NUP43_HUMAN
ID NUP43_HUMAN Reviewed; 380 AA.
AC Q8NFH3; B4E2F0; Q9H8S0;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Nucleoporin Nup43;
DE AltName: Full=Nup107-160 subcomplex subunit Nup43;
DE AltName: Full=p42;
GN Name=NUP43;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=12196509; DOI=10.1083/jcb.200206106;
RA Cronshaw J.M., Krutchinsky A.N., Zhang W., Chait B.T., Matunis M.J.;
RT "Proteomic analysis of the mammalian nuclear pore complex.";
RL J. Cell Biol. 158:915-927(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 247-380 (ISOFORM 1).
RC TISSUE=Ovarian carcinoma, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [5]
RP IDENTIFICATION IN THE NUP107-160 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=15146057; DOI=10.1091/mbc.e03-12-0878;
RA Loieodice I., Alves A., Rabut G., Van Overbeek M., Ellenberg J.,
RA Sibarita J.-B., Doye V.;
RT "The entire Nup107-160 complex, including three new members, is targeted as
RT one entity to kinetochores in mitosis.";
RL Mol. Biol. Cell 15:3333-3344(2004).
RN [6]
RP FUNCTION OF THE NUP107-160 COMPLEX.
RX PubMed=17363900; DOI=10.1038/sj.emboj.7601642;
RA Zuccolo M., Alves A., Galy V., Bolhy S., Formstecher E., Racine V.,
RA Sibarita J.-B., Fukagawa T., Shiekhattar R., Yen T., Doye V.;
RT "The human Nup107-160 nuclear pore subcomplex contributes to proper
RT kinetochore functions.";
RL EMBO J. 26:1853-1864(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE NUP107-160
RP COMPLEX.
RX PubMed=17360435; DOI=10.1073/pnas.0700058104;
RA Glavy J.S., Krutchinsky A.N., Cristea I.M., Berke I.C., Boehmer T.,
RA Blobel G., Chait B.T.;
RT "Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160
RT subcomplex.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3811-3816(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
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).
CC -!- FUNCTION: Component of the Nup107-160 subcomplex of the nuclear pore
CC complex (NPC). The Nup107-160 subcomplex is required for the assembly
CC of a functional NPC. The Nup107-160 subcomplex is also required for
CC normal kinetochore microtubule attachment, mitotic progression and
CC chromosome segregation. {ECO:0000269|PubMed:17363900}.
CC -!- SUBUNIT: Component of the Nup107-160 subcomplex of the nuclear pore
CC complex (NPC). The Nup107-160 subcomplex includes NUP160, NUP133,
CC NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and SEC13.
CC {ECO:0000269|PubMed:15146057, ECO:0000269|PubMed:17360435}.
CC -!- INTERACTION:
CC Q8NFH3; P54253: ATXN1; NbExp=6; IntAct=EBI-1059321, EBI-930964;
CC Q8NFH3; P54252: ATXN3; NbExp=3; IntAct=EBI-1059321, EBI-946046;
CC Q8NFH3; P55212: CASP6; NbExp=3; IntAct=EBI-1059321, EBI-718729;
CC Q8NFH3; P06307: CCK; NbExp=3; IntAct=EBI-1059321, EBI-6624398;
CC Q8NFH3; P07686: HEXB; NbExp=3; IntAct=EBI-1059321, EBI-7133736;
CC Q8NFH3; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1059321, EBI-21591415;
CC Q8NFH3; Q99497: PARK7; NbExp=3; IntAct=EBI-1059321, EBI-1164361;
CC Q8NFH3; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-1059321, EBI-5280197;
CC Q8NFH3; Q13148: TARDBP; NbExp=3; IntAct=EBI-1059321, EBI-372899;
CC Q8NFH3; P02766: TTR; NbExp=3; IntAct=EBI-1059321, EBI-711909;
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore. Nucleus,
CC nuclear pore complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NFH3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NFH3-2; Sequence=VSP_056167;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14536.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF514997; AAM76708.1; -; mRNA.
DR EMBL; AK023349; BAB14536.1; ALT_INIT; mRNA.
DR EMBL; AK304244; BAG65112.1; -; mRNA.
DR EMBL; AL355312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065028; AAH65028.1; -; mRNA.
DR CCDS; CCDS5218.1; -. [Q8NFH3-1]
DR RefSeq; NP_942590.1; NM_198887.2. [Q8NFH3-1]
DR PDB; 4I79; X-ray; 1.75 A; A/B=1-380.
DR PDB; 5A9Q; EM; 23.00 A; 0/9/I/R=1-380.
DR PDB; 7PEQ; EM; 35.00 A; AI/BI/CI/DI=1-380.
DR PDBsum; 4I79; -.
DR PDBsum; 5A9Q; -.
DR PDBsum; 7PEQ; -.
DR AlphaFoldDB; Q8NFH3; -.
DR SMR; Q8NFH3; -.
DR BioGRID; 131544; 102.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR CORUM; Q8NFH3; -.
DR IntAct; Q8NFH3; 47.
DR MINT; Q8NFH3; -.
