ERP44_HUMAN
ID ERP44_HUMAN Reviewed; 406 AA.
AC Q9BS26; O60319; Q4VXC1; Q5VWZ7; Q6UW14; Q8WX67;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Endoplasmic reticulum resident protein 44;
DE Short=ER protein 44;
DE Short=ERp44;
DE AltName: Full=Thioredoxin domain-containing protein 4;
DE Flags: Precursor;
GN Name=ERP44; Synonyms=KIAA0573, TXNDC4; ORFNames=UNQ532/PRO1075;
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], PROTEIN SEQUENCE OF 149-158 AND 314-327,
RP FUNCTION, INTERACTION WITH ERO1A AND ERO1B, MIXED DISULFIDE BOND FORMATION,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC TISSUE=Cervix;
RX PubMed=11847130; DOI=10.1093/emboj/21.4.835;
RA Anelli T., Alessio M., Mezghrani A., Simmen T., Talamo F., Bachi A.,
RA Sitia R.;
RT "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin
RT family.";
RL EMBO J. 21:835-844(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 FUNCTION.
RX PubMed=14517240; DOI=10.1093/emboj/cdg491;
RA Anelli T., Alessio M., Bachi A., Bergamelli L., Bertoli G., Camerini S.,
RA Mezghrani A., Ruffato E., Simmen T., Sitia R.;
RT "Thiol-mediated protein retention in the endoplasmic reticulum: the role of
RT ERp44.";
RL EMBO J. 22:5015-5022(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=11921445;
RX DOI=10.1002/1615-9861(200203)2:3<288::aid-prot288>3.0.co;2-0;
RA O'Neill E.E., Brock C.J., von Kriegsheim A.F., Pearce A.C., Dwek R.A.,
RA Watson S.P., Hebestreit H.F.;
RT "Towards complete analysis of the platelet proteome.";
RL Proteomics 2:288-305(2002).
RN [9]
RP FUNCTION, INTERACTION WITH ITPR1, AND SUBCELLULAR LOCATION.
RX PubMed=15652484; DOI=10.1016/j.cell.2004.11.048;
RA Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T., Mikoshiba K.;
RT "Subtype-specific and ER lumenal environment-dependent regulation of
RT inositol 1,4,5-trisphosphate receptor type 1 by ERp44.";
RL Cell 120:85-98(2005).
RN [10]
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 [11]
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 [12]
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 [13]
RP FUNCTION, AND INTERACTION WITH ERO1A.
RX PubMed=29858230; DOI=10.15252/embj.201798699;
RA Zhang J., Zhu Q., Wang X., Yu J., Chen X., Wang J., Wang X., Xiao J.,
RA Wang C.C., Wang L.;
RT "Secretory kinase Fam20C tunes endoplasmic reticulum redox state via
RT phosphorylation of Ero1alpha.";
RL EMBO J. 37:0-0(2018).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-406, AND DISULFIDE BONDS.
RX PubMed=18552768; DOI=10.1038/embor.2008.88;
RA Wang L., Wang L., Vavassori S., Li S., Ke H., Anelli T., Degano M.,
RA Ronzoni R., Sitia R., Sun F., Wang C.-C.;
RT "Crystal structure of human ERp44 shows a dynamic functional modulation by
RT its carboxy-terminal tail.";
RL EMBO Rep. 9:642-647(2008).
CC -!- FUNCTION: Mediates thiol-dependent retention in the early secretory
CC pathway, forming mixed disulfides with substrate proteins through its
CC conserved CRFS motif (PubMed:11847130, PubMed:14517240). Inhibits the
CC calcium channel activity of ITPR1 (PubMed:15652484). May have a role in
CC the control of oxidative protein folding in the endoplasmic reticulum
CC (PubMed:11847130, PubMed:29858230, PubMed:14517240). Required to retain
CC ERO1A and ERO1B in the endoplasmic reticulum (PubMed:11847130,
CC PubMed:29858230). {ECO:0000269|PubMed:11847130,
CC ECO:0000269|PubMed:14517240, ECO:0000269|PubMed:15652484,
CC ECO:0000269|PubMed:29858230}.
