HAP2_ARATH
ID HAP2_ARATH Reviewed; 705 AA.
AC F4JP36; Q1AP31; Q2PGG6; Q9T0D9;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Protein HAPLESS 2;
DE AltName: Full=GENERATIVE CELL SPECIFIC 1 {ECO:0000303|PubMed:16378100};
DE Flags: Precursor;
GN Name=HAP2; Synonyms=GCS1 {ECO:0000303|PubMed:16378100};
GN OrderedLocusNames=At4g11720; ORFNames=T5C23;
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 / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia; TISSUE=Pollen;
RX PubMed=17079265; DOI=10.1242/dev.02683;
RA von Besser K., Frank A.C., Johnson M.A., Preuss D.;
RT "Arabidopsis HAP2 (GCS1) is a sperm-specific gene required for pollen tube
RT guidance and fertilization.";
RL Development 133:4761-4769(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia; TISSUE=Flower;
RX PubMed=16378100; DOI=10.1038/ncb1345;
RA Mori T., Kuroiwa H., Higashiyama T., Kuroiwa T.;
RT "GENERATIVE CELL SPECIFIC 1 is essential for angiosperm fertilization.";
RL Nat. Cell Biol. 8:64-71(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
RP IDENTIFICATION.
RX PubMed=15514068; DOI=10.1534/genetics.104.029447;
RA Johnson M.A., von Besser K., Zhou Q., Smith E., Aux G., Patton D.,
RA Levin J.Z., Preuss D.;
RT "Arabidopsis hapless mutations define essential gametophytic functions.";
RL Genetics 168:971-982(2004).
RN [6]
RP FUNCTION, AND DOMAIN.
RX PubMed=20333238; DOI=10.1371/journal.pgen.1000882;
RA Wong J.L., Leydon A.R., Johnson M.A.;
RT "HAP2(GCS1)-dependent gamete fusion requires a positively charged carboxy-
RT terminal domain.";
RL PLoS Genet. 6:E1000882-E1000882(2010).
RN [7]
RP FUNCTION, AND DOMAIN.
RX PubMed=21209845; DOI=10.1371/journal.pone.0015957;
RA Mori T., Hirai M., Kuroiwa T., Miyagishima S.Y.;
RT "The functional domain of GCS1-based gamete fusion resides in the amino
RT terminus in plant and parasite species.";
RL PLoS ONE 5:E15957-E15957(2010).
RN [8]
RP REVIEW.
RX PubMed=20080406; DOI=10.1016/j.tcb.2009.12.007;
RA Wong J.L., Johnson M.A.;
RT "Is HAP2-GCS1 an ancestral gamete fusogen?";
RL Trends Cell Biol. 20:134-141(2010).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23180860; DOI=10.1126/science.1223944;
RA Sprunck S., Rademacher S., Vogler F., Gheyselinck J., Grossniklaus U.,
RA Dresselhaus T.;
RT "Egg cell-secreted EC1 triggers sperm cell activation during double
RT fertilization.";
RL Science 338:1093-1097(2012).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28137780; DOI=10.1083/jcb.201610093;
RA Valansi C., Moi D., Leikina E., Matveev E., Grana M., Chernomordik L.V.,
RA Romero H., Aguilar P.S., Podbilewicz B.;
RT "Arabidopsis HAP2/GCS1 is a gamete fusion protein homologous to somatic and
RT viral fusogens.";
RL J. Cell Biol. 216:571-581(2017).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 24-494, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-226.
RX PubMed=30102690; DOI=10.1371/journal.pbio.2006357;
RA Fedry J., Forcina J., Legrand P., Pehau-Arnaudet G., Haouz A., Johnson M.,
RA Rey F.A., Krey T.;
RT "Evolutionary diversification of the HAP2 membrane insertion motifs to
RT drive gamete fusion across eukaryotes.";
RL PLoS Biol. 16:E2006357-E2006357(2018).
CC -!- FUNCTION: Required for male fertility (PubMed:17079265,
CC PubMed:20333238). Plays a role in pollen tube guidance and successful
CC gamete attachment (PubMed:17079265). Essential for the fusion of
CC gametes during double fertilization, where one male gamete fuses with
CC the egg to produce a zygote, and another male gamete fuses with the
CC central cell to produce the endosperm (PubMed:17079265,
CC PubMed:20333238, PubMed:21209845). Mediates the fusion of cell
CC membranes (PubMed:28137780). Not required for pollen tube outgrowth
CC (PubMed:17079265, PubMed:20333238). {ECO:0000269|PubMed:16378100,
CC ECO:0000269|PubMed:17079265, ECO:0000269|PubMed:20333238,
CC ECO:0000269|PubMed:21209845, ECO:0000269|PubMed:23180860,
CC ECO:0000269|PubMed:28137780}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17079265, ECO:0000305|PubMed:23180860}; Single-pass
CC membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000269|PubMed:16378100, ECO:0000269|PubMed:17079265,
CC ECO:0000269|PubMed:23180860, ECO:0000269|PubMed:28137780}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:28137780}.
