PID_ARATH
ID PID_ARATH Reviewed; 438 AA.
AC O64682;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein kinase PINOID;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase ABRUPTUS;
GN Name=PID; Synonyms=ABR; OrderedLocusNames=At2g34650; ORFNames=T31E10.1;
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 [MRNA], FUNCTION, AUTOPHOSPHORYLATION, DEVELOPMENTAL
RP STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-84; GLU-128; HIS-166;
RP ASP-205; ASP-225; LEU-226; 288-SER--SER-290; THR-294; PRO-300; ARG-378 AND
RP GLY-380.
RC STRAIN=cv. Columbia;
RX PubMed=10693763; DOI=10.1016/s0092-8674(00)80682-0;
RA Christensen S.K., Dagenais N., Chory J., Weigel D.;
RT "Regulation of auxin response by the protein kinase PINOID.";
RL Cell 100:469-478(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 DISRUPTION PHENOTYPE.
RA Bennett S.R.M., Alvarez J., Bossinger G., Smyth D.R.;
RT "Morphogenesis in pinoid mutants of Arabidopsis thaliana.";
RL Plant J. 8:505-520(1995).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY AUXIN, AND DISRUPTION PHENOTYPE.
RX PubMed=11641228; DOI=10.1242/dev.128.20.4057;
RA Benjamins R., Quint A., Weijers D., Hooykaas P., Offringa R.;
RT "The PINOID protein kinase regulates organ development in Arabidopsis by
RT enhancing polar auxin transport.";
RL Development 128:4057-4067(2001).
RN [6]
RP INTERACTION WITH CML12 AND PBP1, AND INDUCTION BY AUXIN.
RX PubMed=12857841; DOI=10.1104/pp.103.019943;
RA Benjamins R., Ampudia C.S., Hooykaas P.J., Offringa R.;
RT "PINOID-mediated signaling involves calcium-binding proteins.";
RL Plant Physiol. 132:1623-1630(2003).
RN [7]
RP FUNCTION.
RX PubMed=15371311; DOI=10.1242/dev.01388;
RA Furutani M., Vernoux T., Traas J., Kato T., Tasaka M., Aida M.;
RT "PIN-FORMED1 and PINOID regulate boundary formation and cotyledon
RT development in Arabidopsis embryogenesis.";
RL Development 131:5021-5030(2004).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15514156; DOI=10.1126/science.1100618;
RA Friml J., Yang X., Michniewicz M., Weijers D., Quint A., Tietz O.,
RA Benjamins R., Ouwerkerk P.B., Ljung K., Sandberg G., Hooykaas P.J.,
RA Palme K., Offringa R.;
RT "A PINOID-dependent binary switch in apical-basal PIN polar targeting
RT directs auxin efflux.";
RL Science 306:862-865(2004).
RN [9]
RP FUNCTION.
RX PubMed=16107478; DOI=10.1242/dev.01969;
RA Treml B.S., Winderl S., Radykewicz R., Herz M., Schweizer G., Hutzler P.,
RA Glawischnig E., Ruiz R.A.;
RT "The gene ENHANCER OF PINOID controls cotyledon development in the
RT Arabidopsis embryo.";
RL Development 132:4063-4074(2005).
RN [10]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF ASP-205.
RX PubMed=16731587; DOI=10.1105/tpc.105.035972;
RA Lee S.H., Cho H.T.;
RT "PINOID positively regulates auxin efflux in Arabidopsis root hair cells
RT and tobacco cells.";
RL Plant Cell 18:1604-1616(2006).
RN [11]
RP FUNCTION, INTERACTION WITH PDK1, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP ASP-205; 288-SER--SER-290 AND 435-PHE--PHE-438.
RX PubMed=16601102; DOI=10.1073/pnas.0510283103;
RA Zegzouti H., Anthony R.G., Jahchan N., Boegre L., Christensen S.K.;
RT "Phosphorylation and activation of PINOID by the phospholipid signaling
RT kinase 3-phosphoinositide-dependent protein kinase 1 (PDK1) in
RT Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6404-6409(2006).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17889649; DOI=10.1016/j.cell.2007.07.033;
RA Michniewicz M., Zago M.K., Abas L., Weijers D., Schweighofer A.,
RA Meskiene I., Heisler M.G., Ohno C., Zhang J., Huang F., Schwab R.,
RA Weigel D., Meyerowitz E.M., Luschnig C., Offringa R., Friml J.;
RT "Antagonistic regulation of PIN phosphorylation by PP2A and PINOID directs
RT auxin flux.";
RL Cell 130:1044-1056(2007).
