NUP1_YEAST
ID NUP1_YEAST Reviewed; 1076 AA.
AC P20676; D6W2F9;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Nucleoporin NUP1;
DE AltName: Full=Nuclear pore protein NUP1;
GN Name=NUP1; OrderedLocusNames=YOR098C; ORFNames=YOR3182C;
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].
RX PubMed=2190694; DOI=10.1016/0092-8674(90)90062-j;
RA Davis L.I., Fink G.R.;
RT "The NUP1 gene encodes an essential component of the yeast nuclear pore
RT complex.";
RL Cell 61:965-978(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
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 INTERACTION WITH KAP122.
RX PubMed=10525531; DOI=10.1083/jcb.147.2.235;
RA Titov A.A., Blobel G.;
RT "The karyopherin Kap122p/Pdr6p imports both subunits of the transcription
RT factor IIA into the nucleus.";
RL J. Cell Biol. 147:235-246(1999).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [7]
RP FUNCTION, AND SRP1 RECYCLING.
RX PubMed=11046143; DOI=10.1128/mcb.20.22.8468-8479.2000;
RA Solsbacher J., Maurer P., Vogel F., Schlenstedt G.;
RT "Nup2p, a yeast nucleoporin, functions in bidirectional transport of
RT importin alpha.";
RL Mol. Cell. Biol. 20:8468-8479(2000).
RN [8]
RP FUNCTION, AND INTERACTION THROUGH FG REPEATS.
RX PubMed=11387327; DOI=10.1074/jbc.m102629200;
RA Allen N.P., Huang L., Burlingame A., Rexach M.;
RT "Proteomic analysis of nucleoporin interacting proteins.";
RL J. Biol. Chem. 276:29268-29274(2001).
RN [9]
RP FUNCTION, AND INTERACTION WITH NUP60.
RX PubMed=11535617; DOI=10.1083/jcb.200101007;
RA Denning D.P., Mykytka B., Allen N.P., Huang L., Burlingame A., Rexach M.;
RT "The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p
RT at the nuclear pore complex.";
RL J. Cell Biol. 154:937-950(2001).
RN [10]
RP FUNCTION, AND STRUCTURAL BASIS OF FG REPEAT INTERACTION.
RX PubMed=12372823; DOI=10.1074/jbc.m209037200;
RA Bayliss R., Littlewood T., Strawn L.A., Wente S.R., Stewart M.;
RT "GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta.";
RL J. Biol. Chem. 277:50597-50606(2002).
RN [11]
RP FUNCTION, AND INTERACTION WITH KARYOPHERINS THROUGH FG REPEATS.
RX PubMed=12543930; DOI=10.1074/mcp.t200012-mcp200;
RA Allen N.P., Patel S.S., Huang L., Chalkley R.J., Burlingame A.,
RA Lutzmann M., Hurt E.C., Rexach M.;
RT "Deciphering networks of protein interactions at the nuclear pore
RT complex.";
RL Mol. Cell. Proteomics 1:930-946(2002).
RN [12]
RP FUNCTION, AND IMPORT COMPLEX DISASSEMBLY.
RX PubMed=11867631; DOI=10.1074/jbc.m112306200;
RA Gilchrist D., Mykytka B., Rexach M.;
RT "Accelerating the rate of disassembly of karyopherin-cargo complexes.";
RL J. Biol. Chem. 277:18161-18172(2002).
RN [13]
RP FUNCTION, AND AFFINITY GRADIENT FOR KARYOPHERIN KAP95.
RX PubMed=12917401; DOI=10.1074/jbc.m307135200;
RA Pyhtila B., Rexach M.;
RT "A gradient of affinity for the karyopherin Kap95p along the yeast nuclear
RT pore complex.";
RL J. Biol. Chem. 278:42699-42709(2003).
RN [14]
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 [15]
RP FUNCTION, AND FG REPEAT STRUCTURE.
RX PubMed=12604785; DOI=10.1073/pnas.0437902100;
RA Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M.;
RT "Disorder in the nuclear pore complex: the FG repeat regions of
RT nucleoporins are natively unfolded.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2450-2455(2003).
RN [16]
RP FUNCTION, AND FG REPEATS IN NPC TRANSPORT.
RX PubMed=15039779; DOI=10.1038/ncb1097;
RA Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., Wente S.R.;
RT "Minimal nuclear pore complexes define FG repeat domains essential for
RT transport.";
RL Nat. Cell Biol. 6:197-206(2004).
RN [17]
RP REVIEW.
RX PubMed=12791264; DOI=10.1016/s1534-5807(03)00162-x;
RA Suntharalingam M., Wente S.R.;
RT "Peering through the pore: nuclear pore complex structure, assembly, and
RT function.";
RL Dev. Cell 4:775-789(2003).