CC Note=Predominantly localized in a perinuclear ring (PubMed:17079265).
CC Redistribution to the cell membrane is mediated by EC1 peptides after
CC their secretion upon sperm arrival (PubMed:23180860).
CC {ECO:0000269|PubMed:17079265, ECO:0000269|PubMed:23180860}.
CC -!- TISSUE SPECIFICITY: Expressed only in mature pollen, in the two sperm
CC cells. {ECO:0000269|PubMed:16378100, ECO:0000269|PubMed:17079265}.
CC -!- DEVELOPMENTAL STAGE: Expressed during pollen development and tube
CC growth. {ECO:0000269|PubMed:16378100}.
CC -!- DOMAIN: The N-terminal domain (62-541)and the C-terminal domain (583-
CC 705) are both required for functional gamete fusion. A positive charge,
CC and not a conserved primary amino acid sequence, is required for a
CC functional C-terminal domain. The N-terminal domain may be involved in
CC interactions with another membrane-bound protein on female gametes,
CC while positively charged C-terminus may function through electrostatic
CC interactions with the sperm plasma membrane.
CC {ECO:0000269|PubMed:20333238, ECO:0000269|PubMed:21209845}.
CC -!- DISRUPTION PHENOTYPE: Defective in pollen tube guidance. Prevents
CC gamete interaction and fertilization, resulting in male sterility.
CC {ECO:0000269|PubMed:16378100, ECO:0000269|PubMed:17079265}.
CC -!- MISCELLANEOUS: HAP2/GCS1 family members mediate membrane fusion between
CC gametes in a broad range of eukaryotes, ranging from algae and higher
CC plants to protozoans and cnidaria, suggesting they are derived from an
CC ancestral gamete fusogen. They function similar to viral fusogens, by
CC inserting part of their extracellular domain into the lipid bilayer of
CC an adjoining cell. {ECO:0000303|PubMed:20080406}.
CC -!- SIMILARITY: Belongs to the HAP2/GCS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB39943.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78215.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A wretched tale - Issue 146
CC of January 2013;
CC URL="https://web.expasy.org/spotlight/back_issues/146";
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DR EMBL; DQ022375; AAY51999.1; -; mRNA.
DR EMBL; DQ022676; AAY51998.1; -; Genomic_DNA.
DR EMBL; AB206811; BAE71143.2; -; mRNA.
DR EMBL; AL049500; CAB39943.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161532; CAB78215.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83041.1; -; Genomic_DNA.
DR PIR; T04219; T04219.
DR RefSeq; NP_192909.2; NM_117241.2.
DR PDB; 5OW3; X-ray; 2.75 A; C=24-494.
DR PDBsum; 5OW3; -.
DR AlphaFoldDB; F4JP36; -.
DR SMR; F4JP36; -.
DR STRING; 3702.AT4G11720.1; -.
DR TCDB; 1.N.3.1.1; the hapless2 male gamete fusion factor (fusexin) family.
DR iPTMnet; F4JP36; -.
DR PaxDb; F4JP36; -.
DR PRIDE; F4JP36; -.
DR ProteomicsDB; 247211; -.
DR EnsemblPlants; AT4G11720.1; AT4G11720.1; AT4G11720.
DR GeneID; 826777; -.
DR Gramene; AT4G11720.1; AT4G11720.1; AT4G11720.
DR KEGG; ath:AT4G11720; -.
DR Araport; AT4G11720; -.
DR TAIR; locus:2139772; AT4G11720.
DR eggNOG; ENOG502QREH; Eukaryota.
DR HOGENOM; CLU_022353_1_0_1; -.
DR InParanoid; F4JP36; -.
DR OMA; LERDHND; -.
DR OrthoDB; 1196793at2759; -.
DR PRO; PR:F4JP36; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JP36; baseline and differential.
DR Genevisible; F4JP36; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IMP:UniProtKB.
