CHER1_ARATH
ID CHER1_ARATH Reviewed; 700 AA.
AC Q94AN2; Q9LUQ4; Q9M7X1;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Choline transporter protein 1 {ECO:0000303|PubMed:25008948};
DE Short=AtCTL1 {ECO:0000303|PubMed:25008948};
DE AltName: Full=Protein SIGNIFICANT IONOME CHANGES 1 {ECO:0000303|PubMed:29284002};
GN Name=CHER1 {ECO:0000303|PubMed:25008948};
GN Synonyms=CTL1 {ECO:0000303|PubMed:25008948},
GN SIC1 {ECO:0000303|PubMed:29284002};
GN OrderedLocusNames=At3g15380 {ECO:0000312|Araport:AT3G15380};
GN ORFNames=MJK13.4 {ECO:0000312|EMBL:AAF35404.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25008948; DOI=10.1038/ncomms5276;
RA Dettmer J., Ursache R., Campilho A., Miyashima S., Belevich I., O'Regan S.,
RA Mullendore D.L., Yadav S.R., Lanz C., Beverina L., Papagni A.,
RA Schneeberger K., Weigel D., Stierhof Y.D., Moritz T., Knoblauch M.,
RA Jokitalo E., Helariutta Y.;
RT "CHOLINE TRANSPORTER-LIKE1 is required for sieve plate development to
RT mediate long-distance cell-to-cell communication.";
RL Nat. Commun. 5:4276-4276(2014).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-247, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27743414; DOI=10.1111/tpj.13393;
RA Kraner M.E., Link K., Melzer M., Ekici A.B., Uebe S., Tarazona P.,
RA Feussner I., Hofmann J., Sonnewald U.;
RT "Choline transporter-like1 (CHER1) is crucial for plasmodesmata maturation
RT in Arabidopsis thaliana.";
RL Plant J. 89:394-406(2017).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-247, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=29284002; DOI=10.1371/journal.pbio.2002978;
RA Gao Y.-Q., Chen J.-G., Chen Z.-R., An D., Lv Q.-Y., Han M.-L., Wang Y.-L.,
RA Salt D.E., Chao D.-Y.;
RT "A new vesicle trafficking regulator CTL1 plays a crucial role in ion
RT homeostasis.";
RL PLoS Biol. 15:E2002978-E2002978(2017).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=29283991; DOI=10.1371/journal.pbio.2004310;
RA Wang Y., Yang L., Tang Y., Tang R., Jing Y., Zhang C., Zhang B., Li X.,
RA Cui Y., Zhang C., Shi J., Zhao F., Lan W., Luan S.;
RT "Arabidopsis choline transporter-like 1 (CTL1) regulates secretory
RT trafficking of auxin transporters to control seedling growth.";
RL PLoS Biol. 15:E2004310-E2004310(2017).
CC -!- FUNCTION: Regulator of vesicle trafficking, including endocytosis.
CC Necessary for secondary plasmodesmata (PD) formation and development
CC via the secretory trafficking regulation of proteins required for PD
CC development, thus influencing intercellular communication
CC (PubMed:27743414, PubMed:29284002). Modulates ion homeostasis,
CC especially in roots, by monitoring the transport and subsequent
CC subcellular localization of some ion transporters (PubMed:29284002).
CC Choline transporter involved in the regulation of choline metabolite
CC homeostasis during root and phloem development (PubMed:25008948).
CC Modulates phloem morphogenesis and conductivity (PubMed:25008948).
CC Required for procambium maintenance and sieve plate development (e.g.
CC sieve plate and sieve pore elaboration) to mediate long-distance cell-
CC to-cell communication via symplastic transport through the phloem
CC (PubMed:25008948). Involved in the regulation of intracellular
CC trafficking of PIN-type auxin transporters (e.g. PIN1 and PIN3), a
CC process controlling seedling growth, apical dominance, cell elongation
CC and apical hook development. Modulates also membrane lipids (e.g.
CC phospholipids and sphingolipids) homeostasis (PubMed:29283991).
CC {ECO:0000269|PubMed:25008948, ECO:0000269|PubMed:27743414,
CC ECO:0000269|PubMed:29283991, ECO:0000269|PubMed:29284002}.