RN [18]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; THR-381; SER-383 AND
RP SER-637, AND 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 [21]
RP 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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC).
CC NPC components, collectively referred to as nucleoporins (NUPs), can
CC play the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors. Active directional transport is assured by both, a Phe-Gly
CC (FG) repeat affinity gradient for these transport factors across the
CC NPC and a transport cofactor concentration gradient across the nuclear
CC envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in
CC the nucleus, with GDP in the cytoplasm). As one of the FG repeat
CC nucleoporins NUP1 is involved in interactions with and guidance of
CC nuclear transport receptors such as SRP1-KAP95 (importin alpha and
CC beta) through the NPC. Like the closely related NUP2 it also plays an
CC important role in disassembling and recycling SRP1-KAP95 to the
CC cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1-
CC KAP95-cargo complex in the nucleus, NUP1 binds through its C-terminus
CC to KAP95, thus accelerating the release of KAP95 and, indirectly, of
CC the nuclear localization signal (NLS)-containing cargo from the SRP1-
CC KAP95-cargo complex. {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:11046143, ECO:0000269|PubMed:11387327,
CC ECO:0000269|PubMed:11535617, ECO:0000269|PubMed:11867631,
CC ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:12543930,
CC ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:12917401,
CC ECO:0000269|PubMed:15039779}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). NPC constitutes
CC the exclusive means of nucleocytoplasmic transport. NPCs allow the
CC passive diffusion of ions and small molecules and the active, nuclear
CC transport receptor-mediated bidirectional transport of macromolecules
CC such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal
CC subunits across the nuclear envelope. Due to its 8-fold rotational
CC symmetry, all subunits are present with 8 copies or multiples thereof.
CC Interacts through its FG repeats with nuclear transport receptors.
CC Binds to the nuclear basket of the NPC through NUP60. Interacts with
CC KAP122. {ECO:0000269|PubMed:10525531, ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11535617,
CC ECO:0000269|PubMed:12543930}.
CC -!- INTERACTION:
CC P20676; Q06142: KAP95; NbExp=6; IntAct=EBI-12392, EBI-9145;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane
CC protein; Nucleoplasmic side.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC FG repeat types and their physico-chemical environment change across
CC the NPC from the nucleoplasmic to the cytoplasmic side: FXFG repeats
CC are especially abundant in NUPs on the nucleoplasmic side (in a highly
CC charged environment and enriched in Ser and Thr).
CC -!- PTM: Phosphorylated by CDC28. {ECO:0000305|PubMed:14574415}.
CC -!- MISCELLANEOUS: Present with 468 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M33632; AAA34822.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64020.1; -; Genomic_DNA.
DR EMBL; Z75006; CAA99295.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10875.1; -; Genomic_DNA.
DR PIR; A35622; A35622.
DR RefSeq; NP_014741.1; NM_001183517.1.
DR PDB; 4C31; X-ray; 3.00 A; C/F/X/Y=322-355.
DR PDB; 4MBE; X-ray; 2.61 A; G/H/X/Y=316-340.
DR PDB; 5OWU; X-ray; 2.00 A; B=1-1076.
DR PDBsum; 4C31; -.
DR PDBsum; 4MBE; -.
DR PDBsum; 5OWU; -.
DR AlphaFoldDB; P20676; -.
DR SMR; P20676; -.
DR BioGRID; 34496; 95.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-81N; -.
DR IntAct; P20676; 47.
DR MINT; P20676; -.
DR STRING; 4932.YOR098C; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P20676; -.
DR MaxQB; P20676; -.
DR PaxDb; P20676; -.
DR PRIDE; P20676; -.
DR EnsemblFungi; YOR098C_mRNA; YOR098C; YOR098C.
DR GeneID; 854265; -.
DR KEGG; sce:YOR098C; -.
DR SGD; S000005624; NUP1.
DR VEuPathDB; FungiDB:YOR098C; -.
DR eggNOG; KOG4719; Eukaryota.
DR HOGENOM; CLU_316464_0_0_1; -.
DR InParanoid; P20676; -.
DR OMA; YGTENTE; -.
DR BioCyc; YEAST:G3O-33631-MON; -.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-4570464; SUMOylation of RNA binding proteins.
DR EvolutionaryTrace; P20676; -.
DR PRO; PR:P20676; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P20676; protein.
DR GO; GO:0005635; C:nuclear envelope; IC:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0044613; C:nuclear pore central transport channel; IDA:SGD.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:SGD.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IMP:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR DisProt; DP01075; -.
DR IDEAL; IID50271; -.
DR InterPro; IPR026054; Nucleoporin.
