BNI1_YEAST
ID BNI1_YEAST Reviewed; 1953 AA.
AC P41832; D6W0S3; O13450;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Protein BNI1;
DE AltName: Full=Pointed projection formation protein 3;
DE AltName: Full=Sensitive to high expression protein 5;
DE AltName: Full=Synthetic lethal 39;
GN Name=BNI1; Synonyms=PPF3, SHE5; OrderedLocusNames=YNL271C; ORFNames=N0646;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fares H.F., Pringle J.R.;
RT "Synthetic lethals of CDC12.";
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=7941743; DOI=10.1002/yea.320100503;
RA Yorihuzi T., Ohsumi Y.;
RT "Saccharomyces cerevisiae MATa mutant cells defective in pointed projection
RT formation in response to alpha-factor at high concentrations.";
RL Yeast 10:579-594(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 938.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1553.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740425;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<505::aid-yea932>3.0.co;2-f;
RA Sen-Gupta M., Lyck R., Fleig U., Niedenthal R.K., Hegemann J.H.;
RT "The sequence of a 24,152 bp segment from the left arm of chromosome XIV
RT from Saccharomyces cerevisiae between the BNI1 and the POL2 genes.";
RL Yeast 12:505-514(1996).
RN [6]
RP FUNCTION.
RX PubMed=10085293; DOI=10.1083/jcb.144.5.947;
RA Lee L., Klee S.K., Evangelista M., Boone C., Pellman D.;
RT "Control of mitotic spindle position by the Saccharomyces cerevisiae formin
RT Bni1p.";
RL J. Cell Biol. 144:947-961(1999).
RN [7]
RP FUNCTION, AND TETRAMERIZATION.
RX PubMed=14561409; DOI=10.1016/j.cub.2003.09.057;
RA Zigmond S.H., Evangelista M., Boone C., Yang C., Dar A.C., Sicheri F.,
RA Forkey J., Pring M.;
RT "Formin leaky cap allows elongation in the presence of tight capping
RT proteins.";
RL Curr. Biol. 13:1820-1823(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; SER-1170; SER-1338 AND
RP SER-1344, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311 AND SER-1170, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; SER-1085; SER-1170 AND
RP THR-1918, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1350-1760, AND DIMERIZATION.
RX PubMed=15006353; DOI=10.1016/s0092-8674(04)00210-7;
RA Xu Y., Moseley J.B., Sagot I., Poy F., Pellman D., Goode B.L., Eck M.J.;
RT "Crystal structures of a formin homology-2 domain reveal a tethered dimer
RT architecture.";
RL Cell 116:711-723(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 1327-1769 IN COMPLEX WITH ATP AND
RP ACTIN.
RX PubMed=15635372; DOI=10.1038/nature03251;
RA Otomo T., Tomchick D.R., Otomo C., Panchal S.C., Machius M., Rosen M.K.;
RT "Structural basis of actin filament nucleation and processive capping by a
RT formin homology 2 domain.";
RL Nature 433:488-494(2005).
CC -!- FUNCTION: Required for the assembly of F-actin structures, such as
CC actin cables and stress fibers. Nucleates actin filaments. Binds to the
CC barbed end of the actin filament and acts as leaky capper, slowing both
CC polymerization and depolymerization. Protects the growing actin fiber
CC from tight capping proteins and so increases the time of elongation and
CC the total amount of F-actin. May organize microtubules by mediating
CC spindle positioning and movement in the budding process. Potential
CC target of the RHO family members. {ECO:0000269|PubMed:10085293,
CC ECO:0000269|PubMed:14561409}.
CC -!- SUBUNIT: Homodimer, and possibly also homotetramer. Interacts with PFY1
CC via the FH1 domain and with actin via the FH2 domain.
CC {ECO:0000269|PubMed:15635372}.
CC -!- INTERACTION:
CC P41832; P41832: BNI1; NbExp=3; IntAct=EBI-3692, EBI-3692;
CC P41832; P36006: MYO3; NbExp=3; IntAct=EBI-3692, EBI-11670;
CC P41832; P68139: ACTA1; Xeno; NbExp=2; IntAct=EBI-3692, EBI-3058728;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Cell projection, ruffle membrane.
CC Cytoplasm, cytoskeleton.
CC -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC interaction with the GBD/FH3 domain. This autoinhibition is released
CC upon competitive binding of an activated GTPase. The release of DAD
CC allows the FH2 domain to then nucleate and elongate nonbranched actin
CC filaments (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Each FH2 dimer contains binding sites for 4 actin
CC molecules.
CC -!- MISCELLANEOUS: Present with 166 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000305}.
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DR EMBL; L31766; AAA34455.1; -; Genomic_DNA.
DR EMBL; D38411; BAA22512.1; -; Genomic_DNA.
DR EMBL; Z71546; CAA96178.1; -; Genomic_DNA.
DR EMBL; Z71547; CAA96179.1; -; Genomic_DNA.
