ID   EIF3C_YEAST             Reviewed;         812 AA.
AC   P32497; D6W0D6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   02-SEP-2026, entry version 214.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000255|HAMAP-Rule:MF_03002};
DE            Short=eIF3c {ECO:0000255|HAMAP-Rule:MF_03002};
DE   AltName: Full=Eukaryotic translation initiation factor 3 93 kDa subunit;
DE            Short=eIF3 p93 {ECO:0000255|HAMAP-Rule:MF_03002};
DE   AltName: Full=Nuclear transport protein NIP1;
DE   AltName: Full=Translation initiation factor eIF3, p93 subunit;
GN   Name=NIP1 {ECO:0000255|HAMAP-Rule:MF_03002};
GN   OrderedLocusNames=YMR309C; ORFNames=YM9924.01C, YM9952.11C;
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], AND SUBCELLULAR LOCATION.
RX   PubMed=1332047; DOI=10.1073/pnas.89.21.10355;
RA   Gu Z., Moerschell R.P., Sherman F., Goldfarb D.S.;
RT   "NIP1, a gene required for nuclear transport in yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:10355-10359(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872; DOI=10.1038/387s090;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [3]
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   [4]
RP   IDENTIFICATION IN THE EIF-3 COMPLEX.
RX   PubMed=7798228; DOI=10.1016/s0021-9258(18)31633-8;
RA   Naranda T., MacMillan S.E., Hershey J.W.B.;
RT   "Purified yeast translational initiation factor eIF-3 is an RNA-binding
RT   protein complex that contains the PRT1 protein.";
RL   J. Biol. Chem. 269:32286-32292(1994).
RN   [5]
RP   INTERACTION WITH PRT1, AND ASSOCIATION WITH 40S RIBOSOMES.
RX   PubMed=9722586; DOI=10.1074/jbc.273.36.23485;
RA   Greenberg J.R., Phan L., Gu Z., deSilva A., Apolito C., Sherman F.,
RA   Hinnebusch A.G., Goldfarb D.S.;
RT   "Nip1p associates with 40 S ribosomes and the Prt1p subunit of eukaryotic
RT   initiation factor 3 and is required for efficient translation initiation.";
RL   J. Biol. Chem. 273:23485-23494(1998).
RN   [6]
RP   IDENTIFICATION IN THE EIF-3 CORE COMPLEX, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND INTERACTION WITH TIF5 AND SUI1.
RX   PubMed=9671501; DOI=10.1128/mcb.18.8.4935;
RA   Phan L., Zhang X., Asano K., Anderson J., Vornlocher H.-P., Greenberg J.R.,
RA   Qin J., Hinnebusch A.G.;
RT   "Identification of a translation initiation factor 3 (eIF3) core complex,
RT   conserved in yeast and mammals, that interacts with eIF5.";
RL   Mol. Cell. Biol. 18:4935-4946(1998).
RN   [7]
RP   INTERACTION WITH TIF5.
RX   PubMed=10075937; DOI=10.1093/emboj/18.6.1673;
RA   Asano K., Krishnamoorthy T., Phan L., Pavitt G.D., Hinnebusch A.G.;
RT   "Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-
RT   activating and GDP-GTP exchange factors in translation initiation, mediate
RT   binding to their common substrate eIF2.";
RL   EMBO J. 18:1673-1688(1999).
RN   [8]
RP   FUNCTION, ASSOCIATION WITH THE 40S RIBOSOME, AND INTERACTION WITH RPS0A.
RX   PubMed=12651896; DOI=10.1101/gad.1065403;
RA   Valasek L., Mathew A.A., Shin B.-S., Nielsen K.H., Szamecz B.,
RA   Hinnebusch A.G.;
RT   "The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical
RT   connections with the 40S ribosome in vivo.";
RL   Genes Dev. 17:786-799(2003).
RN   [9]
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   [10]
RP   INTERACTION WITH PRT1, AND ASSOCIATION WITH THE 40S RIBOSOME.
