ID PYL1_ARATH Reviewed; 221 AA. AC Q8VZS8; Q9FIP6; DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=Abscisic acid receptor PYL1; DE AltName: Full=ABI1-binding protein 6; DE AltName: Full=PYR1-like protein 1; DE AltName: Full=Regulatory components of ABA receptor 9; GN Name=PYL1; Synonyms=RCAR12; OrderedLocusNames=At5g46790; GN ORFNames=MZA15.21; 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 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 [4] RP INTERACTION WITH ABI1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=19874541; DOI=10.1111/j.1365-313x.2009.04054.x; RA Nishimura N., Sarkeshik A., Nito K., Park S.-Y., Wang A., Carvalho P.C., RA Lee S., Caddell D.F., Cutler S.R., Chory J., Yates J.R., Schroeder J.I.; RT "PYR/PYL/RCAR family members are major in-vivo ABI1 protein phosphatase 2C- RT interacting proteins in Arabidopsis."; RL Plant J. 61:290-299(2010). RN [5] RP FUNCTION, AND GENE FAMILY. RX PubMed=19407143; DOI=10.1126/science.1172408; RA Ma Y., Szostkiewicz I., Korte A., Moes D., Yang Y., Christmann A., RA Grill E.; RT "Regulators of PP2C phosphatase activity function as abscisic acid RT sensors."; RL Science 324:1064-1068(2009). RN [6] RP INTERACTION WITH HAB1, GENE FAMILY, AND NOMENCLATURE. RX PubMed=19407142; DOI=10.1126/science.1173041; RA Park S.-Y., Fung P., Nishimura N., Jensen D.R., Fujii H., Zhao Y., RA Lumba S., Santiago J., Rodrigues A., Chow T.F., Alfred S.E., Bonetta D., RA Finkelstein R., Provart N.J., Desveaux D., Rodriguez P.L., McCourt P., RA Zhu J.-K., Schroeder J.I., Volkman B.F., Cutler S.R.; RT "Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family RT of START proteins."; RL Science 324:1068-1071(2009). RN [7] RP FUNCTION, HOMODIMER, AND GENE FAMILY. RX PubMed=21658606; DOI=10.1016/j.molcel.2011.05.011; RA Hao Q., Yin P., Li W., Wang L., Yan C., Lin Z., Wu J.Z., Wang J., Yan S.F., RA Yan N.; RT "The molecular basis of ABA-independent inhibition of PP2Cs by a subclass RT of PYL proteins."; RL Mol. Cell 42:662-672(2011). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [9] RP FUNCTION, AND GENE FAMILY. RX PubMed=23844015; DOI=10.1371/journal.pone.0067477; RA Zhang X., Jiang L., Wang G., Yu L., Zhang Q., Xin Q., Wu W., Gong Z., RA Chen Z.; RT "Structural insights into the abscisic acid stereospecificity by the ABA RT receptors PYR/PYL/RCAR."; RL PLoS ONE 8:E67477-E67477(2013). RN [10] RP MUTAGENESIS OF HIS-87; PHE-88; LYS-90; ILE-111; SER-112 AND ASN-117. RX PubMed=24645846; DOI=10.1111/gtc.12140; RA Nakagawa M., Kagiyama M., Shibata N., Hirano Y., Hakoshima T.; RT "Mechanism of high-affinity abscisic acid binding to PYL9/RCAR1."; RL Genes Cells 19:386-404(2014). RN [11] RP INTERACTION WITH CAR1 AND CAR4, AND SUBCELLULAR LOCATION. RX PubMed=25465408; DOI=10.1105/tpc.114.129973; RA Rodriguez L., Gonzalez-Guzman M., Diaz M., Rodrigues A., RA Izquierdo-Garcia A.C., Peirats-Llobet M., Fernandez M.A., Antoni R., RA Fernandez D., Marquez J.A., Mulet J.M., Albert A., Rodriguez P.L.; RT "C2-domain abscisic acid-related proteins mediate the interaction of RT PYR/PYL/RCAR abscisic acid receptors with the plasma membrane and regulate RT abscisic acid sensitivity in Arabidopsis."; RL Plant Cell 26:4802-4820(2014). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 36-211, DIMERIZATION, INTERACTION RP WITH HAB1; ABI1 AND ABI2, FUNCTION, AND DOMAIN. RX PubMed=19898420; DOI=10.1038/nature08613; RA Melcher K., Ng L.-M., Zhou X.E., Soon F.-F., Xu Y., Suino-Powell K.M., RA Park S.-Y., Weiner J.J., Fujii H., Chinnusamy V., Kovach A., Li J., RA Wang Y., Li J., Peterson F.C., Jensen D.R., Yong E.-L., Volkman B.F., RA Cutler S.R., Zhu J.-K., Xu H.E.; RT "A gate-latch-lock mechanism for hormone signalling by abscisic acid RT receptors."; RL Nature 462:602-608(2009). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 8-211 IN COMPLEX WITH ABSCISIC RP ACID AND PP2C ABI1, INTERACTION WITH ABA AND ABI1, MUTAGENESIS OF HIS-87; RP PHE-88; ILE-111; SER-112; LEU-114; PRO-115; HIS-142; ARG-143; LEU-144; RP PRO-178; ASN-181 AND PHE-189, AND FUNCTION. RX PubMed=19855379; DOI=10.1038/nature08583; RA Miyazono K.-I., Miyakawa T., Sawano Y., Kubota K., Kang H.-J., Asano A., RA Miyauchi Y., Takahashi M., Zhi Y., Fujita Y., Yoshida T., Kodaira K.-S., RA Yamaguchi-Shinozaki K., Tanokura M.; RT "Structural basis of abscisic acid signalling."; RL Nature 462:609-614(2009). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 20-221 IN COMPLEX WITH ABSCISIC RP ACID AND PP2C ABI1, AND FUNCTION. RX PubMed=19893533; DOI=10.1038/nsmb.1730; RA Yin P., Fan H., Hao Q., Yuan X., Wu D., Pang Y., Yan C., Li W., Wang J., RA Yan N.; RT "Structural insights into the mechanism of abscisic acid signaling by PYL RT proteins."; RL Nat. Struct. Mol. Biol. 16:1230-1236(2009). CC -!- FUNCTION: Receptor for abscisic acid (ABA) required for ABA-mediated CC responses such as stomatal closure and germination inhibition. Inhibits CC the activity of group-A protein phosphatases type 2C (PP2Cs) when CC activated by ABA (PubMed:19407143, PubMed:19855379, PubMed:19893533, CC PubMed:19898420, PubMed:23844015, PubMed:21658606). Can be activated by CC both (-)-ABA and (+)-ABA (PubMed:23844015). CC {ECO:0000269|PubMed:19407143, ECO:0000269|PubMed:19855379, CC ECO:0000269|PubMed:19893533, ECO:0000269|PubMed:19898420, CC ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:23844015}. CC -!- SUBUNIT: Homodimer (PubMed:21658606, PubMed:19898420). Binds ABA on one CC subunit only. Interacts with HAB1, ABI1 and ABI2, and possibly with CC other PP2Cs (PubMed:19407142, PubMed:19855379, PubMed:19874541, CC PubMed:19893533, PubMed:19898420). Binds to CARs protein in an ABA- CC independent manner, both at the plasma membrane and in the nucleus. CC Interacts directly with CAR1 and CAR4 (PubMed:25465408). CC {ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:19855379, CC ECO:0000269|PubMed:19874541, ECO:0000269|PubMed:19893533, CC ECO:0000269|PubMed:19898420, ECO:0000269|PubMed:21658606, CC ECO:0000269|PubMed:25465408}. CC -!