CC -!- FUNCTION: (Microbial infection) Required for PD localization of MP17,
CC the luteoviral movement protein. {ECO:0000269|PubMed:27743414}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:27743414}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:25008948, ECO:0000269|PubMed:27743414,
CC ECO:0000269|PubMed:29283991}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:25008948}. Prevacuolar compartment membrane
CC {ECO:0000269|PubMed:29283991}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:29283991}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Associated transiently with the
CC phragmoplast during cytokinesis. Follows a polar localization in the
CC forming sieve plates. {ECO:0000269|PubMed:25008948}.
CC -!- TISSUE SPECIFICITY: Expressed in both roots and shoots.
CC {ECO:0000269|PubMed:29283991, ECO:0000269|PubMed:29284002}.
CC -!- DEVELOPMENTAL STAGE: In roots, observed in all cells of the root tip,
CC inculding both meristem and elongation zones, but restricted to
CC vascular tissues of the maturation zone (PubMed:29284002,
CC PubMed:29283991). Also observed in shoot apical meristems, lateral root
CC primordia and the vascular system. Under dark conditions, present in
CC the concave side of the apical hook (PubMed:29283991).
CC {ECO:0000269|PubMed:29283991, ECO:0000269|PubMed:29284002}.
CC -!- DISRUPTION PHENOTYPE: Impaired plasmodesmata (PD) mediated cell-to-cell
CC communication (PubMed:29284002). Altered choline metabolite profile.
CC Several phenotypic abnormalities (e.g. dwarf with defects in both shoot
CC and root architecture), including reduced pore density and altered pore
CC structure in the sieve areas, associated with defective symplastic
CC transport through phloem. Increased number of sieve elements (SE)-like
CC cells instead of two companion cells (CCs) and two SEs. Defects in
CC procambium maintenance and phloem patterning. Abnormal retaining of
CC desmotubules in the symplastic space in sieve pores (PubMed:25008948).
CC In cher1-4, impaired secondary plasmodesmata (PD) formation and
CC development leading to starch and soluble sugars excess accumulation,
CC and stunted growth. Altered PD localization of the luteoviral movement
CC protein MP17. Reduced level of choline and phosphocholine
CC (PubMed:27743414). Altered ion profile due to both PD defects and ion
CC transporter misregulation. Increased leaf concentrations of sodium
CC (Na), lithium (Li), boron (B) ions, and decreased leaf concentrations
CC of phosphorus (P), potassium (K), calcium (Ca), cobalt (Co), nickel
CC (Ni), and copper (Cu), manganese (Mn), iron (Fe), zinc (Zn) and
CC molybdenum (Mo) ions. Defects in leaf and root elongation as well as
CC fewer leaves are also observed, associated with irregular cell
CC organization in roots, probably as a result of irregular cell division
CC (PubMed:29284002). Impaired intracellular trafficking of PIN-type auxin
CC transporters (e.g. PIN1 and PIN3) to the plasma membrane, resulting in
CC abnormal seedling growth, lack of apical dominance, cell elongation
CC defect and apical hook development. Perturbated membrane lipids (e.g.
CC phospholipids and sphingolipids) homeostasis. Reduced sensitivity to
CC auxin (e.g. 1-naphthylacetic acid, NAA) (PubMed:29283991).
CC {ECO:0000269|PubMed:25008948, ECO:0000269|PubMed:27743414,
CC ECO:0000269|PubMed:29283991, ECO:0000269|PubMed:29284002}.
CC -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF35404.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB02367.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB022218; BAB02367.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC024081; AAF35404.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75661.1; -; Genomic_DNA.
DR EMBL; AY045917; AAK76591.1; -; mRNA.
DR EMBL; BT001974; AAN71973.1; -; mRNA.
DR RefSeq; NP_566511.1; NM_112406.5.
DR AlphaFoldDB; Q94AN2; -.
DR STRING; 3702.AT3G15380.1; -.
DR SwissPalm; Q94AN2; -.
DR PaxDb; Q94AN2; -.
DR PRIDE; Q94AN2; -.
DR ProteomicsDB; 220475; -.
DR EnsemblPlants; AT3G15380.1; AT3G15380.1; AT3G15380.
DR GeneID; 820777; -.
DR Gramene; AT3G15380.1; AT3G15380.1; AT3G15380.
DR KEGG; ath:AT3G15380; -.
DR Araport; AT3G15380; -.
DR TAIR; locus:2090171; AT3G15380.
DR eggNOG; KOG1362; Eukaryota.