DR GO; GO:0061936; P:fusion of sperm to egg plasma membrane involved in double fertilization forming a zygote and endosperm; IMP:UniProtKB.
DR GO; GO:0045026; P:plasma membrane fusion; IDA:UniProtKB.
DR GO; GO:0048235; P:pollen sperm cell differentiation; IEP:TAIR.
DR GO; GO:0010183; P:pollen tube guidance; IMP:TAIR.
DR InterPro; IPR040326; HAP2/GCS1.
DR InterPro; IPR018928; HAP2/GCS1_dom.
DR PANTHER; PTHR31764; PTHR31764; 1.
DR Pfam; PF10699; HAP2-GCS1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Fertilization; Glycoprotein; Lipid-binding; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..705
FT /note="Protein HAPLESS 2"
FT /id="PRO_0000416780"
FT TOPO_DOM 25..561
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..705
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 617..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..639
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..684
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:30102690, ECO:0007744|PDB:5OW3"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 36..47
FT /evidence="ECO:0000269|PubMed:30102690,
FT ECO:0007744|PDB:5OW3"
FT DISULFID 125..155
FT /evidence="ECO:0000269|PubMed:30102690,
FT ECO:0007744|PDB:5OW3"
FT DISULFID 137..185
FT /evidence="ECO:0000269|PubMed:30102690,
FT ECO:0007744|PDB:5OW3"
FT DISULFID 156..312
FT /evidence="ECO:0000269|PubMed:30102690,
FT ECO:0007744|PDB:5OW3"
FT DISULFID 158..168
FT /evidence="ECO:0000269|PubMed:30102690,
FT ECO:0007744|PDB:5OW3"
FT DISULFID 295..319
FT /evidence="ECO:0000269|PubMed:30102690,
FT ECO:0007744|PDB:5OW3"
FT DISULFID 432..470
FT /evidence="ECO:0000269|PubMed:30102690,
FT ECO:0007744|PDB:5OW3"
FT CONFLICT 127
FT /note="H -> P (in Ref. 1; AAY51999/AAY51998 and 2;
FT BAE71143)"
FT /evidence="ECO:0000305"
FT STRAND 26..37
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 46..58
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 100..113
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:5OW3"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:5OW3"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 154..164
FT /evidence="ECO:0007829|PDB:5OW3"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 192..204
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:5OW3"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:5OW3"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:5OW3"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:5OW3"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:5OW3"
FT TURN 309..313
FT /evidence="ECO:0007829|PDB:5OW3"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:5OW3"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 372..388
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 393..399
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 424..431
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 467..475
FT /evidence="ECO:0007829|PDB:5OW3"
FT STRAND 477..490
FT /evidence="ECO:0007829|PDB:5OW3"
SQ SEQUENCE 705 AA; 80505 MW; 0D4BEF577DDE6786 CRC64;
MVNAILMACI LAGIFVGMFN EVDGIQILSK SKLEKCEKTS DSGNLNCSTK IVLNLAVPSG
SSGGEASIVA EIVEVEDNSS SNMQTVRIPP VITVNKSAAY ALYDLTYIRD VPYKPQEYHV
TTRKCEHDAG PDIVQICERL RDEKGNVLEQ TQPICCPCGP QRRMPSSCGD IFDKMIKGKA
NTAHCLRFPG DWFHVFGIGQ RSLGFSVRVE LKTGTRVSEV IIGPENRTAT ANDNFLKVNL
IGDFGGYTSI PSFEDFYLVI PREAAEAGQP GSLGANYSMW MLLERVRFTL DGLECNKIGV
GYEAFNTQPN FCSSPYWSCL HNQLWNFRES DINRIDRHQL PLYGLEGRFE RINQHPNAGP
HSFSIGVTET LNTNLMIELR ADDIEYVFQR SPGKIINIAI PTFEALTQFG VAAVIIKNTG
EVEASYSLTF DCSKGVAFVE EQFFIIKPKA VTTRSFKLYP TKDQAAKYIC TAILKDSQFS
EVDRAECQFS TTATVLDNGT QVTNPFQIPE TQPKGFFDSI RILWTKIING LVDFITGDTC
RNKCSSFFDF SCHIQYVCLS WMVMFGLLLA LFPITCLLLW LLHQKGLFDP CYDWWEDHFD
LDHHRRLLPS RADVVNRHHH HHKHRHHHNH HRRTHQRHKH HHGQDDDVLQ KMMLERDHSD
SHYYHQLHRV HKDSKQKQRR RAKHGIVLPR DVHVERQRKQ RLRES