RX   PubMed=16581774; DOI=10.1128/mcb.26.8.2984-2998.2006;
RA   Nielsen K.H., Valasek L., Sykes C., Jivotovskaya A., Hinnebusch A.G.;
RT   "Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of
RT   eukaryotic initiation factor 3 in yeast.";
RL   Mol. Cell. Biol. 26:2984-2998(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-99 AND SER-103, AND
RP   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   [12]
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   [13]
RP   IDENTIFICATION IN THE EIF-3 COMPLEX WITH PRT1; TIF32; TIF34 AND TIF35.
RX   PubMed=18599441; DOI=10.1073/pnas.0801313105;
RA   Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
RA   Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
RA   Doudna J.A., Robinson C.V.;
RT   "Mass spectrometry reveals modularity and a complete subunit interaction
RT   map of the eukaryotic translation factor eIF3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-99 AND SER-103, AND
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).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is involved in protein synthesis of a
CC       specialized repertoire of mRNAs and, together with other initiation
CC       factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC       ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
CC       {ECO:0000255|HAMAP-Rule:MF_03002, ECO:0000269|PubMed:12651896}.
CC   -!- SUBUNIT: The eukaryotic translation initiation factor 3 (eIF-3) core
CC       complex is composed of TIF32, PRT1, NIP1, TIF34 and TIF35. A subcomplex
CC       of TIF32, NIP1 and PRT1 mediates the interaction with eIF-1, TIF5/eIF-5
CC       and HCR1. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-
CC       tRNAi form a multifactor complex (MFC) that may bind to the 40S
CC       ribosome. TIF32, NIP1 and TIF5/eIF-5 comprise a minimal 40S-ribosome-
CC       binding unit. NIP1 interacts with TIF5/eIF-5 and SUI1.
CC       {ECO:0000269|PubMed:10075937, ECO:0000269|PubMed:12651896,
CC       ECO:0000269|PubMed:16581774, ECO:0000269|PubMed:18599441,
CC       ECO:0000269|PubMed:7798228, ECO:0000269|PubMed:9671501,
CC       ECO:0000269|PubMed:9722586}.
CC   -!- INTERACTION:
CC       P32497; P06103: PRT1; NbExp=13; IntAct=EBI-8965, EBI-8973;
CC       P32497; P20433: RPB4; NbExp=5; IntAct=EBI-8965, EBI-15777;
CC       P32497; P38249: RPG1; NbExp=14; IntAct=EBI-8965, EBI-8981;
CC       P32497; P32911: SUI1; NbExp=3; IntAct=EBI-8965, EBI-18527;
CC       P32497; P38431: TIF5; NbExp=6; IntAct=EBI-8965, EBI-9038;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002,
CC       ECO:0000269|PubMed:1332047}. Note=Mainly cytoplasmic.
CC   -!- MISCELLANEOUS: Present with 78900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000255|HAMAP-
CC       Rule:MF_03002}.
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DR   EMBL; L02899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z54141; CAA90827.1; -; Genomic_DNA.
DR   EMBL; Z49212; CAA89142.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10210.1; -; Genomic_DNA.
DR   PIR; A46417; A46417.
DR   RefSeq; NP_014040.1; NM_001182820.1.
DR   PDB; 3JAP; EM; 4.90 A; p=251-812.
DR   PDB; 4U1C; X-ray; 3.50 A; C=247-812.
DR   PDB; 5H7U; NMR; -; A=36-163.
DR   PDB; 6FYX; EM; 3.05 A; q=251-812.
DR   PDB; 6FYY; EM; 3.05 A; q=251-812.
DR   PDB; 6GSM; EM; 5.15 A; q=96-794.
DR   PDB; 6GSN; EM; 5.75 A; q=96-794.
DR   PDB; 6ZCE; EM; 5.30 A; q=1-812.
DR   PDB; 6ZU9; EM; 6.20 A; q=1-812.
DR   PDB; 8CAH; EM; 3.00 A; q=1-812.