- INTERACTION: CC Q8VZS8; P49597: ABI1; NbExp=13; IntAct=EBI-2363104, EBI-782526; CC Q8VZS8; O04719-1: ABI2; NbExp=2; IntAct=EBI-2363104, EBI-15803514; CC Q8VZS8; Q9CAJ0: HAB1; NbExp=7; IntAct=EBI-2363104, EBI-2309302; CC Q8VZS8; Q8VZS8: PYL1; NbExp=3; IntAct=EBI-2363104, EBI-2363104; CC Q8VZS8; Q9LVG2: TOE2; NbExp=3; IntAct=EBI-2363104, EBI-4424568; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. Nucleus CC {ECO:0000269|PubMed:25465408}. Cell membrane CC {ECO:0000269|PubMed:25465408}. Note=Localizes at the plasma membrane in CC the presence of a CAR protein (e.g. CAR1 and CAR4). CC {ECO:0000269|PubMed:25465408}. CC -!- DOMAIN: Upon interaction with ABA, the 'latch' and 'gate' loops change CC in conformation leading to a tight dimerization and the creation a CC surface that enables the receptor to dock into and inhibit the PP2C CC active site. {ECO:0000269|PubMed:19898420}. CC -!- MISCELLANEOUS: The synthetic growth inhibitor pyrabactin inhibits ABA- CC binding and subsequent PP2Cs inhibitor properties. CC -!- SIMILARITY: Belongs to the PYR/PYL/RCAR abscisic acid intracellular CC receptor family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB08923.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB016882; BAB08923.1; ALT_INIT; Genomic_DNA. DR EMBL; CP002688; AED95426.1; -; Genomic_DNA. DR EMBL; CP002688; ANM69642.1; -; Genomic_DNA. DR EMBL; AY063877; AAL36233.1; -; mRNA. DR EMBL; AY117328; AAM51403.1; -; mRNA. DR RefSeq; NP_001331305.1; NM_001344698.1. DR RefSeq; NP_199491.2; NM_124049.5. DR PDB; 3JRQ; X-ray; 2.10 A; B=28-210. DR PDB; 3JRS; X-ray; 2.05 A; A/B/C=8-211. DR PDB; 3KAY; X-ray; 2.40 A; A/B=36-211. DR PDB; 3KDJ; X-ray; 1.88 A; A=20-221. DR PDB; 3NEF; X-ray; 2.40 A; A/B=20-221. DR PDB; 3NEG; X-ray; 2.80 A; A/B=20-221. DR PDB; 3NMN; X-ray; 2.15 A; A/C=36-211. DR PDBsum; 3JRQ; -. DR PDBsum; 3JRS; -. DR PDBsum; 3KAY; -. DR PDBsum; 3KDJ; -. DR PDBsum; 3NEF; -. DR PDBsum; 3NEG; -. DR PDBsum; 3NMN; -. DR AlphaFoldDB; Q8VZS8; -. DR SMR; Q8VZS8; -. DR BioGRID; 19970; 8. DR ComplexPortal; CPX-3561; PYL1 ABA receptor complex. DR DIP; DIP-48581N; -. DR IntAct; Q8VZS8; 6. DR MINT; Q8VZS8; -. DR STRING; 3702.Q8VZS8; -. DR BindingDB; Q8VZS8; -. DR iPTMnet; Q8VZS8; -. DR PaxDb; 3702-AT5G46790-1; -. DR ProteomicsDB; 226140; -. DR EnsemblPlants; AT5G46790.1; AT5G46790.1; AT5G46790. DR EnsemblPlants; AT5G46790.2; AT5G46790.2; AT5G46790. DR GeneID; 834722; -. DR Gramene; AT5G46790.1; AT5G46790.1; AT5G46790. DR Gramene; AT5G46790.2; AT5G46790.2; AT5G46790. DR KEGG; ath:AT5G46790; -. DR Araport; AT5G46790; -. DR TAIR; AT5G46790; PYL1. DR