DR PANTHER; PTHR23193; PTHR23193; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Membrane; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1076
FT /note="Nucleoporin NUP1"
FT /id="PRO_0000204902"
FT REPEAT 336..338
FT /note="FXF 1"
FT REPEAT 384..386
FT /note="FXF 2"
FT REPEAT 406..409
FT /note="FXFG 1"
FT REPEAT 422..425
FT /note="FXFG 2"
FT REPEAT 448..451
FT /note="FXFG 3"
FT REPEAT 484..487
FT /note="FXFG 4"
FT REPEAT 510..513
FT /note="FXFG 5"
FT REPEAT 525..528
FT /note="FXFG 6"
FT REPEAT 543..546
FT /note="FXFG 7"
FT REPEAT 571..574
FT /note="FXFG 8"
FT REPEAT 591..593
FT /note="FXF 3"
FT REPEAT 614..616
FT /note="FXF 4"
FT REPEAT 636..638
FT /note="FXF 5"
FT REPEAT 657..659
FT /note="FXF 6"
FT REPEAT 671..674
FT /note="FXFG 9"
FT REPEAT 689..691
FT /note="FXF 7"
FT REPEAT 708..711
FT /note="FXFG 10"
FT REPEAT 727..730
FT /note="FXFG 11"
FT REPEAT 753..755
FT /note="FXF 8"
FT REPEAT 800..803
FT /note="FXFG 12"
FT REPEAT 819..821
FT /note="FXF 9"
FT REPEAT 866..868
FT /note="FXF 10"
FT REPEAT 885..888
FT /note="FXFG 13"
FT REPEAT 929..931
FT /note="FXF 11"
FT REPEAT 1008..1009
FT /note="FG 1"
FT REPEAT 1027..1028
FT /note="FG 2"
FT REPEAT 1038..1039
FT /note="FG 3"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1076
FT /note="Interaction with KAP95"
FT COMPBIAS 143..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 381
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 1004..1007
FT /evidence="ECO:0007829|PDB:5OWU"
FT TURN 1008..1010
FT /evidence="ECO:0007829|PDB:5OWU"
SQ SEQUENCE 1076 AA; 113581 MW; 4AC23567D2FB53CC CRC64;
MSSNTSSVMS SPRVEKRSFS STLKSFFTNP NKKRPSSKKV FSSNLSYANH LEESDVEDTL
HVNKRKRVSG TSQHSDSLTQ NNNNAPIIIY GTENTERPPL LPILPIQRLR LLREKQRVRN
MRELGLIQST EFPSITSSVI LGSQSKSDEG GSYLCTSSTP SPIKNGSCTR QLAGKSGEDT
NVGLPILKSL KNRSNRKRFH SQSKGTVWSA NFEYDLSEYD AIQKKDNKDK EGNAGGDQKT
SENRNNIKSS ISNGNLATGP NLTSEIEDLR ADINSNRLSN PQKNLLLKGP ASTVAKTAPI
QESFVPNSER SGTPTLKKNI EPKKDKESIV LPTVGFDFIK DNETPSKKTS PKATSSAGAV
FKSSVEMGKT DKSTKTAEAP TLSFNFSQKA NKTKAVDNTV PSTTLFNFGG KSDTVTSASQ
PFKFGKTSEK SENHTESDAP PKSTAPIFSF GKQEENGDEG DDENEPKRKR RLPVSEDTNT
KPLFDFGKTG DQKETKKGES EKDASGKPSF VFGASDKQAE GTPLFTFGKK ADVTSNIDSS
AQFTFGKAAT AKETHTKPSE TPATIVKKPT FTFGQSTSEN KISEGSAKPT FSFSKSEEER
KSSPISNEAA KPSFSFPGKP VDVQAPTDDK TLKPTFSFTE PAQKDSSVVS EPKKPSFTFA
SSKTSQPKPL FSFGKSDAAK EPPGSNTSFS FTKPPANETD KRPTPPSFTF GGSTTNNTTT
TSTKPSFSFG APESMKSTAS TAAANTEKLS NGFSFTKFNH NKEKSNSPTS FFDGSASSTP
IPVLGKPTDA TGNTTSKSAF SFGTANTNGT NASANSTSFS FNAPATGNGT TTTSNTSGTN
IAGTFNVGKP DQSIASGNTN GAGSAFGFSS SGTAATGAAS NQSSFNFGNN GAGGLNPFTS
ATSSTNANAG LFNKPPSTNA QNVNVPSAFN FTGNNSTPGG GSVFNMNGNT NANTVFAGSN
NQPHQSQTPS FNTNSSFTPS TVPNINFSGL NGGITNTATN ALRPSDIFGA NAASGSNSNV
TNPSSIFGGA GGVPTTSFGQ PQSAPNQMGM GTNNGMSMGG GVMANRKIAR MRHSKR
