TXND5_HUMAN
ID TXND5_HUMAN Reviewed; 432 AA.
AC Q8NBS9; B2RDM2; Q5TCQ0; Q8ND33; Q8TCT2; Q9BVH9;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Thioredoxin domain-containing protein 5 {ECO:0000250|UniProtKB:Q91W90};
DE EC=1.8.4.- {ECO:0000250|UniProtKB:Q91W90};
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:Q91W90};
DE AltName: Full=Endoplasmic reticulum resident protein 46 {ECO:0000250|UniProtKB:Q91W90};
DE Short=ER protein 46 {ECO:0000250|UniProtKB:Q91W90};
DE Short=ERp46 {ECO:0000250|UniProtKB:Q91W90};
DE AltName: Full=Thioredoxin-like protein p46;
DE Flags: Precursor;
GN Name=TXNDC5 {ECO:0000312|HGNC:HGNC:21073}; Synonyms=TLP46;
GN ORFNames=UNQ364/PRO700 {ECO:0000312|EMBL:AAQ89009.1};
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung;
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 70-432 (ISOFORM 1).
RC TISSUE=Liver;
RA Lo S.L., Nissom P.M., Ong S.E., Choong M.L., Ng S.S., Lim J.W.E.,
RA Liang R.C.M.Y., Ou K., Seow T.K., Chung M.C.M.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-432 (ISOFORM 1).
RC TISSUE=Eye;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-432 (ISOFORMS 1/2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(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].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP STRUCTURE BY NMR OF 322-432.
RG RIKEN structural genomics initiative (RSGI);
RT "The solution structure of the third thioredoxin domain of human
RT thioredoxin domain-containing protein 5.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Protein disulfide isomerase of the endoplasmic reticulum
CC lumen involved in the formation of disulfide bonds in proteins. Can
CC reduce insulin disulfide bonds. {ECO:0000250|UniProtKB:Q91W90}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:Q91W90};
CC -!- INTERACTION:
CC Q8NBS9; Q13162: PRDX4; NbExp=2; IntAct=EBI-2510815, EBI-2211957;
CC Q8NBS9; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2510815, EBI-947187;
CC Q8NBS9-1; O08807: Prdx4; Xeno; NbExp=2; IntAct=EBI-16091651, EBI-494652;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q91W90, ECO:0000255|PROSITE-ProRule:PRU10138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NBS9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NBS9-2; Sequence=VSP_045181;
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01199.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY358646; AAQ89009.1; -; mRNA.
DR EMBL; AK075291; BAC11526.1; -; mRNA.
DR EMBL; AK315598; BAG37969.1; -; mRNA.
DR EMBL; AL023694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL096800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55221.1; -; Genomic_DNA.
DR EMBL; AJ440721; CAD29430.1; -; mRNA.
DR EMBL; BC001199; AAH01199.1; ALT_INIT; mRNA.
DR EMBL; AL834423; CAD39084.1; -; mRNA.
DR CCDS; CCDS4505.1; -. [Q8NBS9-1]
DR CCDS; CCDS47369.1; -. [Q8NBS9-2]
DR RefSeq; NP_001139021.1; NM_001145549.3. [Q8NBS9-2]
DR RefSeq; NP_110437.2; NM_030810.4. [Q8NBS9-1]
DR PDB; 2DIZ; NMR; -; A=323-432.
DR PDB; 3UJ1; X-ray; 2.65 A; A=323-432.
DR PDB; 3UVT; X-ray; 2.00 A; A/B/C/D/E=323-428.
DR PDB; 3WGD; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I=62-170.
DR PDB; 3WGE; X-ray; 0.95 A; A=190-298.
DR PDB; 3WGX; X-ray; 0.92 A; A/B=190-298.
DR PDBsum; 2DIZ; -.
DR PDBsum; 3UJ1; -.
DR PDBsum; 3UVT; -.
DR PDBsum; 3WGD; -.
DR PDBsum; 3WGE; -.
DR PDBsum; 3WGX; -.
DR AlphaFoldDB; Q8NBS9; -.
DR SMR; Q8NBS9; -.
DR BioGRID; 123529; 148.
DR DIP; DIP-53700N; -.
DR IntAct; Q8NBS9; 48.
DR MINT; Q8NBS9; -.
DR STRING; 9606.ENSP00000369081; -.
DR BindingDB; Q8NBS9; -.
DR ChEMBL; CHEMBL4739698; -.
DR GlyGen; Q8NBS9; 6 sites, 5 O-linked glycans (5 sites).
DR iPTMnet; Q8NBS9; -.
DR MetOSite; Q8NBS9; -.
DR PhosphoSitePlus; Q8NBS9; -.
DR SwissPalm; Q8NBS9; -.
DR BioMuta; TXNDC5; -.
DR DMDM; 29839560; -.
DR EPD; Q8NBS9; -.
DR jPOST; Q8NBS9; -.
DR MassIVE; Q8NBS9; -.
DR MaxQB; Q8NBS9; -.
DR PaxDb; Q8NBS9; -.
DR PeptideAtlas; Q8NBS9; -.
DR PRIDE; Q8NBS9; -.
DR ProteomicsDB; 3428; -.
DR ProteomicsDB; 72817; -. [Q8NBS9-1]
DR Antibodypedia; 34993; 565 antibodies from 34 providers.
