PDIA4_HUMAN
ID PDIA4_HUMAN Reviewed; 645 AA.
AC P13667; A8K4K6; Q549T6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 2.
DT 03-AUG-2022, entry version 228.
DE RecName: Full=Protein disulfide-isomerase A4;
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:P08003};
DE AltName: Full=Endoplasmic reticulum resident protein 70;
DE Short=ER protein 70;
DE Short=ERp70;
DE AltName: Full=Endoplasmic reticulum resident protein 72;
DE Short=ER protein 72;
DE Short=ERp-72;
DE Short=ERp72;
DE Flags: Precursor;
GN Name=PDIA4; Synonyms=ERP70, ERP72;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2549034; DOI=10.1016/s0021-9258(18)63764-0;
RA Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.;
RT "Human deoxycytidine kinase. Sequence of cDNA clones and analysis of
RT expression in cell lines with and without enzyme activity.";
RL J. Biol. Chem. 264:14762-14768(1989).
RN [2]
RP ERRATUM OF PUBMED:2549034, AND SEQUENCE REVISION.
RX PubMed=2002068; DOI=10.1016/s0021-9258(19)67795-1;
RA Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.;
RL J. Biol. Chem. 266:5353-5353(1991).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Muscle;
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 COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein complexes in
RT endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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 [12]
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 [13]
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 [14]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 53-284.
RX PubMed=20600112; DOI=10.1016/j.jmb.2010.06.045;
RA Kozlov G., Azeroual S., Rosenauer A., Maeaettaenen P., Denisov A.Y.,
RA Thomas D.Y., Gehring K.;
RT "Structure of the catalytic a(0)a fragment of the protein disulfide
RT isomerase ERp72.";
RL J. Mol. Biol. 401:618-625(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P08003};
CC -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1
CC and very small amounts of ERP29, but not, or at very low levels, CALR
CC nor CANX. Component of a complex containing at least CRELD2, MANF,
CC MATN3 and PDIA4 (By similarity). {ECO:0000250|UniProtKB:P08003}.
CC -!- INTERACTION:
CC P13667; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1054653, EBI-10171774;
CC P13667; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-1054653, EBI-10210845;
CC P13667; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-1054653, EBI-10302392;
CC P13667; P80188: LCN2; NbExp=3; IntAct=EBI-1054653, EBI-11911016;
CC P13667; O15232: MATN3; NbExp=6; IntAct=EBI-1054653, EBI-6262458;
CC P13667; P23284: PPIB; NbExp=2; IntAct=EBI-1054653, EBI-359252;
CC P13667; PRO_0000025479 [P23284]: PPIB; NbExp=3; IntAct=EBI-1054653, EBI-8771982;
CC P13667; Q76353; Xeno; NbExp=3; IntAct=EBI-1054653, EBI-6248077;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:12643545}. Melanosome
CC {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV (PubMed:17081065).
CC {ECO:0000269|PubMed:17081065}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a deoxycytidine kinase.
CC {ECO:0000305|PubMed:2549034}.
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DR EMBL; J05016; AAA58460.1; -; mRNA.
DR EMBL; AK290971; BAF83660.1; -; mRNA.
DR EMBL; AC093743; AAQ96863.1; -; Genomic_DNA.
DR EMBL; CH471146; EAW80065.1; -; Genomic_DNA.
DR EMBL; CH471146; EAW80066.1; -; Genomic_DNA.
DR EMBL; BC000425; AAH00425.1; -; mRNA.
DR EMBL; BC001928; AAH01928.1; -; mRNA.
DR EMBL; BC006344; AAH06344.1; -; mRNA.
DR EMBL; BC011754; AAH11754.1; -; mRNA.
DR CCDS; CCDS5893.1; -.
DR PIR; A23723; A23723.
DR RefSeq; NP_004902.1; NM_004911.4.
DR PDB; 3IDV; X-ray; 1.95 A; A=53-284.
DR PDBsum; 3IDV; -.
DR AlphaFoldDB; P13667; -.
DR SMR; P13667; -.
DR BioGRID; 114966; 384.
DR IntAct; P13667; 96.
DR MINT; P13667; -.
DR STRING; 9606.ENSP00000286091; -.
DR BindingDB; P13667; -.
DR ChEMBL; CHEMBL4295717; -.
DR GlyGen; P13667; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P13667; -.
DR MetOSite; P13667; -.
DR PhosphoSitePlus; P13667; -.
DR SwissPalm; P13667; -.
DR BioMuta; PDIA4; -.
DR DMDM; 119530; -.
DR OGP; P13667; -.
DR REPRODUCTION-2DPAGE; IPI00009904; -.
DR CPTAC; CPTAC-105; -.
DR CPTAC; CPTAC-106; -.
DR EPD; P13667; -.
DR jPOST; P13667; -.
DR MassIVE; P13667; -.
DR MaxQB; P13667; -.
DR PaxDb; P13667; -.
DR PeptideAtlas; P13667; -.
DR PRIDE; P13667; -.
DR ProteomicsDB; 52955; -.
DR Antibodypedia; 3377; 498 antibodies from 33 providers.
DR DNASU; 9601; -.