RN [13]
RP FUNCTION.
RX PubMed=19075219; DOI=10.1073/pnas.0809761106;
RA Cheng Y., Qin G., Dai X., Zhao Y.;
RT "NPY genes and AGC kinases define two key steps in auxin-mediated
RT organogenesis in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:21017-21022(2008).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20040538; DOI=10.1105/tpc.109.071639;
RA Kleine-Vehn J., Huang F., Naramoto S., Zhang J., Michniewicz M.,
RA Offringa R., Friml J.;
RT "PIN auxin efflux carrier polarity is regulated by PINOID kinase-mediated
RT recruitment into GNOM-independent trafficking in Arabidopsis.";
RL Plant Cell 21:3839-3849(2009).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19363095; DOI=10.1104/pp.108.131607;
RA Sukumar P., Edwards K.S., Rahman A., Delong A., Muday G.K.;
RT "PINOID kinase regulates root gravitropism through modulation of PIN2-
RT dependent basipetal auxin transport in Arabidopsis.";
RL Plant Physiol. 150:722-735(2009).
RN [16]
RP FUNCTION.
RX PubMed=20407025; DOI=10.1105/tpc.109.072678;
RA Huang F., Zago M.K., Abas L., van Marion A., Galvan-Ampudia C.S.,
RA Offringa R.;
RT "Phosphorylation of conserved PIN motifs directs Arabidopsis PIN1 polarity
RT and auxin transport.";
RL Plant Cell 22:1129-1142(2010).
RN [17]
RP FUNCTION.
RX PubMed=20080776; DOI=10.1073/pnas.0909460107;
RA Zhang J., Nodzynski T., Pencik A., Rolcik J., Friml J.;
RT "PIN phosphorylation is sufficient to mediate PIN polarity and direct auxin
RT transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:918-922(2010).
RN [18]
RP FUNCTION.
RX PubMed=21423279; DOI=10.1038/cr.2011.49;
RA Li H., Lin D., Dhonukshe P., Nagawa S., Chen D., Friml J., Scheres B.,
RA Guo H., Yang Z.;
RT "Phosphorylation switch modulates the interdigitated pattern of PIN1
RT localization and cell expansion in Arabidopsis leaf epidermis.";
RL Cell Res. 21:970-978(2011).
RN [19]
RP FUNCTION.
RX PubMed=21569134; DOI=10.1111/j.1365-313x.2011.04636.x;
RA Rakusova H., Gallego-Bartolome J., Vanstraelen M., Robert H.S., Alabadi D.,
RA Blazquez M.A., Benkova E., Friml J.;
RT "Polarization of PIN3-dependent auxin transport for hypocotyl gravitropic
RT response in Arabidopsis thaliana.";
RL Plant J. 67:817-826(2011).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the regulation of
CC auxin signaling. Acts as a positive regulator of cellular auxin efflux
CC and regulates organ development by enhancing polar auxin transport.
CC Phosphorylates conserved serine residues in the PIN auxin efflux
CC carriers. Phosphorylation of PIN proteins is required and sufficient
CC for apical-basal PIN polarity that enables directional intercellular
CC auxin fluxes, which mediate differential growth, tissue patterning and
CC organogenesis. Acts in association with PIN1 to control the
CC establishment of bilateral symmetry and promotion of cotyledon
CC outgrowth. Regulates root gravitropism through modulation of PIN2-
CC dependent basipetal auxin transport. Required for polarization of PIN3-
CC dependent auxin transport for hypocotyl gravitropic response. The
CC protein kinase activity of PID is essential for its auxin efflux
CC regulatory function. PID kinase and PP2A phosphatase activities
CC antagonistically regulate phosphorylation of PIN proteins, affecting
CC PIN sorting. {ECO:0000269|PubMed:10693763, ECO:0000269|PubMed:11641228,
CC ECO:0000269|PubMed:15371311, ECO:0000269|PubMed:15514156,
CC ECO:0000269|PubMed:16107478, ECO:0000269|PubMed:16601102,
CC ECO:0000269|PubMed:16731587, ECO:0000269|PubMed:17889649,
CC ECO:0000269|PubMed:19075219, ECO:0000269|PubMed:19363095,
CC ECO:0000269|PubMed:20040538, ECO:0000269|PubMed:20080776,
CC ECO:0000269|PubMed:20407025, ECO:0000269|PubMed:21423279,
CC ECO:0000269|PubMed:21569134}.
