWRIL NHVEKNTHKV EEEGEIVMVH EHRELDRSGT RKGHIVIKAT
PERLIMHLIE EHSIVDPTYI EDFLLTYRTF LESPLDVGIK LLEWFKIDSL RDKVTRIVLL
WVNNHFNDFE GDPAMTRFLE EFEKNLEDTK MNGHLRLLNI ACAAKAKWRQ VVLQKASRES
PLQFSLNGGS EKGFGIFVEG VEPGSKAADS GLKRGDQIME VNGQNFENIT FMKAVEILRN
NTHLALTVKT NIFVFKELLF RTEQEKSGVP HIPKIAEKKS NRHSIQHVPG DIEQTSQEKG
SKKVKANTVS GGRNKIRKIL DKTRFSILPP KLFSDGGLSQ SQDDSIVGTR HCRHSLAIMP
IPGTLSSSSP DLLQPTTSML DFSNPSDIPD QVIRVFKVDQ QSCYIIISKD TTAKEVVFHA
VHEFGLTGAS DTYSLCEVSV TPEGVIKQRR LPDQFSKLAD RIQLNGRYYL KNNMETETLC
SDEDAQELVK ESQLSMLQLS TIEVATQLSM RDFDLFRNIE PTEYIDDLFK LNSKTGNTHL
KRFEDIVNQE TFWVASEILT EANQLKRMKI IKHFIKIALH CRECKNFNSM FAIISGLNLA
SVARLRGTWE KLPSKYEKHL QDLQDIFDPS RNMAKYRNIL SSQSMQPPII PLFPVVKKDM
TFLHEGNDSK VDGLVNFEKL RMISKEIRQV VRMTSANMDP AMMFRQRSLS QGSTNSNMLD
VQGGAHKKRA RRSSLLNAKK LYEDAQMARK VKQYLSSLDV ETDEEKFQMM SLQWEPAYGT
LTKNLSEKRS AKSSEMSPVP MRSAGQTTKA HLHQPHRVSQ VLQVPAVNLH PIRKKGQTKD
PALNTSLPQK VLGTTEEISG KKHTEDTISV ASSLHSSPPA SPQGSPHKGY TLIPSAKSDN
LSDSSHSEIS SRSSIVSNCS VDSMSAALQD ERCSSQALAV PESTGALEKT EHASGIGDHS
QHGPGWTLLK PSLIKCLAVS SSVSNEEISQ EHIIIEAADS GRGSWTSCSS SSHDNFQSLP
NPKSWDFLNS YRHTHLDDPI AEVEPTDSEP YSCSKSCSRT CGQCKGSLER KSWTSSSSLS
DTYEPNYGTV KQRVLESTPA ESSEGLDPKD ATDPVYKTVT SSTEKGLIVY CVTSPKKDDR
YREPPPTPPG YLGISLADLK EGPHTHLKPP DYSVAVQRSK MMHNSLSRLP PASLSSNLVA
CVPSKIVTQP QRHNLQPFHP KLGDVTDADS EADENEQVSA V