DR EMBL; X92494; CAA63225.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10289.2; -; Genomic_DNA.
DR PIR; S63244; S63244.
DR RefSeq; NP_014128.2; NM_001183109.2.
DR PDB; 1UX4; X-ray; 3.30 A; A/B=1352-1765.
DR PDB; 1UX5; X-ray; 2.50 A; A=1350-1760.
DR PDB; 1Y64; X-ray; 3.05 A; B=1327-1769.
DR PDBsum; 1UX4; -.
DR PDBsum; 1UX5; -.
DR PDBsum; 1Y64; -.
DR AlphaFoldDB; P41832; -.
DR SMR; P41832; -.
DR BioGRID; 35569; 462.
DR ComplexPortal; CPX-3188; Polarisome.
DR DIP; DIP-974N; -.
DR IntAct; P41832; 29.
DR MINT; P41832; -.
DR STRING; 4932.YNL271C; -.
DR iPTMnet; P41832; -.
DR MaxQB; P41832; -.
DR PaxDb; P41832; -.
DR PRIDE; P41832; -.
DR EnsemblFungi; YNL271C_mRNA; YNL271C; YNL271C.
DR GeneID; 855450; -.
DR KEGG; sce:YNL271C; -.
DR SGD; S000005215; BNI1.
DR VEuPathDB; FungiDB:YNL271C; -.
DR eggNOG; KOG1922; Eukaryota.
DR GeneTree; ENSGT00940000175034; -.
DR HOGENOM; CLU_001313_1_0_1; -.
DR InParanoid; P41832; -.
DR OMA; ILENRDW; -.
DR BioCyc; YEAST:G3O-33265-MON; -.
DR EvolutionaryTrace; P41832; -.
DR PRO; PR:P41832; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P41832; protein.
DR GO; GO:0005884; C:actin filament; IDA:SGD.
DR GO; GO:0032153; C:cell division site; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0000133; C:polarisome; IDA:SGD.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005522; F:profilin binding; IDA:SGD.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:SGD.
DR GO; GO:0045010; P:actin nucleation; IDA:SGD.
DR GO; GO:0051016; P:barbed-end actin filament capping; IDA:SGD.
DR GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IC:ComplexPortal.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:SGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IC:ComplexPortal.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; IDA:SGD.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IGI:SGD.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:SGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR GO; GO:0006903; P:vesicle targeting; IC:ComplexPortal.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014767; DAD_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..1953
FT /note="Protein BNI1"
FT /id="PRO_0000194899"
FT DOMAIN 174..696
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 1053..1337
FT /note="FH1"
FT DOMAIN 1348..1766
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1792..1826
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 1..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1768..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1809..1844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1872..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 712..807
FT /evidence="ECO:0000255"
FT COILED 864..894
FT /evidence="ECO:0000255"
FT COILED 928..981
FT /evidence="ECO:0000255"
FT COILED 1732..1811
FT /evidence="ECO:0000255"
FT COMPBIAS 312..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1066
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1311
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1821..1835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1876..1896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 1344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 1918
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 938
FT /note="A -> T (in Ref. 3; CAA96178/CAA96179 and 5;
FT CAA63225)"
FT /evidence="ECO:0000305"
FT CONFLICT 1430
FT /note="G -> C (in Ref. 1; AAA34455)"
FT /evidence="ECO:0000305"
FT STRAND 1371..1373
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1378..1388
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1391..1398
FT /evidence="ECO:0007829|PDB:1UX5"
FT STRAND 1400..1402
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1405..1413
FT /evidence="ECO:0007829|PDB:1UX5"
FT TURN 1414..1416
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1423..1432
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1434..1436