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 -!- 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;
CC -!- ACTIVITY REGULATION: Activated by magnesium and PDK1. Inhibited by
CC staurosporine. Repressed by calcium. {ECO:0000269|PubMed:16601102,
CC ECO:0000269|PubMed:16731587}.
CC -!- SUBUNIT: Interacts with PDK1, CML12 and PBP1.
CC {ECO:0000269|PubMed:12857841, ECO:0000269|PubMed:16601102}.
CC -!- INTERACTION:
CC O64682; P25071: CML12; NbExp=4; IntAct=EBI-1393382, EBI-1238781;
CC O64682; Q9LPQ3: MKK7; NbExp=3; IntAct=EBI-1393382, EBI-2128593;
CC O64682; Q9LSQ6: PBP1; NbExp=4; IntAct=EBI-1393382, EBI-1393367;
CC O64682; Q9XF67: PDPK1; NbExp=3; IntAct=EBI-1393382, EBI-1103587;
CC O64682; Q9C6B8: PIN1; NbExp=2; IntAct=EBI-1393382, EBI-1541799;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16731587,
CC ECO:0000269|PubMed:17889649, ECO:0000269|PubMed:20040538}.
CC Note=Targeted to the cell periphery.
CC -!- TISSUE SPECIFICITY: Expressed in root hair cells, shoot xylem
CC parenchyma cells and endodermis around the vasculature. Expressed in
CC anther primordia, vasculature of the growing flower stalk, young
CC pedicels and bracts and developing sepals, but not in petals. In
CC pistils, transiently expressed in the vasculature of the style and the
CC septum, and in the integuments and funiculus of the developing ovule.
CC {ECO:0000269|PubMed:11641228, ECO:0000269|PubMed:16731587}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis at the globular
CC stage on the apical flanks of the embryo, where the cotyledons are
CC subsequently formed. Expression in the cotyledons persists at the heart
CC stage until the mid-torpedo stage. At the bent-cotyledon stage,
CC expressed weakly in the apical meristem. At the early phase of
CC flowering, expressed in discrete groups of cells on the flanks of the
CC apex initially marking the floral anlagen. During primordia
CC differentiation, expressed in the adaxial portion of the primordia. In
CC developing flowers, transiently expressed in nascent floral organs and
CC then decreases as floral organs mature. {ECO:0000269|PubMed:10693763}.
CC -!- INDUCTION: By auxin. {ECO:0000269|PubMed:11641228,
CC ECO:0000269|PubMed:12857841}.
CC -!- PTM: Autophosphorylated. Phosphorylated by PDK1.
CC -!- DISRUPTION PHENOTYPE: Pleiotropic defects in the development of floral
CC organs, cotyledons and leaves, especially in the number of organs
CC produced. Loss of function induces an apical-to-basal shift in PIN1
CC polar targeting at the inflorescence apex, accompanied by defective
CC organogenesis. {ECO:0000269|PubMed:10693763,
CC ECO:0000269|PubMed:11641228, ECO:0000269|PubMed:15514156,
CC ECO:0000269|PubMed:19363095, ECO:0000269|Ref.4}.
CC -!- MISCELLANEOUS: Plants overexpressing PID are small with dark green,
CC curled leaves, with vegetative and floral organs defects and reduced
CC apical dominance and internode elongation. Specific overexpression of
CC PID in root hair cells suppresses root hair development. Over-
CC expression of PID induces a basal-to-apical shift in PIN2 and PIN4
CC localization, resulting in the loss of auxin gradients and strong
CC defects in embryo and seedling roots.
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; AF232236; AAF40202.1; -; mRNA.
DR EMBL; AC004077; AAC26704.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09003.1; -; Genomic_DNA.
DR PIR; C84759; C84759.
DR RefSeq; NP_181012.1; NM_129019.5.
DR AlphaFoldDB; O64682; -.
DR SMR; O64682; -.
DR BioGRID; 3376; 5.
DR DIP; DIP-39595N; -.
DR IntAct; O64682; 7.
DR STRING; 3702.AT2G34650.1; -.
DR iPTMnet; O64682; -.
DR PaxDb; O64682; -.
DR PRIDE; O64682; -.
DR ProteomicsDB; 235087; -.
DR EnsemblPlants; AT2G34650.1; AT2G34650.1; AT2G34650.
