SH3P2_ARATH
ID SH3P2_ARATH Reviewed; 368 AA.
AC Q8VWF1; F4JLF5; F4JLF6; O65689;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=SH3 domain-containing protein 2 {ECO:0000303|PubMed:11701884};
DE Short=AtSH3P2 {ECO:0000303|PubMed:11701884};
GN Name=SH3P2 {ECO:0000303|PubMed:11701884};
GN OrderedLocusNames=At4g34660 {ECO:0000312|Araport:AT4G34660};
GN ORFNames=T4L20.240 {ECO:0000312|EMBL:CAA18845.1};
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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11701884; DOI=10.2307/3871590;
RA Lam B.C.-H., Sage T.L., Bianchi F., Blumwald E.;
RT "Role of SH3 domain-containing proteins in clathrin-mediated vesicle
RT trafficking in Arabidopsis.";
RL Plant Cell 13:2499-2512(2001).
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 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH FREE1.
RX PubMed=25699591; DOI=10.1104/pp.114.253377;
RA Kolb C., Nagel M.K., Kalinowska K., Hagmann J., Ichikawa M.,
RA Anzenberger F., Alkofer A., Sato M.H., Braun P., Isono E.;
RT "FYVE1 is essential for vacuole biogenesis and intracellular trafficking in
RT Arabidopsis.";
RL Plant Physiol. 167:1361-1373(2015).
RN [7]
RP INTERACTION WITH FREE1, DOMAIN, AND IDENTIFICATION IN A PI3K COMPLEX.
RX PubMed=25624505; DOI=10.1073/pnas.1421271112;
RA Gao C., Zhuang X., Cui Y., Fu X., He Y., Zhao Q., Zeng Y., Shen J., Luo M.,
RA Jiang L.;
RT "Dual roles of an Arabidopsis ESCRT component FREE1 in regulating vacuolar
RT protein transport and autophagic degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:1886-1891(2015).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH ATG8E AND ATG8F,
RP AND IDENTIFICATION IN A PI3K COMPLEX.
RX PubMed=24249832; DOI=10.1105/tpc.113.118307;
RA Zhuang X., Wang H., Lam S.K., Gao C., Wang X., Cai Y., Jiang L.;
RT "A BAR-domain protein SH3P2, which binds to phosphatidylinositol 3-
RT phosphate and ATG8, regulates autophagosome formation in Arabidopsis.";
RL Plant Cell 25:4596-4615(2013).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX DOI=10.4161/auto.28060;
RA Zhuang X., Jiang L.;
RT "Autophagosome biogenesis in plants.";
RL Autophagy 10:704-705(2014).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLN-154; ARG-155;
RP 160-ARG-GLN-161; ARG-172; ARG-173 AND LYS-189, SUBCELLULAR LOCATION,
RP INTERACTION WITH DRP1A AND SH3P3, AND SUBUNIT.
RC STRAIN=cv. Columbia, and cv. Wassilewskija-2;
RX PubMed=28584166; DOI=10.1105/tpc.17.00108;
RA Ahn G., Kim H., Kim D.H., Hanh H., Yoon Y., Singaram I., Wijesinghe K.J.,
RA Johnson K.A., Zhuang X., Liang Z., Stahelin R.V., Jiang L., Cho W.,
RA Kang B.-H., Hwang I.;
RT "SH3 domain-containing protein 2 plays a crucial role at the step of
RT membrane tubulation during cell plate formation.";
RL Plant Cell 29:1388-1405(2017).
CC -!- FUNCTION: Regulator for autophaosome formation and/or maturation
CC (PubMed:24249832, Ref.9). Binds phosphatidylinositol-phosphate; highest
CC affinity for vesicles containing PtdIns(3,4,5)P(3), followed by those
CC containing PtdIns(4,5)P(2) and PtdIns(3,4)P(2), with minimal binding to
CC phosphatidylinositol monophosphates, including PtdIns(3)P
CC (PubMed:24249832, PubMed:28584166). Together with DRP1A, converts the
CC fused vesicles to tubular structures at the cell plate during
CC cytokinesis (PubMed:28584166). {ECO:0000269|PubMed:24249832,
CC ECO:0000269|PubMed:28584166, ECO:0000269|Ref.9}.
CC -!- SUBUNIT: Homodimer (PubMed:24249832, PubMed:28584166). Interacts with
CC FREE1 (PubMed:25699591, PubMed:25624505). Interacts (via SH3 domain)
CC with ATG8E and ATG8F (PubMed:24249832). Component of a phosphoinositide
CC 3-kinase (PI3K) complex containing ATG6, SH3P2 and FREE1
CC (PubMed:25624505, PubMed:24249832). Binds to SH3P3 and DRP1A
CC (PubMed:28584166). Forms a complex made of SH3P2 and DRP1A and triggers
CC its accumulation at the cell plate (PubMed:28584166).