eggNOG; ENOG502QW1M; Eukaryota. DR HOGENOM; CLU_077517_0_1_1; -. DR InParanoid; Q8VZS8; -. DR OMA; THHITIP; -. DR OrthoDB; 656543at2759; -. DR PhylomeDB; Q8VZS8; -. DR EvolutionaryTrace; Q8VZS8; -. DR PRO; PR:Q8VZS8; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q8VZS8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009536; C:plastid; HDA:TAIR. DR GO; GO:0062049; C:protein phosphatase inhibitor complex; IPI:ComplexPortal. DR GO; GO:0010427; F:abscisic acid binding; IDA:TAIR. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:UniProtKB. DR GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB. DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IDA:UniProtKB. DR GO; GO:0006952; P:defense response; IEP:TAIR. DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IDA:TAIR. DR CDD; cd07821; PYR_PYL_RCAR_like; 1. DR Gene3D; 3.30.530.20; -; 1. DR InterPro; IPR019587; Polyketide_cyclase/dehydratase. DR InterPro; IPR023393; START-like_dom_sf. DR PANTHER; PTHR31213:SF73; ABSCISIC ACID RECEPTOR PYL1; 1. DR PANTHER; PTHR31213; OS03G0300400 PROTEIN-RELATED; 1. DR Pfam; PF10604; Polyketide_cyc2; 1. DR SUPFAM; SSF55961; Bet v1-like; 1. DR Genevisible; Q8VZS8; AT. PE 1: Evidence at protein level; KW 3D-structure; Abscisic acid signaling pathway; Acetylation; Cell membrane; KW Cytoplasm; Membrane; Nucleus; Protein phosphatase inhibitor; Receptor; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..221 FT /note="Abscisic acid receptor PYL1" FT /id="PRO_0000391736" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 50..206 FT /note="START-like" FT MOTIF 112..116 FT /note="Gate loop" FT /evidence="ECO:0000269|PubMed:19898420" FT MOTIF 142..144 FT /note="Latch loop" FT /evidence="ECO:0000269|PubMed:19898420" FT BINDING 86 FT /ligand="abscisate" FT /ligand_id="ChEBI:CHEBI:62432" FT /evidence="ECO:0000269|PubMed:19855379, FT ECO:0000269|PubMed:19893533" FT BINDING 116..121 FT /ligand="abscisate" FT /ligand_id="ChEBI:CHEBI:62432" FT /evidence="ECO:0000269|PubMed:19855379, FT ECO:0000269|PubMed:19893533" FT BINDING 143..149 FT /ligand="abscisate" FT /ligand_id="ChEBI:CHEBI:62432" FT /evidence="ECO:0000269|PubMed:19855379, FT ECO:0000269|PubMed:19893533" FT BINDING 171 FT /ligand="abscisate" FT /ligand_id="ChEBI:CHEBI:62432" FT /evidence="ECO:0000269|PubMed:19855379, FT ECO:0000269|PubMed:19893533" FT SITE 115 FT /note="Involved in interactions with PP2Cs" FT /evidence="ECO:0000269|PubMed:19855379" FT SITE 182 FT /note="Involved in interactions with PP2Cs" FT /evidence="ECO:0000250|UniProtKB:O49686" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22223895" FT MUTAGEN 87 FT /note="H->A: Normal affinity for ABI1. Forms monomers and FT exhibits normal ABA affinity; when associated by A-88 and FT S-90." FT /evidence="ECO:0000269|PubMed:19855379, FT ECO:0000269|PubMed:24645846" FT MUTAGEN 88 FT /note="F->A: Reduced