BIP1_ARATH
ID BIP1_ARATH Reviewed; 669 AA.
AC Q9LKR3; Q41928; Q56Y82;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Heat shock 70 kDa protein BIP1;
DE AltName: Full=Heat shock 70 kDa protein 11 {ECO:0000303|PubMed:11599561};
DE AltName: Full=Heat shock protein 70-11 {ECO:0000303|PubMed:11599561};
DE Short=AtHsp70-11 {ECO:0000303|PubMed:11599561};
DE AltName: Full=Luminal-binding protein 1;
DE Short=AtBP1 {ECO:0000303|Ref.1};
DE Short=BiP1 {ECO:0000303|PubMed:21909944};
DE Flags: Precursor;
GN Name=BIP1 {ECO:0000303|PubMed:21909944};
GN Synonyms=HSP70-11 {ECO:0000303|PubMed:11599561},
GN MED37_5 {ECO:0000303|PubMed:22021418}, MED37A;
GN OrderedLocusNames=At5g28540 {ECO:0000312|Araport:AT5G28540};
GN ORFNames=T26D3.10 {ECO:0000312|EMBL:AAF88019.1}, T26D3_50;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Koizumi N., Sano H.;
RT "Isolation of two genes encoding luminal binding protein from Arabidopsis
RT thaliana.";
RL (er) Plant Gene Register PGR97-028(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 537-669.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 620-669.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11599561; DOI=10.1379/1466-1268(2001)006<0201:gaoths>2.0.co;2;
RA Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A., Delseny M.;
RT "Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana.";
RL Cell Stress Chaperones 6:201-208(2001).
RN [8]
RP DNAK GENE SUBFAMILY, INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11402207; DOI=10.1104/pp.126.2.789;
RA Sung D.Y., Vierling E., Guy C.L.;
RT "Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene
RT family.";
RL Plant Physiol. 126:789-800(2001).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17560376; DOI=10.1016/j.molcel.2007.05.007;
RA Baeckstroem S., Elfving N., Nilsson R., Wingsle G., Bjoerklund S.;
RT "Purification of a plant mediator from Arabidopsis thaliana identifies PFT1
RT as the Med25 subunit.";
RL Mol. Cell 26:717-729(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [11]
RP INTERACTION WITH ERDJ3B.
RX PubMed=19763086; DOI=10.1038/emboj.2009.262;
RA Nekrasov V., Li J., Batoux M., Roux M., Chu Z.H., Lacombe S., Rougon A.,
RA Bittel P., Kiss-Papp M., Chinchilla D., van Esse H.P., Jorda L.,
RA Schwessinger B., Nicaise V., Thomma B.P., Molina A., Jones J.D., Zipfel C.;
RT "Control of the pattern-recognition receptor EFR by an ER protein complex
RT in plant immunity.";
RL EMBO J. 28:3428-3438(2009).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20080634; DOI=10.1073/pnas.0905795107;
RA Maruyama D., Endo T., Nishikawa S.;
RT "BiP-mediated polar nuclei fusion is essential for the regulation of
RT endosperm nuclei proliferation in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1684-1689(2010).
RN [13]
RP INTERACTION WITH PDIL1-4.
RX PubMed=21909944; DOI=10.1007/s10059-011-0150-3;
RA Cho E.J., Yuen C.Y., Kang B.H., Ondzighi C.A., Staehelin L.A.,
RA Christopher D.A.;
RT "Protein disulfide isomerase-2 of Arabidopsis mediates protein folding and
RT localizes to both the secretory pathway and nucleus, where it interacts
RT with maternal effect embryo arrest factor.";
RL Mol. Cells 32:459-475(2011).
RN [14]
RP NOMENCLATURE.
RX PubMed=22021418; DOI=10.1104/pp.111.188300;
RA Mathur S., Vyas S., Kapoor S., Tyagi A.K.;
RT "The Mediator complex in plants: structure, phylogeny, and expression
RT profiling of representative genes in a dicot (Arabidopsis) and a monocot
RT (rice) during reproduction and abiotic stress.";
RL Plant Physiol. 157:1609-1627(2011).
RN [15]
RP INTERACTION WITH BZIP28, AND SUBCELLULAR LOCATION.
RX PubMed=23624714; DOI=10.1105/tpc.113.110684;
RA Srivastava R., Deng Y., Shah S., Rao A.G., Howell S.H.;
RT "BINDING PROTEIN is a master regulator of the endoplasmic reticulum stress
RT sensor/transducer bZIP28 in Arabidopsis.";
RL Plant Cell 25:1416-1429(2013).
