ID MIK1_ARATH Reviewed; 1013 AA.
AC Q9M0G7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=MDIS1-interacting receptor like kinase 1 {ECO:0000303|PubMed:26863186};
DE Short=AtMIK1 {ECO:0000303|PubMed:26863186};
DE AltName: Full=Leucine-rich repeat receptor-like protein kinase PXL2 {ECO:0000303|PubMed:17570668};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein PHLOEM INTERCALATED WITH XYLEM-LIKE 2 {ECO:0000303|PubMed:17570668};
DE Flags: Precursor;
GN Name=MIK1 {ECO:0000303|PubMed:26863186};
GN Synonyms=PXL2 {ECO:0000303|PubMed:17570668};
GN OrderedLocusNames=At4g28650 {ECO:0000312|Araport:AT4G28650};
GN ORFNames=T5F17.100 {ECO:0000312|EMBL:CAB81453.1};
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 MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [2]
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 [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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17570668; DOI=10.1016/j.cub.2007.05.049;
RA Fisher K., Turner S.;
RT "PXY, a receptor-like kinase essential for maintaining polarity during
RT plant vascular-tissue development.";
RL Curr. Biol. 17:1061-1066(2007).
RN [5]
RP REVIEW.
RX PubMed=20016993; DOI=10.1007/s00709-009-0095-y;
RA Wang G., Fiers M.;
RT "CLE peptide signaling during plant development.";
RL Protoplasma 240:33-43(2010).
RN [6]
RP FUNCTION, INTERACTION WITH MDIS1 AND LURE1.2, TISSUE SPECIFICITY,
RP PHOSPHORYLATION AT THR-710; THR-741; THR-742; THR-862; SER-864; TYR-879;
RP THR-880 AND THR-992, AND SUBUNIT.
RX PubMed=26863186; DOI=10.1038/nature16975;
RA Wang T., Liang L., Xue Y., Jia P.F., Chen W., Zhang M.X., Wang Y.C.,
RA Li H.J., Yang W.C.;
RT "A receptor heteromer mediates the male perception of female attractants in
RT plants.";
RL Nature 531:241-244(2016).
CC -!- FUNCTION: Involved in the regulation of procambium maintenance and
CC polarity during vascular-tissue development (PubMed:17570668). Involved
CC in the pollen tube perception of the female signal (PubMed:26863186).
CC Phosphorylates MDSI1 (PubMed:26863186). {ECO:0000269|PubMed:17570668,
CC ECO:0000269|PubMed:26863186}.
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:0000305};
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:0000305};
CC -!- SUBUNIT: Homodimer. Interacts with MDIS1 and LURE1.2.
CC {ECO:0000269|PubMed:26863186}.
CC -!- INTERACTION:
CC Q9M0G7; Q9LT96: At5g49770; NbExp=2; IntAct=EBI-16196224, EBI-17123993;
CC Q9M0G7; Q9FL28: FLS2; NbExp=3; IntAct=EBI-16196224, EBI-1799448;
CC Q9M0G7; Q4VP08: LURE1.2; NbExp=4; IntAct=EBI-16196224, EBI-16196186;
CC Q9M0G7; C0LGU7: MDIS1; NbExp=7; IntAct=EBI-16196224, EBI-16196163;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen tubes.
CC {ECO:0000269|PubMed:26863186}.
CC -!- PTM: Autophosphorylation induced by the interaction with LURE1.2.
CC {ECO:0000269|PubMed:26863186}.
CC -!- DISRUPTION PHENOTYPE: Reduced procambial cells number, and adjacent or
CC interspersed xylem and phloem formation. {ECO:0000269|PubMed:17570668}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; FJ708756; ACN59350.1; -; mRNA.
DR EMBL; AL161573; CAB81453.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85518.1; -; Genomic_DNA.
DR PIR; T10659; T10659.
DR RefSeq; NP_194594.1; NM_119007.3.
DR AlphaFoldDB; Q9M0G7; -.
DR SMR; Q9M0G7; -.
DR BioGRID; 14270; 32.
DR DIP; DIP-61969N; -.
DR IntAct; Q9M0G7; 31.
DR STRING; 3702.Q9M0G7; -.
DR GlyCosmos; Q9M0G7; 16 sites, No reported glycans.
DR iPTMnet; Q9M0G7; -.
DR PaxDb; 3702-AT4G28650-1; -.
DR ProteomicsDB; 238290; -.