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1441..1449
FT /evidence="ECO:0007829|PDB:1UX5"
FT TURN 1450..1452
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1453..1456
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1459..1464
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1468..1471
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1475..1480
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1482..1484
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1494..1496
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1504..1506
FT /evidence="ECO:0007829|PDB:1Y64"
FT HELIX 1509..1516
FT /evidence="ECO:0007829|PDB:1UX5"
FT TURN 1517..1524
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1525..1535
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1538..1560
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1563..1579
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1582..1584
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1591..1596
FT /evidence="ECO:0007829|PDB:1UX5"
FT STRAND 1597..1599
FT /evidence="ECO:0007829|PDB:1UX5"
FT STRAND 1603..1608
FT /evidence="ECO:0007829|PDB:1UX4"
FT HELIX 1609..1620
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1622..1626
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1627..1630
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1632..1637
FT /evidence="ECO:0007829|PDB:1UX5"
FT HELIX 1642..1665
FT /evidence="ECO:0007829|PDB:1UX5"
FT TURN 1667..1669
FT /evidence="ECO:0007829|PDB:1UX5"
FT TURN 1671..1673
FT /evidence="ECO:0007829|PDB:1Y64"
FT HELIX 1680..1715
FT /evidence="ECO:0007829|PDB:1UX5"
FT STRAND 1720..1722
FT /evidence="ECO:0007829|PDB:1Y64"
FT HELIX 1723..1757
FT /evidence="ECO:0007829|PDB:1UX5"
SQ SEQUENCE 1953 AA; 219673 MW; 0C5A9D5280A5858F CRC64;
MLKNSGSKHS NSKESHSNSS SGIFQNLKRL ANSNATNSNT GSPTYASQQQ HSPVGNEVST
SPASSSSFRK LNAPSRSTST EARPLNKKST LNTQNLSQYM NGKLSGDVPV SSQHARSHSM
QSKYSYSKRN SSQASNKLTR QHTGQSHSAS SLLSQGSLTN LSKFTTPDGK IYLEMPSDPY
EVEVLFEDIM YKRNIFQSLS EDKQEALMGY SIEKKWLIVK QDLQNELKKM RANTTSSSTA
SRTSMASDHH PILTANSSLS SPKSVLMTSA SSPTSTVYSN SLNHSTTLSS VGTSTSKGKK
LVSGSLKKQP SLNNIYRGGA ENNTSASTLP GDRTNRPPIH YVQRILADKL TSDEMKDLWV
TLRTEQLDWV DAFIDHQGHI AMANVLMNSI YKTAPRENLT KELLEKENSF FKCFRVLSML
SQGLYEFSTH RLMTDTVAEG LFSTKLATRK MATEIFVCML EKKNKSRFEA VLTSLDKKFR
IGQNLHMIQN FKKMPQYFSH LTLESHLKII QAWLFAVEQT LDGRGKMGSL VGASDEFKNG
GGENAILEYC QWTMVFINHL CSCSDNINQR MLLRTKLENC GILRIMNKIK LLDYDKVIDQ
IELYDNNKLD DFNVKLEANN KAFNVDLHDP LSLLKNLWDI CKGTENEKLL VSLVQHLFLS
SSKLIEENQN SSKLTKQLKL MDSLVTNVSV ASTSDEETNM NMAIQRLYDA MQTDEVARRA
ILESRALTKK LEEIQAERDS LSEKLSKAEH GLVGQLEDEL HERDRILAKN QRVMQQLEAE
LEELKKKHLL EKHQQEVELR KMLTILNSRP EESFNKNEGT RGMNSSLNSS EKANIQKVLQ
DGLSRAKKDY KDDSKKFGMT LQPNKRLKML RMQMENIENE ARQLEMTNFA EFEKDRLEPP
IHIKKPKVKK MKNKDRKPLV KPQEADVNKL NDLRRALAEI QMESNDISKF NVEERVNELF
NEKKSLALKR LKELETKYKG FGIDFNVDEI MDSPKKNTGD VETEEDANYA SLDPKTYQKK
LDEINRITDQ LLDIQTQTEH EIQVEEDGES DLSSSSSDDE SEEIYQDASP TQELRSEHSE
LSSGSGPGSF LDALSQKYGT GQNVTASAAF GENNNGSGIG PLHSKVEKTF MNRLRKSTVS
SAPYLEELTQ KVNKVEPYEQ NEDEGLDKKS LPENSTASAA SAFDKAEKDM RQHVENGKQG
RVVNHEEDKT ADFSAVSKLN NTDGAEDLST QSSVLSSQPP PPPPPPPPVP AKLFGESLEK
EKKSEDDTVK QETTGDSPAP PPPPPPPPPP PMALFGKPKG ETPPPPPLPS VLSSSTDGVI
PPAPPMMPAS QIKSAVTSPL LPQSPSLFEK YPRPHKKLKQ LHWEKLDCTD NSIWGTGKAE
KFADDLYEKG VLADLEKAFA AREIKSLASK RKEDLQKITF LSRDISQQFG INLHMYSSLS
VADLVKKILN CDRDFLQTPS VVEFLSKSEI IEVSVNLARN YAPYSTDWEG VRNLEDAKPP
EKDPNDLQRA DQIYLQLMVN LESYWGSRMR ALTVVTSYER EYNELLAKLR KVDKAVSALQ
ESDNLRNVFN VILAVGNFMN DTSKQAQGFK LSTLQRLTFI KDTTNSMTFL NYVEKIVRLN
YPSFNDFLSE LEPVLDVVKV SIEQLVNDCK DFSQSIVNVE RSVEIGNLSD SSKFHPLDKV
LIKTLPVLPE ARKKGDLLED EVKLTIMEFE SLMHTYGEDS GDKFAKISFF KKFADFINEY
KKAQAQNLAA EEEERLYIKH KKIVEEQQKR AQEKEKQKEN SNSPSSEGNE EDEAEDRRAV
MDKLLEQLKN AGPAKSDPSS ARKRALVRKK YLSEKDNAPQ LLNDLDTEEG SILYSPEAMD
PTADTVIHAE SPTPLATRGV MNTSEDLPSP SKTSALEDQE EISDRARMLL KELRGSDTPV
KQNSILDEHL EKLRARKERS IGEASTGNRL SFK