RN [16]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24486762; DOI=10.1093/pcp/pcu018;
RA Maruyama D., Sugiyama T., Endo T., Nishikawa S.;
RT "Multiple BiP genes of Arabidopsis thaliana are required for male
RT gametogenesis and pollen competitiveness.";
RL Plant Cell Physiol. 55:801-810(2014).
RN [17]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH ERDJ3A, AND INDUCTION BY
RP DTT.
RX PubMed=26186593; DOI=10.1371/journal.pone.0132500;
RA Ma Z.X., Leng Y.J., Chen G.X., Zhou P.M., Ye D., Chen L.Q.;
RT "The THERMOSENSITIVE MALE STERILE 1 interacts with the BiPs via DnaJ domain
RT and stimulates their ATPase enzyme activities in Arabidopsis.";
RL PLoS ONE 10:E0132500-E0132500(2015).
RN [18]
RP DISRUPTION PHENOTYPE.
RX PubMed=26251880; DOI=10.1080/15592324.2015.1035853;
RA Maruyama D., Endo T., Nishikawa S.;
RT "BiP3 supports the early stages of female gametogenesis in the absence of
RT BiP1 and BiP2 in Arabidopsis thaliana.";
RL Plant Signal. Behav. 10:E1035853-E1035853(2015).
RN [19]
RP FUNCTION.
RX PubMed=31410484; DOI=10.1093/pcp/pcz158;
RA Maruyama D., Higashiyama T., Endo T., Nishikawa S.I.;
RT "Fertilization-coupled sperm nuclear fusion is required for normal
RT endosperm nuclear proliferation.";
RL Plant Cell Physiol. 61:29-40(2020).
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s are key
CC components that facilitate folding of de novo synthesized proteins,
CC assist translocation of precursor proteins into organelles, and are
CC responsible for degradation of damaged protein under stress conditions
CC (Probable). Involved in polar nuclei fusion during female gametophyte
CC development and is essential for the regulation of endosperm nuclei
CC proliferation (PubMed:20080634). Involved in sperm nuclear fusion with
CC central cell polar nuclei at fertilization, which is critical for
CC normal endosperm nuclear proliferation (PubMed:31410484). Required for
CC pollen development and pollen tube growth (PubMed:24486762). Possesses
CC ATPase activity in vitro (PubMed:26186593).
CC {ECO:0000269|PubMed:20080634, ECO:0000269|PubMed:24486762,
CC ECO:0000269|PubMed:26186593, ECO:0000269|PubMed:31410484,
CC ECO:0000305|PubMed:11402207}.
CC -!- ACTIVITY REGULATION: Binding to ERDJ3A activates the ATPase activity of
CC BIP1. {ECO:0000269|PubMed:26186593}.
CC -!- SUBUNIT: Interacts with ERDJ3B (PubMed:19763086). Interacts with PDIL1-
CC 4 (PubMed:21909944). Interacts with BZIP28 (via C-terminus) in the
CC endoplasmic reticulum (ER) lumen (PubMed:23624714). Under ER stress,
CC BIP1 dissociates from BZIP28, a transcription factor involved in ER
CC stress responses (PubMed:23624714). Interacts with ERDJ3A
CC (PubMed:26186593). {ECO:0000269|PubMed:19763086,
CC ECO:0000269|PubMed:21909944, ECO:0000269|PubMed:23624714,
CC ECO:0000269|PubMed:26186593}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:23624714}. Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in mature pollen grains, and pollen
CC tubes. {ECO:0000269|PubMed:24486762}.
CC -!- DEVELOPMENTAL STAGE: Down-regulated during seed maturation. Up-
CC regulated during germination. {ECO:0000269|PubMed:11402207}.
CC -!- INDUCTION: Induced by heat shock (PubMed:11402207). Induced by DTT
CC (PubMed:26186593). {ECO:0000269|PubMed:11402207,
CC ECO:0000269|PubMed:26186593}.
CC -!- DISRUPTION PHENOTYPE: Bip1 and bip2 double mutation affects the fusion
CC of polar nuclei during female gametophyte development
CC (PubMed:20080634). Bip1 and bip2 double mutation affects pollen tube
CC growth and length (PubMed:24486762). Bip1, bip2 and bip3 triple
CC mutation is pollen lethal (PubMed:24486762). Bip1, bip2 and bip3 triple
CC mutation affects female gametophyte development during the early stages
CC (PubMed:26186593). {ECO:0000269|PubMed:20080634,
CC ECO:0000269|PubMed:24486762, ECO:0000269|PubMed:26186593}.
