PYL1_ARATH
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 03-AUG-2022, entry version 115.
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; 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};
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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.AT5G46790.1; -.
DR BindingDB; Q8VZS8; -.
DR iPTMnet; Q8VZS8; -.
DR PaxDb; Q8VZS8; -.
DR PRIDE; Q8VZS8; -.
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; locus:2178585; AT5G46790.
DR eggNOG; ENOG502QW1M; Eukaryota.
DR HOGENOM; CLU_077517_0_1_1; -.
DR InParanoid; Q8VZS8; -.
DR OMA; STVDAHH; -.
DR OrthoDB; 1238726at2759; -.
DR PhylomeDB; Q8VZS8; -.
DR EvolutionaryTrace; Q8VZS8; -.
DR PRO; PR:Q8VZS8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VZS8; baseline and differential.
DR Genevisible; Q8VZS8; AT.
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 Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR019587; Polyketide_cyclase/dehydratase.
DR InterPro; IPR023393; START-like_dom_sf.
DR Pfam; PF10604; Polyketide_cyc2; 1.
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
