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   27-MAR-2024, entry version 175.
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}, MED37_5
GN   {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.Q9LKR3; -.
DR   iPTMnet; Q9LKR3; -.
DR   MetOSite; Q9LKR3; -.
DR   PaxDb; 3702-AT5G28540-1; -.
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; AT5G28540; BIP1.
DR   eggNOG; KOG0100; Eukaryota.
DR   HOGENOM; CLU_005965_2_1_1; -.
DR   InParanoid; Q9LKR3; -.
DR   OMA; VNHERTI; -.
DR   OrthoDB; 143at2759; -.
DR   PhylomeDB; Q9LKR3; -.
DR   PRO; PR:Q9LKR3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LKR3; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
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; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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; 3.30.420.40; -; 2.
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; PTHR45639:SF4; HSC70CB, ISOFORM G; 1.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
DR   SWISS-2DPAGE; Q9LKR3; -.
DR   Genevisible; Q9LKR3; AT.
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
//