DR STRING; 9606.ENSP00000342262; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q8NFH3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NFH3; -.
DR PhosphoSitePlus; Q8NFH3; -.
DR SwissPalm; Q8NFH3; -.
DR BioMuta; NUP43; -.
DR DMDM; 27923819; -.
DR EPD; Q8NFH3; -.
DR jPOST; Q8NFH3; -.
DR MassIVE; Q8NFH3; -.
DR MaxQB; Q8NFH3; -.
DR PaxDb; Q8NFH3; -.
DR PeptideAtlas; Q8NFH3; -.
DR PRIDE; Q8NFH3; -.
DR ProteomicsDB; 5814; -.
DR ProteomicsDB; 73305; -. [Q8NFH3-1]
DR Antibodypedia; 33283; 251 antibodies from 22 providers.
DR DNASU; 348995; -.
DR Ensembl; ENST00000340413.7; ENSP00000342262.2; ENSG00000120253.14. [Q8NFH3-1]
DR Ensembl; ENST00000367404.8; ENSP00000356374.4; ENSG00000120253.14. [Q8NFH3-2]
DR GeneID; 348995; -.
DR KEGG; hsa:348995; -.
DR MANE-Select; ENST00000340413.7; ENSP00000342262.2; NM_198887.3; NP_942590.1.
DR UCSC; uc003qmz.5; human. [Q8NFH3-1]
DR CTD; 348995; -.
DR DisGeNET; 348995; -.
DR GeneCards; NUP43; -.
DR HGNC; HGNC:21182; NUP43.
DR HPA; ENSG00000120253; Low tissue specificity.
DR MIM; 608141; gene.
DR neXtProt; NX_Q8NFH3; -.
DR OpenTargets; ENSG00000120253; -.
DR PharmGKB; PA134930788; -.
DR VEuPathDB; HostDB:ENSG00000120253; -.
DR eggNOG; KOG4714; Eukaryota.
DR GeneTree; ENSGT00390000004803; -.
DR HOGENOM; CLU_060663_1_0_1; -.
DR InParanoid; Q8NFH3; -.
DR OMA; FRHHQNN; -.
DR PhylomeDB; Q8NFH3; -.
DR TreeFam; TF321692; -.
DR PathwayCommons; Q8NFH3; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-HSA-180746; Nuclear import of Rev protein.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC).
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q8NFH3; -.
DR SIGNOR; Q8NFH3; -.
DR BioGRID-ORCS; 348995; 649 hits in 1101 CRISPR screens.
DR ChiTaRS; NUP43; human.
DR GeneWiki; NUP43; -.
DR GenomeRNAi; 348995; -.
DR Pharos; Q8NFH3; Tbio.
DR PRO; PR:Q8NFH3; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8NFH3; protein.
DR Bgee; ENSG00000120253; Expressed in oocyte and 205 other tissues.
DR ExpressionAtlas; Q8NFH3; baseline and differential.
DR Genevisible; Q8NFH3; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; IC:ComplexPortal.
DR GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Centromere; Chromosome; Chromosome partition; Kinetochore; Mitosis;
KW mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; WD repeat.
FT CHAIN 1..380
FT /note="Nucleoporin Nup43"
FT /id="PRO_0000051111"
FT REPEAT 8..57
FT /note="WD 1"
FT REPEAT 72..110
FT /note="WD 2"
FT REPEAT 127..166
FT /note="WD 3"
FT REPEAT 170..208
FT /note="WD 4"
FT REPEAT 215..255
FT /note="WD 5"
FT REPEAT 259..299
FT /note="WD 6"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 168..264
FT /note="DNADSSTLHAVTFLRTPEILTVNSIGQLKIWDFRQQGNEPSQILSLTGDRVP
FT LHCVDRHPNQQHVVATGGQDGMLSIWDVRQGTMPVSLLKAHEAEM -> V (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056167"
FT CONFLICT 247
FT /note="V -> A (in Ref. 2; BAB14536)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 31..48
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 77..92
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:4I79"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:4I79"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:4I79"
SQ SEQUENCE 380 AA; 42151 MW; EE44714B8E5BFB42 CRC64;
MEEIYAKFVS QKISKTRWRP LPPGSLQTAE TFATGSWDNE ENYISLWSIG DFGNLDSDGG
FEGDHQLLCD IRHHGDVMDL QFFDQERIVA ASSTGCVTVF LHHPNNQTLS VNQQWTTAHY
HTGPGSPSYS SAPCTGVVCN NPEIVTVGED GRINLFRADH KEAVRTIDNA DSSTLHAVTF
LRTPEILTVN SIGQLKIWDF RQQGNEPSQI LSLTGDRVPL HCVDRHPNQQ HVVATGGQDG
MLSIWDVRQG TMPVSLLKAH EAEMWEVHFH PSNPEHLFTC SEDGSLWHWD ASTDVPEKSS
LFHQGGRSST FLSHSISNQA NVHQSVISSW LSTDPAKDRI EITSLLPSRS LSVNTLDVLG
PCLVCGTDAE AIYVTRHLFS