DR Ensembl; ENST00000652332.1; ENSP00000499129.1; ENSG00000155660.11.
DR GeneID; 9601; -.
DR KEGG; hsa:9601; -.
DR MANE-Select; ENST00000652332.1; ENSP00000499129.1; NM_004911.5; NP_004902.1.
DR UCSC; uc003wff.3; human.
DR CTD; 9601; -.
DR DisGeNET; 9601; -.
DR GeneCards; PDIA4; -.
DR HGNC; HGNC:30167; PDIA4.
DR HPA; ENSG00000155660; Low tissue specificity.
DR neXtProt; NX_P13667; -.
DR OpenTargets; ENSG00000155660; -.
DR PharmGKB; PA142671190; -.
DR VEuPathDB; HostDB:ENSG00000155660; -.
DR eggNOG; KOG0190; Eukaryota.
DR GeneTree; ENSGT00940000157738; -.
DR HOGENOM; CLU_025879_6_2_1; -.
DR InParanoid; P13667; -.
DR OMA; ISQPNWT; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; P13667; -.
DR TreeFam; TF106382; -.
DR BRENDA; 5.3.4.1; 2681.
DR PathwayCommons; P13667; -.
DR SignaLink; P13667; -.
DR BioGRID-ORCS; 9601; 10 hits in 1077 CRISPR screens.
DR ChiTaRS; PDIA4; human.
DR EvolutionaryTrace; P13667; -.
DR GenomeRNAi; 9601; -.
DR Pharos; P13667; Tbio.
DR PRO; PR:P13667; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P13667; protein.
DR Bgee; ENSG00000155660; Expressed in pylorus and 203 other tissues.
DR ExpressionAtlas; P13667; baseline and differential.
DR Genevisible; P13667; HS.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:ProtInc.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISS:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; TAS:ProtInc.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR CDD; cd03068; PDI_b_ERp72; 1.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR041866; PDIA4_PDI_b.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR017068; Protein_diS-isomerase_A4.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 3.
DR PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
DR SUPFAM; SSF52833; SSF52833; 5.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 3.
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; Acetylation; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Isomerase; Redox-active center; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..645
FT /note="Protein disulfide-isomerase A4"
FT /id="PRO_0000034229"
FT DOMAIN 21..169
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 158..301
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 505..636
FT /note="Thioredoxin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 24..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 91..94
FT /note="CXXC"
FT /evidence="ECO:0000250|UniProtKB:P08003"
FT MOTIF 555..558
FT /note="CXXC"
FT /evidence="ECO:0000250|UniProtKB:P08003"
FT MOTIF 642..645
FT /note="Prevents secretion from ER"
FT COMPBIAS 34..58
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 366
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT DISULFID 91..94
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P08003,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 206..209
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 555..558
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P08003,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
FT VARIANT 173
FT /note="T -> M (in dbSNP:rs2290971)"
FT /id="VAR_052580"
FT CONFLICT 102
FT /note="E -> G (in Ref. 3; BAF83660)"
FT /evidence="ECO:0000305"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3IDV"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3IDV"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3IDV"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:3IDV"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:3IDV"
FT HELIX 92..109
FT /evidence="ECO:0007829|PDB:3IDV"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3IDV"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:3IDV"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:3IDV"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:3IDV"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:3IDV"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:3IDV"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:3IDV"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:3IDV"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:3IDV"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:3IDV"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:3IDV"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:3IDV"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:3IDV"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3IDV"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:3IDV"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:3IDV"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:3IDV"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:3IDV"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:3IDV"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:3IDV"
SQ SEQUENCE 645 AA; 72932 MW; 1919C2AE12CD2684 CRC64;
MRPRKAFLLL LLLGLVQLLA VAGAEGPDED SSNRENAIED EEEEEEEDDD EEEDDLEVKE
ENGVLVLNDA NFDNFVADKD TVLLEFYAPW CGHCKQFAPE YEKIANILKD KDPPIPVAKI
DATSASVLAS RFDVSGYPTI KILKKGQAVD YEGSRTQEEI VAKVREVSQP DWTPPPEVTL
VLTKENFDEV VNDADIILVE FYAPWCGHCK KLAPEYEKAA KELSKRSPPI PLAKVDATAE
TDLAKRFDVS GYPTLKIFRK GRPYDYNGPR EKYGIVDYMI EQSGPPSKEI LTLKQVQEFL
KDGDDVIIIG VFKGESDPAY QQYQDAANNL REDYKFHHTF STEIAKFLKV SQGQLVVMQP
EKFQSKYEPR SHMMDVQGST QDSAIKDFVL KYALPLVGHR KVSNDAKRYT RRPLVVVYYS
VDFSFDYRAA TQFWRSKVLE VAKDFPEYTF AIADEEDYAG EVKDLGLSES GEDVNAAILD
ESGKKFAMEP EEFDSDTLRE FVTAFKKGKL KPVIKSQPVP KNNKGPVKVV VGKTFDSIVM
DPKKDVLIEF YAPWCGHCKQ LEPVYNSLAK KYKGQKGLVI AKMDATANDV PSDRYKVEGF
PTIYFAPSGD KKNPVKFEGG DRDLEHLSKF IEEHATKLSR TKEEL