DR   PDB; 8CAS; EM; 3.30 A; q=1-812.
DR   PDB; 8S8E; EM; 3.85 A; p=1-812.
DR   PDB; 8S8K; EM; 4.00 A; n=1-812.
DR   AlphaFoldDB; P32497; -.
DR   EMDB; EMD-0057; -.
DR   EMDB; EMD-0058; -.
DR   EMDB; EMD-11160; -.
DR   EMDB; EMD-11439; -.
DR   EMDB; EMD-19802; -.
DR   EMDB; EMD-19808; -.
DR   EMDB; EMD-4327; -.
DR   EMDB; EMD-4328; -.
DR   SMR; P32497; -.
DR   BioGRID; 35489; 301.
DR   ComplexPortal; CPX-1831; Eukaryotic translation initiation factor 3 core complex.
DR   DIP; DIP-1470N; -.
DR   FunCoup; P32497; 1456.
DR   IntAct; P32497; 70.
DR   MINT; P32497; -.
DR   STRING; 4932.YMR309C; -.
DR   iPTMnet; P32497; -.
DR   PaxDb; 4932-YMR309C; -.
DR   PeptideAtlas; P32497; -.
DR   EnsemblFungi; YMR309C_mRNA; YMR309C; YMR309C.
DR   GeneID; 855357; -.
DR   KEGG; sce:YMR309C; -.
DR   AGR; SGD:S000004926; -.
DR   SGD; S000004926; NIP1.
DR   VEuPathDB; FungiDB:YMR309C; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_2_1; -.
DR   InParanoid; P32497; -.
DR   OMA; FRCGLIK; -.
DR   OrthoDB; 29647at2759; -.
DR   BioCyc; YEAST:G3O-32973-MONOMER; -.
DR   Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-SCE-72649; Translation initiation complex formation.
DR   Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR   BioGRID-ORCS; 855357; 8 hits in 10 CRISPR screens.
DR   CD-CODE; E03F929F; Stress granule.
DR   EvolutionaryTrace; P32497; -.
DR   PRO; PR:P32497; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P32497; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:SGD.
DR   GO; GO:0043614; C:multi-eIF complex; IDA:SGD.
DR   GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR   GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR   GO; GO:0031369; F:translation initiation factor binding; IDA:SGD.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006413; P:translational initiation; IDA:ComplexPortal.
DR   HAMAP; MF_03002; eIF3c; 1.
DR   InterPro; IPR027516; EIF3C.
DR   InterPro; IPR008905; EIF3C_N_dom.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR13937; EUKARYOTIC TRANSLATION INITATION FACTOR 3, SUBUNIT 8 EIF3S8 -RELATED; 1.
DR   PANTHER; PTHR13937:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C-RELATED; 1.
DR   Pfam; PF05470; eIF-3c_N; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   PROSITE; PS50250; PCI; 1.
DR   PDBsum; 3JAP; -.
DR   PDBsum; 4U1C; -.
DR   PDBsum; 5H7U; -.
DR   PDBsum; 6FYX; -.
DR   PDBsum; 6FYY; -.
DR   PDBsum; 6GSM; -.
DR   PDBsum; 6GSN; -.
DR   PDBsum; 6ZCE; -.
DR   PDBsum; 6ZU9; -.
DR   PDBsum; 8CAH; -.
DR   PDBsum; 8CAS; -.
DR   PDBsum; 8S8E; -.