CC {ECO:0000269|PubMed:24249832, ECO:0000269|PubMed:25624505,
CC ECO:0000269|PubMed:25699591, ECO:0000269|PubMed:28584166}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24249832,
CC ECO:0000269|PubMed:25699591}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:11701884, ECO:0000269|PubMed:25699591}.
CC Cell membrane {ECO:0000269|PubMed:25699591,
CC ECO:0000269|PubMed:28584166}. Late endosome
CC {ECO:0000269|PubMed:25699591, ECO:0000269|PubMed:28584166}. Cytoplasmic
CC vesicle, autophagosome membrane {ECO:0000269|PubMed:24249832,
CC ECO:0000269|Ref.9}; Peripheral membrane protein {ECO:0000269|Ref.9}.
CC Note=Transolcate from the cytosol to the phagophore assembly
CC site/preautophagosome structure upon autophagy induction
CC (PubMed:24249832). Localized at the leading edge of the cell plate in
CC dividing cells, especially in constricted or curved regions
CC (PubMed:28584166). Observed at the plasma membrane and in endosomal
CC compartments in non-dividing cells (PubMed:28584166).
CC {ECO:0000269|PubMed:24249832, ECO:0000269|PubMed:28584166}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VWF1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VWF1-2; Sequence=VSP_057911;
CC Name=3;
CC IsoId=Q8VWF1-3; Sequence=VSP_057912;
CC -!- TISSUE SPECIFICITY: Highly expressed in seedlings. Detected in flowers,
CC leaves and stems. {ECO:0000269|PubMed:11701884}.
CC -!- DOMAIN: The N-terminal BAR domain is required for the interaction with
CC FREE1. {ECO:0000269|PubMed:25624505}.
CC -!- DISRUPTION PHENOTYPE: Delayed germination, but almost normal growth
CC after germination in sh3p2 partial mutants (PubMed:28584166). RNAi
CC plants exhibit cytokinesis-defective phenotypes associated with the
CC aggregation of vesicles at the leading edge of the cell plate and
CC abnormal cytosolic localization of DRP1A in dividing cells
CC (PubMed:28584166). {ECO:0000269|PubMed:28584166}.
CC -!- MISCELLANEOUS: Knockdown of SH3P2 is developmentally lethal and
CC significantly suppresses autophagosome formation.
CC {ECO:0000269|PubMed:24249832}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18845.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80183.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF367774; AAL32439.1; -; mRNA.
DR EMBL; AL023094; CAA18845.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161585; CAB80183.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86405.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86406.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86407.1; -; Genomic_DNA.
DR EMBL; AY072132; AAL59954.1; -; mRNA.
DR EMBL; AY096478; AAM20118.1; -; mRNA.
DR EMBL; AY087158; AAM64716.1; -; mRNA.
DR PIR; T05286; T05286.
DR RefSeq; NP_001190913.1; NM_001203984.1. [Q8VWF1-2]
DR RefSeq; NP_001190914.1; NM_001203985.1. [Q8VWF1-3]
DR RefSeq; NP_567969.1; NM_119632.4. [Q8VWF1-1]
DR AlphaFoldDB; Q8VWF1; -.
DR SMR; Q8VWF1; -.
DR IntAct; Q8VWF1; 2.
DR STRING; 3702.AT4G34660.1; -.
DR iPTMnet; Q8VWF1; -.
DR PaxDb; Q8VWF1; -.
DR PRIDE; Q8VWF1; -.
DR ProteomicsDB; 234501; -. [Q8VWF1-1]
DR EnsemblPlants; AT4G34660.1; AT4G34660.1; AT4G34660. [Q8VWF1-1]
DR EnsemblPlants; AT4G34660.2; AT4G34660.2; AT4G34660. [Q8VWF1-2]
DR EnsemblPlants; AT4G34660.3; AT4G34660.3; AT4G34660. [Q8VWF1-3]
DR GeneID; 829618; -.
DR Gramene; AT4G34660.1; AT4G34660.1; AT4G34660. [Q8VWF1-1]
DR Gramene; AT4G34660.2; AT4G34660.2; AT4G34660. [Q8VWF1-2]
DR Gramene; AT4G34660.3; AT4G34660.3; AT4G34660. [Q8VWF1-3]
DR KEGG; ath:AT4G34660; -.
DR Araport; AT4G34660; -.
DR TAIR; locus:2139554; AT4G34660.
DR eggNOG; ENOG502QQJ7; Eukaryota.
