ID GSO2_ARATH Reviewed; 1252 AA.
AC Q9FIZ3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 27-MAR-2024, entry version 161.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase GSO2 {ECO:0000303|PubMed:18088309};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein EMBRYO SAC DEVELOPMENT ARREST 23 {ECO:0000303|PubMed:15634699};
DE AltName: Full=Protein GASSHO 2 {ECO:0000303|PubMed:18088309};
DE Flags: Precursor;
GN Name=GSO2 {ECO:0000303|PubMed:18088309};
GN Synonyms=EDA23 {ECO:0000303|PubMed:15634699};
GN OrderedLocusNames=At5g44700 {ECO:0000312|Araport:AT5G44700};
GN ORFNames=K23L20.3 {ECO:0000312|EMBL:BAB08823.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=18088309; DOI=10.1111/j.1365-313x.2007.03395.x;
RA Tsuwamoto R., Fukuoka H., Takahata Y.;
RT "GASSHO1 and GASSHO2 encoding a putative leucine-rich repeat transmembrane-
RT type receptor kinase are essential for the normal development of the
RT epidermal surface in Arabidopsis embryos.";
RL Plant J. 54:30-42(2008).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=24123341; DOI=10.1002/dvdy.24066;
RA Racolta A., Bryan A.C., Tax F.E.;
RT "The receptor-like kinases GSO1 and GSO2 together regulate root growth in
RT Arabidopsis through control of cell division and cell fate specification.";
RL Dev. Dyn. 243:257-278(2014).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH CIF1 AND CIF2.
RX PubMed=28104889; DOI=10.1126/science.aai9057;
RA Nakayama T., Shinohara H., Tanaka M., Baba K., Ogawa-Ohnishi M.,
RA Matsubayashi Y.;
RT "A peptide hormone required for Casparian strip diffusion barrier formation
RT in Arabidopsis roots.";
RL Science 355:284-286(2017).
CC -!- FUNCTION: Together with GSO1, receptor-like serine/threonine-kinase
CC required during the development of the epidermal surface in embryos and
CC cotyledons. Involved in the nuclear division phase of
CC megagametogenesis. In coordination with GSO2, regulates root growth
CC through control of cell division and cell fate specification. Controls
CC seedling root growth by modulating sucrose response after germination
CC (PubMed:24123341). Receptor of the peptide hormones CIF1 and CIF2
CC required for contiguous Casparian strip diffusion barrier formation in
CC roots (PubMed:28104889). {ECO:0000269|PubMed:15634699,
CC ECO:0000269|PubMed:18088309, ECO:0000269|PubMed:24123341,
CC ECO:0000269|PubMed:28104889}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Interacts with CIF1 and CIF2. {ECO:0000269|PubMed:28104889}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:C0LGQ5};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FIZ3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Mostly expressed in siliques, seeds, developing
CC embryos and seedlings, detected in flower buds, but not in roots,
CC leaves or stems. {ECO:0000269|PubMed:18088309}.
CC -!- DEVELOPMENTAL STAGE: In flower buds, localized in pollen grains and the
CC separation layer between the bud and the peduncle. During
CC embryogenesis, uniform expression from the globular embryo to the
CC mature cotyledonary embryo, except in the embryo suspensor. After
CC germination, detected in whole cotyledons and in the hypocotyl.
CC Detected in the aerial tissue of 1-3-day-old seedlings, and in the root
CC epidermis and lateral root cap cells. Within the epidermis, mostly
CC expressed in H cells during the first three days after germination
CC (DAG) and becomes restricted to these H cells in mature roots. In the
CC root apical meristem (RAM), mostly confined to the quiescent center
CC (QC) by six DAG. Mostly observed in the outer layers of the mature root
CC and the RAM, including the QC (PubMed:24123341).
CC {ECO:0000269|PubMed:18088309, ECO:0000269|PubMed:24123341}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype during embryogenesis and
CC seedling development. Arrested at two-nuclear stage and unfused polar
CC nuclei. Gso1 and gso2 double mutants produce slightly contorted seeds,
CC with abnormally shaped embryos and seedlings; adhesion between
CC cotyledons and the peripheral tissue of the endosperm, short hypocotyl,
CC and concave cotyledons sometimes fused, with compressed epidermal
CC cells, endosperm tissue partially adherent to the surface of the
CC cotyledons, and a rough surface. In addition, seedlings of gso1 gso2
CC have also root growth and patterning defects characterized by abnormal
CC numbers of cells in longitudinal files and radial cell layers, as well
CC as aberrant stem cell division planes. Root growth arrest and cell
CC divisions defects are rescued by exogenous application of sucrose, but
CC not patterning defects (PubMed:24123341). The double mutant gso1 gso2
CC exhibits a repeatedly interrupted, discontinuous Casparian strip due to
CC patch-like localization of the CASPs proteins (PubMed:28104889).
CC {ECO:0000269|PubMed:15634699, ECO:0000269|PubMed:18088309,
CC ECO:0000269|PubMed:24123341, ECO:0000269|PubMed:28104889}.
CC -!- MISCELLANEOUS: [Isoform 1]: No experimental confirmation available.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08823.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016874; BAB08823.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95148.1; -; Genomic_DNA.
DR RefSeq; NP_199283.1; NM_123837.3. [Q9FIZ3-1]
DR AlphaFoldDB; Q9FIZ3; -.
DR SMR; Q9FIZ3; -.
DR BioGRID; 19749; 7.
DR STRING; 3702.Q9FIZ3; -.
DR GlyCosmos; Q9FIZ3; 19 sites, No reported glycans.
DR PaxDb; 3702-AT5G44700-1; -.