CC -!- MISCELLANEOUS: Baeckstroem et al identified BIP1 in a Mediator complex
CC pull-down assay and suggested that BIP1 could be a plant specific
CC component of the Mediator complex (PubMed:17560376). However, no
CC experimental evidence has been brought so far to confirm this
CC hypothesis (Probable). {ECO:0000269|PubMed:17560376, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33) family.
CC DnaK subfamily. {ECO:0000305}.
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DR EMBL; D89341; BAA13947.1; -; Genomic_DNA.
DR EMBL; AF262043; AAF88019.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93812.1; -; Genomic_DNA.
DR EMBL; BT000453; AAN17430.1; -; mRNA.
DR EMBL; BT001212; AAN65099.1; -; mRNA.
DR EMBL; AK221441; BAD94482.1; -; mRNA.
DR EMBL; Z17760; CAA79056.1; -; mRNA.
DR RefSeq; NP_198206.1; NM_122737.4.
DR AlphaFoldDB; Q9LKR3; -.
DR SMR; Q9LKR3; -.
DR BioGRID; 18223; 31.
DR IntAct; Q9LKR3; 4.
DR MINT; Q9LKR3; -.
DR STRING; 3702.AT5G28540.1; -.
DR iPTMnet; Q9LKR3; -.
DR MetOSite; Q9LKR3; -.
DR SWISS-2DPAGE; Q9LKR3; -.
DR PaxDb; Q9LKR3; -.
DR PRIDE; Q9LKR3; -.
DR ProteomicsDB; 238329; -.
DR EnsemblPlants; AT5G28540.1; AT5G28540.1; AT5G28540.
DR GeneID; 832950; -.
DR Gramene; AT5G28540.1; AT5G28540.1; AT5G28540.
DR KEGG; ath:AT5G28540; -.
DR Araport; AT5G28540; -.
DR TAIR; locus:2182783; AT5G28540.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; Q9LKR3; -.
DR OMA; DQVHEIV; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; Q9LKR3; -.
DR PRO; PR:Q9LKR3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LKR3; baseline and differential.
DR Genevisible; Q9LKR3; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:TAIR.
DR CDD; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042050; BIP_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Nucleotide-binding; Nucleus;
KW Reference proteome; Signal; Transcription; Transcription regulation.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..669
FT /note="Heat shock 70 kDa protein BIP1"
FT /id="PRO_0000013588"
FT REGION 642..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 666..669
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CONFLICT 215..216
FT /note="YG -> NV (in Ref. 2; BAA13947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 73629 MW; 20F38DA029F3F3F2 CRC64;
MARSFGANST VVLAIIFFGC LFALSSAIEE ATKLGSVIGI DLGTTYSCVG VYKNGHVEII
ANDQGNRITP SWVGFTDSER LIGEAAKNQA AVNPERTVFD VKRLIGRKFE DKEVQKDRKL
VPYQIVNKDG KPYIQVKIKD GETKVFSPEE ISAMILTKMK ETAEAYLGKK IKDAVVTVPA
YFNDAQRQAT KDAGVIAGLN VARIINEPTA AAIAYGLDKK GGEKNILVFD LGGGTFDVSV
LTIDNGVFEV LSTNGDTHLG GEDFDHRVME YFIKLIKKKH QKDISKDNKA LGKLRRECER
AKRALSSQHQ VRVEIESLFD GVDFSEPLTR ARFEELNNDL FRKTMGPVKK AMDDAGLQKS
QIDEIVLVGG STRIPKVQQL LKDFFEGKEP NKGVNPDEAV AYGAAVQGGI LSGEGGDETK
DILLLDVAPL TLGIETVGGV MTKLIPRNTV IPTKKSQVFT TYQDQQTTVS IQVFEGERSL
TKDCRLLGKF DLNGIPPAPR GTPQIEVTFE VDANGILNVK AEDKASGKSE KITITNEKGR
LSQEEIDRMV KEAEEFAEED KKVKEKIDAR NALETYVYNM KNQVNDKDKL ADKLEGDEKE
KIEAATKEAL EWLDENQNSE KEEYDEKLKE VEAVCNPIIT AVYQRSGGAP GGAGGESSTE
EEDESHDEL