DR HOGENOM; CLU_017181_3_0_1; -.
DR InParanoid; Q94AN2; -.
DR OMA; CIAYWAC; -.
DR OrthoDB; 329225at2759; -.
DR PhylomeDB; Q94AN2; -.
DR PRO; PR:Q94AN2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94AN2; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009551; C:secondary plasmodesma; IMP:UniProtKB.
DR GO; GO:0097218; C:sieve plate; IDA:TAIR.
DR GO; GO:0055044; C:symplast; IMP:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0015220; F:choline transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015871; P:choline transport; IDA:TAIR.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0050801; P:ion homeostasis; IMP:UniProtKB.
DR GO; GO:0048366; P:leaf development; IMP:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IMP:UniProtKB.
DR GO; GO:0010088; P:phloem development; IMP:TAIR.
DR GO; GO:0009663; P:plasmodesma organization; IMP:UniProtKB.
DR GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IMP:UniProtKB.
DR GO; GO:0010067; P:procambium histogenesis; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IMP:UniProtKB.
DR GO; GO:2000012; P:regulation of auxin polar transport; IMP:UniProtKB.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:UniProtKB.
DR GO; GO:0051510; P:regulation of unidimensional cell growth; IMP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR GO; GO:0090603; P:sieve element differentiation; IMP:TAIR.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
DR InterPro; IPR007603; Choline_transptr-like.
DR PANTHER; PTHR12385; PTHR12385; 1.
DR Pfam; PF04515; Choline_transpo; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Developmental protein; Endocytosis;
KW Endosome; Glycoprotein; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..700
FT /note="Choline transporter protein 1"
FT /id="PRO_0000440037"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..241
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..322
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..432
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..595
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 617..633
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 655..700
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 247
FT /note="G->E: In cher1-5 and sic1; impaired secondary
FT plasmodesmata (PD) formation (e.g. blocked or shrunken) and
FT development leading to starch and soluble sugars excess
FT accumulation, abnormal cell-to-cell communication, and
FT stunted growth. Altered PD localization of the luteoviral
FT movement protein MP17. Abnormal subcellular localization.
FT Increased leaf concentrations of sodium (Na), lithium (Li),
FT boron (B) ions, and decreased leaf concentrations of
FT phosphorus (P), potassium (K), calcium (Ca), cobalt (Co),
FT nickel (Ni), and copper (Cu), manganese (Mn), iron (Fe),
FT zinc (Zn) and molybdenum (Mo) ions."
FT /evidence="ECO:0000269|PubMed:27743414,
FT ECO:0000269|PubMed:29284002"
SQ SEQUENCE 700 AA; 78737 MW; DF9F0E38C4E36C25 CRC64;
MRGPLGAVIG RYTSSDGSAP NDGIIKHNRK CRDITFLIIF IAFWVSMIVN SSFGFNQGNP
LRLTYGLDYE GNVCGSKHRH RDLTQLELRY WLNPNQVYES GLKDGELKLA NARTICLLDC
PAPSDDTLNW VCDYPDGEIR LKMNDWIDRN YDYFEFLTPE MRNSSLQLQG PCYPVIFPSV
NVYWSCQYIA RASNSSLRHW QQMGGVNIQE DMIIDKSIRR SMNSRASVLK RYVADIGKSW
PVLIVCGGLV PLFLSIIWLL LIRHFVAAMP WITVVLFNML LISVTVFYYL KAGWIGNDAV
TPIIGEHDPY FHVYGRELTH VRGVAILMTF ISVVAILTSI AIIRRILMAT SVLKVAAKVI
GEVQALIIFP AIPFAMLAIF YMFWISAALH LFSSGQVVQN NCNNTNCCAY DLVLKKVNCD
RCCGYSIHYT PHITIAIFFH LFGCYWATQF FIASSATVIA GSVASYYWAQ GEASPEIPFL
PVFASMKRLA RYNLGSVALG SLIVSFVESV RFILEAIRRK TKVSGTIPDH WFWRMAHYTS
RGCLKSVEWT IKSVNRNAYI MIAITGKSFC KSSAIATELI ISNILRIGKV NVIGDVILFL
GKLCVSLFSA LFGFLMLDSH RYRASHNKVS SPLLPVLACW ALGYIVATLF FAVVEMSIDT
IILSFCQDSE ENQGNAQHAP PLLLETLDSN QEEEVQSLTH