DR GeneID; 818030; -.
DR Gramene; AT2G34650.1; AT2G34650.1; AT2G34650.
DR KEGG; ath:AT2G34650; -.
DR Araport; AT2G34650; -.
DR TAIR; locus:2062268; AT2G34650.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; O64682; -.
DR OMA; GSSACEY; -.
DR OrthoDB; 799520at2759; -.
DR PhylomeDB; O64682; -.
DR PRO; PR:O64682; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64682; baseline and differential.
DR Genevisible; O64682; AT.
DR GO; GO:0009986; C:cell surface; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS:TAIR.
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; IDA:TAIR.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0048825; P:cotyledon development; IGI:UniProtKB.
DR GO; GO:0048827; P:phyllome development; IGI:TAIR.
DR GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR GO; GO:0048766; P:root hair initiation; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Auxin signaling pathway; Cytoplasm; Developmental protein;
KW Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..438
FT /note="Protein kinase PINOID"
FT /id="PRO_0000411970"
FT DOMAIN 75..394
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 395..438
FT /note="AGC-kinase C-terminal"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 81..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 84
FT /note="G->S: In pid-10; intermediate pid phenotype."
FT /evidence="ECO:0000269|PubMed:10693763"
FT MUTAGEN 128
FT /note="E->K: In pid-5 and pid-11; strong pid phenotype."
FT /evidence="ECO:0000269|PubMed:10693763"
FT MUTAGEN 166
FT /note="H->S: In pid-13; weak pid phenotype."
FT /evidence="ECO:0000269|PubMed:10693763"
FT MUTAGEN 205
FT /note="D->A: Loss of autophosphorylation. Loss of
FT localization to the cell periphery."
FT /evidence="ECO:0000269|PubMed:10693763,
FT ECO:0000269|PubMed:16601102, ECO:0000269|PubMed:16731587"
FT MUTAGEN 225
FT /note="D->G: Increases autophosphorylation activity."
FT /evidence="ECO:0000269|PubMed:10693763"
FT MUTAGEN 226
FT /note="L->F: In pid-3; strong pid phenotype."
FT /evidence="ECO:0000269|PubMed:10693763"
FT MUTAGEN 288..290
FT /note="SGS->EGE: Increases autophosphorylation activity.
FT Loss of phosphorylation by PDK1."
FT /evidence="ECO:0000269|PubMed:10693763,
FT ECO:0000269|PubMed:16601102"
FT MUTAGEN 294
FT /note="T->E: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:10693763"
FT MUTAGEN 300
FT /note="P->Q: In pid-8; weak pid phenotype."
FT /evidence="ECO:0000269|PubMed:10693763"
FT MUTAGEN 378
FT /note="R->K: In pid-4 and pid-12; strong pid phenotype."
FT /evidence="ECO:0000269|PubMed:10693763"
FT MUTAGEN 380
FT /note="G->R: In pid-2; intermediate pid phenotype."
FT /evidence="ECO:0000269|PubMed:10693763"
FT MUTAGEN 435..438
FT /note="FDYF->VDYV: Decreases autophosphorylation 3-fold.
FT Loss of phosphorylation by PDK1."
FT /evidence="ECO:0000269|PubMed:16601102"
SQ SEQUENCE 438 AA; 49271 MW; 29A33E80FF96B032 CRC64;
MLRESDGEMS LGTTNSPISS GTESCSSFSR LSFDAPPSTI PEEESFLSLK PHRSSDFAYA
EIRRRKKQGL TFRDFRLMRR IGAGDIGTVY LCRLAGDEEE SRSSYFAMKV VDKEALALKK
KMHRAEMEKT ILKMLDHPFL PTLYAEFEAS HFSCIVMEYC SGGDLHSLRH RQPHRRFSLS
SARFYAAEVL VALEYLHMLG IIYRDLKPEN ILVRSDGHIM LSDFDLSLCS DSIAAVESSS
SSPENQQLRS PRRFTRLARL FQRVLRSKKV QTLEPTRLFV AEPVTARSGS FVGTHEYVAP
EVASGGSHGN AVDWWAFGVF LYEMIYGKTP FVAPTNDVIL RNIVKRQLSF PTDSPATMFE
LHARNLISGL LNKDPTKRLG SRRGAAEVKV HPFFKGLNFA LIRTLTPPEI PSSVVKKPMK
SATFSGRSSN KPAAFDYF