CC -!- SUBUNIT: Forms mixed disulfides with both ERO1A and ERO1B and cargo
CC folding intermediates; the interactions with ERO1A and ERO1B result in
CC their retention in the endoplasmic reticulum (PubMed:11847130,
CC PubMed:29858230). Directly interacts with ITPR1 in a pH-, redox
CC state- and calcium-dependent manner, but not with ITPR2 or ITPR3
CC (PubMed:15652484). The strength of this interaction inversely
CC correlates with calcium concentration (By similarity).
CC {ECO:0000250|UniProtKB:Q9D1Q6, ECO:0000269|PubMed:11847130,
CC ECO:0000269|PubMed:15652484, ECO:0000269|PubMed:29858230}.
CC -!- INTERACTION:
CC Q9BS26; Q06481-5: APLP2; NbExp=3; IntAct=EBI-541644, EBI-25646567;
CC Q9BS26; P05067: APP; NbExp=3; IntAct=EBI-541644, EBI-77613;
CC Q9BS26; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-541644, EBI-9087876;
CC Q9BS26; P49257: LMAN1; NbExp=3; IntAct=EBI-541644, EBI-1057738;
CC Q9BS26; P07948: LYN; NbExp=3; IntAct=EBI-541644, EBI-79452;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:11847130, ECO:0000269|PubMed:15652484}.
CC -!- INDUCTION: Up-regulated by inducers of the unfolded protein response
CC (UPR), including tunicamycin and dithiothreitol.
CC {ECO:0000269|PubMed:11847130}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25499.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ344330; CAC87611.1; -; mRNA.
DR EMBL; AB011145; BAA25499.1; ALT_INIT; mRNA.
DR EMBL; AY359048; AAQ89407.1; -; mRNA.
DR EMBL; AK075024; BAG52054.1; -; mRNA.
DR EMBL; AL360084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005374; AAH05374.1; -; mRNA.
DR CCDS; CCDS35082.1; -.
DR RefSeq; NP_055866.1; NM_015051.2.
DR PDB; 2R2J; X-ray; 2.60 A; A=30-406.
DR PDB; 5GU6; X-ray; 2.00 A; A=30-402.
DR PDB; 5GU7; X-ray; 2.05 A; C=30-402.
DR PDB; 5HQP; X-ray; 2.60 A; C/D=30-406.
DR PDB; 5XWM; X-ray; 2.45 A; A/B/C/D=30-406.
DR PDBsum; 2R2J; -.
DR PDBsum; 5GU6; -.
DR PDBsum; 5GU7; -.
DR PDBsum; 5HQP; -.
DR PDBsum; 5XWM; -.
DR AlphaFoldDB; Q9BS26; -.
DR SMR; Q9BS26; -.
DR BioGRID; 116704; 151.
DR IntAct; Q9BS26; 81.
DR MINT; Q9BS26; -.
DR STRING; 9606.ENSP00000262455; -.
DR GlyGen; Q9BS26; 4 sites, 5 O-linked glycans (4 sites).
DR iPTMnet; Q9BS26; -.
DR MetOSite; Q9BS26; -.
DR PhosphoSitePlus; Q9BS26; -.
DR SwissPalm; Q9BS26; -.
DR BioMuta; ERP44; -.
DR DMDM; 31077035; -.
DR REPRODUCTION-2DPAGE; IPI00401264; -.
DR CPTAC; CPTAC-363; -.
DR CPTAC; CPTAC-364; -.
DR EPD; Q9BS26; -.
DR jPOST; Q9BS26; -.
DR MassIVE; Q9BS26; -.
DR MaxQB; Q9BS26; -.
DR PaxDb; Q9BS26; -.
DR PeptideAtlas; Q9BS26; -.
DR PRIDE; Q9BS26; -.
DR ProteomicsDB; 78861; -.
DR Antibodypedia; 753; 325 antibodies from 34 providers.
DR DNASU; 23071; -.
DR Ensembl; ENST00000262455.7; ENSP00000262455.6; ENSG00000023318.9.
DR GeneID; 23071; -.
DR KEGG; hsa:23071; -.
DR MANE-Select; ENST00000262455.7; ENSP00000262455.6; NM_015051.3; NP_055866.1.
DR UCSC; uc004bam.4; human.
DR CTD; 23071; -.