DR ProteomicsDB; 247183; -. [Q9FIZ3-1]
DR EnsemblPlants; AT5G44700.1; AT5G44700.1; AT5G44700. [Q9FIZ3-1]
DR GeneID; 834499; -.
DR Gramene; AT5G44700.1; AT5G44700.1; AT5G44700. [Q9FIZ3-1]
DR KEGG; ath:AT5G44700; -.
DR Araport; AT5G44700; -.
DR TAIR; AT5G44700; GSO2.
DR eggNOG; ENOG502QRD1; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9FIZ3; -.
DR OMA; VWDWLHA; -.
DR OrthoDB; 1211134at2759; -.
DR PhylomeDB; Q9FIZ3; -.
DR PRO; PR:Q9FIZ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIZ3; baseline and differential.
DR Genevisible; Q9FIZ3; AT.
DR GO; GO:0048226; C:Casparian strip; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0160073; P:Casparian strip assembly; IMP:UniProtKB.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051302; P:regulation of cell division; IMP:UniProtKB.
DR GO; GO:0042659; P:regulation of cell fate specification; IMP:UniProtKB.
DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB.
DR GO; GO:2000067; P:regulation of root morphogenesis; IMP:UniProtKB.
DR GO; GO:0090708; P:specification of plant organ axis polarity; IMP:UniProtKB.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 5.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR PANTHER; PTHR48056:SF66; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 7.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51450; LRR; 22.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane;
KW Cell wall biogenesis/degradation; Developmental protein; Glycoprotein;
KW Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1252
FT /note="LRR receptor-like serine/threonine-protein kinase
FT GSO2"
FT /id="PRO_0000387514"
FT TOPO_DOM 23..876
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 898..1252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 94..118
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 120..143
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 144..166
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 168..190
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 191..215
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 217..239
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 240..263
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 265..286
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 287..310
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 312..335
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 337..360
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 361..384
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 386..408
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 409..433
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 435..456
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 457..480
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 481..504
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 506..528
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 529..552
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 554..575
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 577..599
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 600..622
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 623..648
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 650..670
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 671..695
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 697..719
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT REPEAT 720..743
FT /note="LRR 27"
FT /evidence="ECO:0000255"
FT REPEAT 745..767
FT /note="LRR 28"
FT /evidence="ECO:0000255"
FT REPEAT 768..792
FT /note="LRR 29"
FT /evidence="ECO:0000255"
FT REPEAT 793..816
FT /note="LRR 30"
FT /evidence="ECO:0000255"
FT REPEAT 818..839
FT /note="LRR 31"
FT /evidence="ECO:0000255"
FT DOMAIN 948..1232
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 1079
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 954..962
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 976
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 945
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 1024
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 1066
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 1124
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 1131
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1252 AA; 137532 MW; 426A88D45C2C131A CRC64;
MQQNSVLLAL FFLCFSSGLG SGQPGQRDDL QTLLELKNSF ITNPKEEDVL RDWNSGSPSY
CNWTGVTCGG REIIGLNLSG LGLTGSISPS IGRFNNLIHI DLSSNRLVGP IPTTLSNLSS
SLESLHLFSN LLSGDIPSQL GSLVNLKSLK LGDNELNGTI PETFGNLVNL QMLALASCRL
TGLIPSRFGR LVQLQTLILQ DNELEGPIPA EIGNCTSLAL FAAAFNRLNG SLPAELNRLK
NLQTLNLGDN SFSGEIPSQL GDLVSIQYLN LIGNQLQGLI PKRLTELANL QTLDLSSNNL
TGVIHEEFWR MNQLEFLVLA KNRLSGSLPK TICSNNTSLK QLFLSETQLS GEIPAEISNC
QSLKLLDLSN NTLTGQIPDS LFQLVELTNL YLNNNSLEGT LSSSISNLTN LQEFTLYHNN
LEGKVPKEIG FLGKLEIMYL YENRFSGEMP VEIGNCTRLQ EIDWYGNRLS GEIPSSIGRL
KDLTRLHLRE NELVGNIPAS LGNCHQMTVI DLADNQLSGS IPSSFGFLTA LELFMIYNNS
LQGNLPDSLI NLKNLTRINF SSNKFNGSIS PLCGSSSYLS FDVTENGFEG DIPLELGKST
NLDRLRLGKN QFTGRIPRTF GKISELSLLD ISRNSLSGII PVELGLCKKL THIDLNNNYL
SGVIPTWLGK LPLLGELKLS SNKFVGSLPT EIFSLTNILT LFLDGNSLNG SIPQEIGNLQ
ALNALNLEEN QLSGPLPSTI GKLSKLFELR LSRNALTGEI PVEIGQLQDL QSALDLSYNN
FTGRIPSTIS TLPKLESLDL SHNQLVGEVP GQIGDMKSLG YLNLSYNNLE GKLKKQFSRW
QADAFVGNAG LCGSPLSHCN RAGSKNQRSL SPKTVVIISA ISSLAAIALM VLVIILFFKQ
NHDLFKKVRG GNSAFSSNSS SSQAPLFSNG GAKSDIKWDD IMEATHYLNE EFMIGSGGSG
KVYKAELKNG ETIAVKKILW KDDLMSNKSF NREVKTLGTI RHRHLVKLMG YCSSKADGLN
LLIYEYMANG SVWDWLHANE NTKKKEVLGW ETRLKIALGL AQGVEYLHYD CVPPIVHRDI
KSSNVLLDSN IEAHLGDFGL AKILTGNYDT NTESNTMFAG SYGYIAPEYA YSLKATEKSD
VYSMGIVLME IVTGKMPTEA MFDEETDMVR WVETVLDTPP GSEAREKLID SELKSLLPCE
EEAAYQVLEI ALQCTKSYPQ ERPSSRQASE YLLNVFNNRA ASYREMQTDT DK
//