DR DNASU; 81567; -.
DR Ensembl; ENST00000379757.9; ENSP00000369081.4; ENSG00000239264.9. [Q8NBS9-1]
DR Ensembl; ENST00000473453.2; ENSP00000420784.1; ENSG00000239264.9. [Q8NBS9-2]
DR GeneID; 81567; -.
DR KEGG; hsa:81567; -.
DR MANE-Select; ENST00000379757.9; ENSP00000369081.4; NM_030810.5; NP_110437.2.
DR UCSC; uc003mxv.4; human. [Q8NBS9-1]
DR CTD; 81567; -.
DR DisGeNET; 81567; -.
DR GeneCards; TXNDC5; -.
DR HGNC; HGNC:21073; TXNDC5.
DR HPA; ENSG00000239264; Low tissue specificity.
DR MIM; 616412; gene.
DR neXtProt; NX_Q8NBS9; -.
DR OpenTargets; ENSG00000239264; -.
DR PharmGKB; PA134992492; -.
DR VEuPathDB; HostDB:ENSG00000239264; -.
DR eggNOG; KOG0191; Eukaryota.
DR GeneTree; ENSGT00940000156920; -.
DR HOGENOM; CLU_066321_0_0_1; -.
DR InParanoid; Q8NBS9; -.
DR OMA; TKHQTLC; -.
DR OrthoDB; 522268at2759; -.
DR PhylomeDB; Q8NBS9; -.
DR TreeFam; TF106379; -.
DR BRENDA; 5.3.4.1; 2681.
DR PathwayCommons; Q8NBS9; -.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q8NBS9; -.
DR BioGRID-ORCS; 81567; 9 hits in 1080 CRISPR screens.
DR EvolutionaryTrace; Q8NBS9; -.
DR GeneWiki; TXNDC5; -.
DR GenomeRNAi; 81567; -.
DR Pharos; Q8NBS9; Tbio.
DR PRO; PR:Q8NBS9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8NBS9; protein.
DR Bgee; ENSG00000239264; Expressed in duodenum and 101 other tissues.
DR ExpressionAtlas; Q8NBS9; baseline and differential.
DR Genevisible; Q8NBS9; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISS:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 3.
DR SUPFAM; SSF52833; SSF52833; 3.
DR TIGRFAMs; TIGR01126; pdi_dom; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Endoplasmic reticulum;
KW Isomerase; Oxidoreductase; Redox-active center; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..432
FT /note="Thioredoxin domain-containing protein 5"
FT /id="PRO_0000034183"
FT DOMAIN 36..169
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 170..295
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 304..429
FT /note="Thioredoxin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 40..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 429..432
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT DISULFID 89..92
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 217..220
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 350..353
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045181"
FT CONFLICT 354
FT /note="K -> R (in Ref. 2; BAC11526)"
FT /evidence="ECO:0000305"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:3WGD"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:3WGD"
FT HELIX 90..106
FT /evidence="ECO:0007829|PDB:3WGD"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:3WGD"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3WGD"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:3WGD"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:3WGD"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3WGD"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:3WGD"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:3WGX"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:3WGX"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:3WGX"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:3WGX"
FT HELIX 218..233
FT /evidence="ECO:0007829|PDB:3WGX"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3WGX"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:3WGX"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:3WGX"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:3WGX"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:3WGX"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:3WGX"
FT HELIX 283..294
FT /evidence="ECO:0007829|PDB:3WGX"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:3UVT"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:3UVT"
FT HELIX 332..336
FT /evidence="ECO:0007829|PDB:3UVT"
FT STRAND 337..346
FT /evidence="ECO:0007829|PDB:3UVT"
FT HELIX 351..364
FT /evidence="ECO:0007829|PDB:3UVT"
FT STRAND 374..380
FT /evidence="ECO:0007829|PDB:3UVT"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:3UVT"
FT HELIX 385..390
FT /evidence="ECO:0007829|PDB:3UVT"
FT STRAND 395..403
FT /evidence="ECO:0007829|PDB:3UVT"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:3UVT"
FT HELIX 417..427
FT /evidence="ECO:0007829|PDB:3UVT"
SQ SEQUENCE 432 AA; 47629 MW; 85E398008D6DB98C CRC64;
MPARPGRLLP LLARPAALTA LLLLLLGHGG GGRWGARAQE AAAAAADGPP AADGEDGQDP
HSKHLYTADM FTHGIQSAAH FVMFFAPWCG HCQRLQPTWN DLGDKYNSME DAKVYVAKVD
CTAHSDVCSA QGVRGYPTLK LFKPGQEAVK YQGPRDFQTL ENWMLQTLNE EPVTPEPEVE
PPSAPELKQG LYELSASNFE LHVAQGDHFI KFFAPWCGHC KALAPTWEQL ALGLEHSETV
KIGKVDCTQH YELCSGNQVR GYPTLLWFRD GKKVDQYKGK RDLESLREYV ESQLQRTETG
ATETVTPSEA PVLAAEPEAD KGTVLALTEN NFDDTIAEGI TFIKFYAPWC GHCKTLAPTW
EELSKKEFPG LAGVKIAEVD CTAERNICSK YSVRGYPTLL LFRGGKKVSE HSGGRDLDSL
HRFVLSQAKD EL