DR   PDBsum; 8S8K; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..812
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000123530"
FT   DOMAIN          608..783
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..30
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..64
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         103
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   CONFLICT        111
FT                   /note="V -> D (in Ref. 1; L02899)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        583
FT                   /note="Q -> H (in Ref. 1; L02899)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        641
FT                   /note="K -> N (in Ref. 1; L02899)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        643
FT                   /note="K -> N (in Ref. 1; L02899)"
FT                   /evidence="ECO:0000305"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:5H7U"
FT   HELIX           117..135
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:5H7U"
FT   HELIX           142..158
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           165..179
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           191..205
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           210..213
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           252..266
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   STRAND          267..269
FT                   /evidence="ECO:0007829|PDB:4U1C"
FT   HELIX           272..285
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           289..297
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           300..306
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   STRAND          308..312
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           315..335
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   TURN            336..344
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   TURN            353..355
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   STRAND          361..363
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   TURN            364..368
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           369..386
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   STRAND          389..391
FT                   /evidence="ECO:0007829|PDB:8CAS"
FT   HELIX           392..418
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           422..438
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   TURN            439..442
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           445..458
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   STRAND          469..471
FT                   /evidence="ECO:0007829|PDB:6FYY"
FT   HELIX           479..490
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           497..509
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           510..514
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           517..526
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           531..534
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           538..556
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           560..567
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   TURN            568..572
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           577..580
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   TURN            586..591
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   TURN            596..599
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           600..602
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           608..610
FT                   /evidence="ECO:0007829|PDB:6FYY"
FT   HELIX           611..613
FT                   /evidence="ECO:0007829|PDB:4U1C"
FT   HELIX           614..638
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           652..661
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           671..684
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           688..696
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           698..702
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   STRAND          703..705
FT                   /evidence="ECO:0007829|PDB:6FYY"
FT   HELIX           707..728
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   STRAND          729..732
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   STRAND          733..737
FT                   /evidence="ECO:0007829|PDB:4U1C"
FT   HELIX           738..744
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   HELIX           749..763
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   STRAND          768..770
FT                   /evidence="ECO:0007829|PDB:4U1C"
FT   STRAND          771..773
FT                   /evidence="ECO:0007829|PDB:8CAH"
FT   STRAND          775..777
FT                   /evidence="ECO:0007829|PDB:4U1C"
FT   HELIX           784..793
FT                   /evidence="ECO:0007829|PDB:8CAH"
SQ   SEQUENCE   812 AA;  93204 MW;  EE05097C44C45A4C CRC64;
     MSRFFSSNYE YDVASSSSEE DLLSSSEEDL LSSSSSESEL DQESDDSFFN ESESESEADV
     DSDDSDAKPY GPDWFKKSEF RKQGGGSNKF LKSSNYDSSD EESDEEDGKK VVKSAKEKLL
     DEMQDVYNKI SQAENSDDWL TISNEFDLIS RLLVRAQQQN WGTPNIFIKV VAQVEDAVNN
     TQQADLKNKA VARAYNTTKQ RVKKVSRENE DSMAKFRNDP ESFDKEPTAD LDISANGFTI
     SSSQGNDQAV QEDFFTRLQT IIDSRGKKTV NQQSLISTLE ELLTVAEKPY EFIMAYLTLI
     PSRFDASANL SYQPIDQWKS SFNDISKLLS ILDQTIDTYQ VNEFADPIDF IEDEPKEDSD
     GVKRILGSIF SFVERLDDEF MKSLLNIDPH SSDYLIRLRD EQSIYNLILR TQLYFEATLK
     DEHDLERALT RPFVKRLDHI YYKSENLIKI METAAWNIIP AQFKSKFTSK DQLDSADYVD
     NLIDGLSTIL SKQNNIAVQK RAILYNIYYT ALNKDFQTAK DMLLTSQVQT NINQFDSSLQ
     ILFNRVVVQL GLSAFKLCLI EECHQILNDL LSSSHLREIL GQQSLHRISL NSSNNASADE
     RARQCLPYHQ HINLDLIDVV FLTCSLLIEI PRMTAFYSGI KVKRIPYSPK SIRRSLEHYD
     KLSFQGPPET LRDYVLFAAK SMQKGNWRDS VKYLREIKSW ALLPNMETVL NSLTERVQVE
     SLKTYFFSFK RFYSSFSVAK LAELFDLPEN KVVEVLQSVI AELEIPAKLN DEKTIFVVEK
     GDEITKLEEA MVKLNKEYKI AKERLNPPSN RR
//