affinity for ABI1. Forms monomers and FT exhibits normal ABA affinity; when associated by A-87 and FT S-90." FT /evidence="ECO:0000269|PubMed:19855379, FT ECO:0000269|PubMed:24645846" FT MUTAGEN 90 FT /note="K->S: Forms monomers and exhibits normal ABA FT affinity; when associated by A-87 and A-88." FT /evidence="ECO:0000269|PubMed:24645846" FT MUTAGEN 111 FT /note="I->A: Normal affinity for ABI1." FT /evidence="ECO:0000269|PubMed:19855379" FT MUTAGEN 111 FT /note="I->K: Forms monomer and exhibits an enhanced ABA FT affinity." FT /evidence="ECO:0000269|PubMed:24645846" FT MUTAGEN 112 FT /note="S->A: Reduced binding affinity and inhibitory FT activity toward ABI1." FT /evidence="ECO:0000269|PubMed:19855379" FT MUTAGEN 112 FT /note="S->R: Forms homodimer and exhibits an enhanced ABA FT affinity; when associated with R-117." FT /evidence="ECO:0000269|PubMed:24645846" FT MUTAGEN 114 FT /note="L->A: Reduced affinity for ABI1." FT /evidence="ECO:0000269|PubMed:19855379" FT MUTAGEN 115 FT /note="P->A: Reduced affinity for ABI1." FT /evidence="ECO:0000269|PubMed:19855379" FT MUTAGEN 117 FT /note="N->R: Forms homodimer and exhibits an enhanced ABA FT affinity; when associated with R-112." FT /evidence="ECO:0000269|PubMed:24645846" FT MUTAGEN 142 FT /note="H->A: Loss of affinity for ABI1." FT /evidence="ECO:0000269|PubMed:19855379" FT MUTAGEN 143 FT /note="R->A: Loss of affinity for ABI1." FT /evidence="ECO:0000269|PubMed:19855379" FT MUTAGEN 144 FT /note="L->A: Loss of affinity for ABI1." FT /evidence="ECO:0000269|PubMed:19855379" FT MUTAGEN 178 FT /note="P->A: Normal affinity for ABI1." FT /evidence="ECO:0000269|PubMed:19855379" FT MUTAGEN 181 FT /note="N->A: Reduced affinity for ABI1." FT /evidence="ECO:0000269|PubMed:19855379" FT MUTAGEN 189 FT /note="F->A: Reduced affinity for ABI1." FT /evidence="ECO:0000269|PubMed:19855379" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:3NEG" FT HELIX 34..47 FT /evidence="ECO:0007829|PDB:3KDJ" FT STRAND 56..67 FT /evidence="ECO:0007829|PDB:3KDJ" FT HELIX 69..76 FT /evidence="ECO:0007829|PDB:3KDJ" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:3KDJ" FT STRAND 89..93 FT /evidence="ECO:0007829|PDB:3KDJ" FT STRAND 105..110 FT /evidence="ECO:0007829|PDB:3KDJ" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:3KAY" FT STRAND 117..127 FT /evidence="ECO:0007829|PDB:3KDJ" FT TURN 128..131 FT /evidence="ECO:0007829|PDB:3KDJ" FT STRAND 132..143 FT /evidence="ECO:0007829|PDB:3KDJ" FT STRAND 148..176 FT /evidence="ECO:0007829|PDB:3KDJ" FT HELIX 183..208 FT /evidence="ECO:0007829|PDB:3KDJ" SQ SEQUENCE 221 AA; 25361 MW; B64B1A52C43072C2 CRC64; MANSESSSSP VNEEENSQRI STLHHQTMPS DLTQDEFTQL SQSIAEFHTY QLGNGRCSSL LAQRIHAPPE TVWSVVRRFD RPQIYKHFIK SCNVSEDFEM RVGCTRDVNV ISGLPANTSR ERLDLLDDDR RVTGFSITGG EHRLRNYKSV TTVHRFEKEE EEERIWTVVL ESYVVDVPEG NSEEDTRLFA DTVIRLNLQK LASITEAMNR NNNNNNSSQV R //