DR EnsemblPlants; AT4G28650.1; AT4G28650.1; AT4G28650.
DR GeneID; 828983; -.
DR Gramene; AT4G28650.1; AT4G28650.1; AT4G28650.
DR KEGG; ath:AT4G28650; -.
DR Araport; AT4G28650; -.
DR TAIR; AT4G28650; PXL2.
DR eggNOG; ENOG502QPWI; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9M0G7; -.
DR OMA; KESNMIG; -.
DR OrthoDB; 1081233at2759; -.
DR PhylomeDB; Q9M0G7; -.
DR PRO; PR:Q9M0G7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0G7; baseline and differential.
DR Genevisible; Q9M0G7; AT.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:0010183; P:pollen tube guidance; IGI:TAIR.
DR GO; GO:0010067; P:procambium histogenesis; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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:SF26; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 11.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 2.
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 ATP-binding; Cell membrane; Developmental protein; Differentiation;
KW Glycoprotein; Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1013
FT /note="MDIS1-interacting receptor like kinase 1"
FT /id="PRO_0000401293"
FT TOPO_DOM 24..633
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 655..1013
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 70..94
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 95..117
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 119..137
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 139..163
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 164..186
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 187..213
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 215..234
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 235..259
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 260..283
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 284..307
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 308..331
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 333..355
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 357..379
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 381..403
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 405..426
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 427..451
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 453..475
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 477..498
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 499..523
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 525..547
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 548..571
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 573..595
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT DOMAIN 699..983
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 976..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 831
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 705..713
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 728
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 691
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 710
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26863186"
FT MOD_RES 741
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26863186"
FT MOD_RES 742
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26863186"
FT MOD_RES 777
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 818
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 862
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26863186"
FT MOD_RES 864
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26863186"
FT MOD_RES 872
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 879
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26863186"
FT MOD_RES 880
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26863186"
FT MOD_RES 992
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26863186"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1013 AA; 110478 MW; AE52A716DCC26695 CRC64;
MKMKIIVLFL YYCYIGSTSS VLASIDNVNE LSVLLSVKST LVDPLNFLKD WKLSDTSDHC
NWTGVRCNSN GNVEKLDLAG MNLTGKISDS ISQLSSLVSF NISCNGFESL LPKSIPPLKS
IDISQNSFSG SLFLFSNESL GLVHLNASGN NLSGNLTEDL GNLVSLEVLD LRGNFFQGSL
PSSFKNLQKL RFLGLSGNNL TGELPSVLGQ LPSLETAILG YNEFKGPIPP EFGNINSLKY
LDLAIGKLSG EIPSELGKLK SLETLLLYEN NFTGTIPREI GSITTLKVLD FSDNALTGEI
PMEITKLKNL QLLNLMRNKL SGSIPPAISS LAQLQVLELW NNTLSGELPS DLGKNSPLQW
LDVSSNSFSG EIPSTLCNKG NLTKLILFNN TFTGQIPATL STCQSLVRVR MQNNLLNGSI
PIGFGKLEKL QRLELAGNRL SGGIPGDISD SVSLSFIDFS RNQIRSSLPS TILSIHNLQA
FLVADNFISG EVPDQFQDCP SLSNLDLSSN TLTGTIPSSI ASCEKLVSLN LRNNNLTGEI
PRQITTMSAL AVLDLSNNSL TGVLPESIGT SPALELLNVS YNKLTGPVPI NGFLKTINPD
DLRGNSGLCG GVLPPCSKFQ RATSSHSSLH GKRIVAGWLI GIASVLALGI LTIVTRTLYK
KWYSNGFCGD ETASKGEWPW RLMAFHRLGF TASDILACIK ESNMIGMGAT GIVYKAEMSR
SSTVLAVKKL WRSAADIEDG TTGDFVGEVN LLGKLRHRNI VRLLGFLYND KNMMIVYEFM
LNGNLGDAIH GKNAAGRLLV DWVSRYNIAL GVAHGLAYLH HDCHPPVIHR DIKSNNILLD
ANLDARIADF GLARMMARKK ETVSMVAGSY GYIAPEYGYT LKVDEKIDIY SYGVVLLELL
TGRRPLEPEF GESVDIVEWV RRKIRDNISL EEALDPNVGN CRYVQEEMLL VLQIALLCTT
KLPKDRPSMR DVISMLGEAK PRRKSNSNEE NTSRSLAEKH SSVFSTSPVN GLL
//