DR DisGeNET; 23071; -.
DR GeneCards; ERP44; -.
DR HGNC; HGNC:18311; ERP44.
DR HPA; ENSG00000023318; Low tissue specificity.
DR MIM; 609170; gene.
DR neXtProt; NX_Q9BS26; -.
DR OpenTargets; ENSG00000023318; -.
DR PharmGKB; PA164719295; -.
DR VEuPathDB; HostDB:ENSG00000023318; -.
DR eggNOG; KOG0912; Eukaryota.
DR GeneTree; ENSGT00930000151031; -.
DR HOGENOM; CLU_054449_1_0_1; -.
DR InParanoid; Q9BS26; -.
DR OMA; IGKLGPC; -.
DR OrthoDB; 623253at2759; -.
DR PhylomeDB; Q9BS26; -.
DR TreeFam; TF106378; -.
DR PathwayCommons; Q9BS26; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9BS26; -.
DR SIGNOR; Q9BS26; -.
DR BioGRID-ORCS; 23071; 31 hits in 1084 CRISPR screens.
DR ChiTaRS; ERP44; human.
DR EvolutionaryTrace; Q9BS26; -.
DR GeneWiki; ERP44; -.
DR GenomeRNAi; 23071; -.
DR Pharos; Q9BS26; Tbio.
DR PRO; PR:Q9BS26; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9BS26; protein.
DR Bgee; ENSG00000023318; Expressed in type B pancreatic cell and 214 other tissues.
DR ExpressionAtlas; Q9BS26; baseline and differential.
DR Genevisible; Q9BS26; HS.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; TAS:UniProtKB.
DR GO; GO:0009100; P:glycoprotein metabolic process; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IDA:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IDA:UniProtKB.
DR CDD; cd03072; PDI_b'_ERp44; 1.
DR CDD; cd03070; PDI_b_ERp44; 1.
DR DisProt; DP02173; -.
DR InterPro; IPR041862; ERp44_PDI_b.
DR InterPro; IPR041870; ERp44_PDI_b.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 3.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Reference proteome; Signal; Stress response.
FT SIGNAL 1..29
FT CHAIN 30..406
FT /note="Endoplasmic reticulum resident protein 44"
FT /id="PRO_0000034180"
FT DOMAIN 30..138
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 236..285
FT /note="Interaction with ITPR1"
FT /evidence="ECO:0000250"
FT REGION 360..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 403..406
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 373..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 58
FT /note="Interchain (with ERO1A)"
FT /evidence="ECO:0000269|PubMed:18552768"
FT DISULFID 189..241
FT /evidence="ECO:0000269|PubMed:18552768"
FT DISULFID 301..318
FT /evidence="ECO:0000269|PubMed:18552768"
FT CONFLICT 35
FT /note="D -> A (in Ref. 3; AAQ89407)"
FT /evidence="ECO:0000305"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:5GU6"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 59..78
FT /evidence="ECO:0007829|PDB:5GU6"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:5HQP"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:5GU6"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:5GU7"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2R2J"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:5HQP"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:5GU6"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 230..241
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:5GU6"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:5GU6"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:5GU6"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 305..310
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 343..352
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:5GU6"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:5GU6"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:5GU6"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:5GU6"
SQ SEQUENCE 406 AA; 46971 MW; 3865DCF3811BC263 CRC64;
MHPAVFLSLP DLRCSLLLLV TWVFTPVTTE ITSLDTENID EILNNADVAL VNFYADWCRF
SQMLHPIFEE ASDVIKEEFP NENQVVFARV DCDQHSDIAQ RYRISKYPTL KLFRNGMMMK
REYRGQRSVK ALADYIRQQK SDPIQEIRDL AEITTLDRSK RNIIGYFEQK DSDNYRVFER
VANILHDDCA FLSAFGDVSK PERYSGDNII YKPPGHSAPD MVYLGAMTNF DVTYNWIQDK
CVPLVREITF ENGEELTEEG LPFLILFHMK EDTESLEIFQ NEVARQLISE KGTINFLHAD
CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFKDVLI PGKLKQFVFD LHSGKLHREF
HHGPDPTDTA PGEQAQDVAS SPPESSFQKL APSEYRYTLL RDRDEL