DR InParanoid; Q8VWF1; -.
DR OMA; MAYKLEA; -.
DR PhylomeDB; Q8VWF1; -.
DR PRO; PR:Q8VWF1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VWF1; baseline and differential.
DR Genevisible; Q8VWF1; AT.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA:TAIR.
DR GO; GO:0009920; P:cell plate formation involved in plant-type cell wall biogenesis; IDA:TAIR.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IPI:TAIR.
DR GO; GO:1903527; P:positive regulation of membrane tubulation; IMP:UniProtKB.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Endosome; Membrane; Reference proteome; SH3 domain.
FT CHAIN 1..368
FT /note="SH3 domain-containing protein 2"
FT /id="PRO_0000434151"
FT DOMAIN 1..264
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 299..358
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 258..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..21
FT /evidence="ECO:0000255"
FT COILED 146..210
FT /evidence="ECO:0000255"
FT VAR_SEQ 20..42
FT /note="Missing (in isoform 2)"
FT /id="VSP_057911"
FT VAR_SEQ 253..303
FT /note="Missing (in isoform 3)"
FT /id="VSP_057912"
FT MUTAGEN 154
FT /note="Q->E: Reduced binding to PtdIns(3,4,5)P(3)-
FT containing vesicles and lower capacity to mediates the
FT tubulation of liposomes. Impaired binding to
FT PtdIns(3,4,5)P(3)-containing vesicles; when associated with
FT E-155, E-160 and E-161. Strongly impaired binding to
FT PtdIns(3,4,5)P(3)-containing vesicles; when associated with
FT E-155, E-160, E-161, E-172, E-175 and E-189."
FT /evidence="ECO:0000269|PubMed:28584166"
FT MUTAGEN 155
FT /note="R->E: Reduced binding to PtdIns(3,4,5)P(3)-
FT containing vesicles and lower capacity to mediates the
FT tubulation of liposomes. Impaired binding to
FT PtdIns(3,4,5)P(3)-containing vesicles; when associated with
FT E-154, E-160 and E-161. Strongly impaired binding to
FT PtdIns(3,4,5)P(3)-containing vesicles; when associated with
FT E-154, E-160, E-161, E-172, E-175 and E-189."
FT /evidence="ECO:0000269|PubMed:28584166"
FT MUTAGEN 160..161
FT /note="RQ->EE: Reduced binding to PtdIns(3,4,5)P(3)-
FT containing vesicles and lower capacity to mediates the
FT tubulation of liposomes. Impaired binding to
FT PtdIns(3,4,5)P(3)-containing vesicles; when associated with
FT E-154 and E-155. Strongly impaired binding to
FT PtdIns(3,4,5)P(3)-containing vesicles; when associated with
FT E-154, E-155, E-160, E-172, E-175 and E-189."
FT /evidence="ECO:0000269|PubMed:28584166"
FT MUTAGEN 172
FT /note="R->E: Strongly impaired binding to
FT PtdIns(3,4,5)P(3)-containing vesicles and lower capacity to
FT mediates the tubulation of liposomes; when associated with
FT E-154, E-155, E-160, E-161, E-173 and E-189."
FT /evidence="ECO:0000269|PubMed:28584166"
FT MUTAGEN 173
FT /note="R->E: Strongly impaired binding to
FT PtdIns(3,4,5)P(3)-containing vesicles and lower capacity to
FT mediates the tubulation of liposomes; when associated with
FT E-154, E-155, E-160, E-161, E-172 and E-189."
FT /evidence="ECO:0000269|PubMed:28584166"
FT MUTAGEN 189
FT /note="K->E: Reduced binding to PtdIns(3,4,5)P(3)-
FT containing vesicles and lower capacity to mediates the
FT tubulation of liposomes. Strongly impaired binding to
FT PtdIns(3,4,5)P(3)-containing vesicles; when associated with
FT E-154, E-155, E-160, E-161, E-172 and E-173."
FT /evidence="ECO:0000269|PubMed:28584166"
SQ SEQUENCE 368 AA; 40925 MW; FBC1EB62BCEEE9D8 CRC64;
MDAIRKQASR LREQVARQQQ AVFKQFGGGG YGSGLADEAE LNQHQKLEKL YISTRAAKHY
QRDIVRGVEG YIVTGSKQVE IGTKLSEDSR KYGSENTCTN GNVLTRAALN YGRARAQMEK
ERGNMLKALG TQVAEPLRAM VLGAPLEDAR HLAQRYDRMR QEAEAQATEV ARRQAKARES
QGNPDILMKL ESAEAKLHDL KSNMTILGKE AASALASVED QQQKLTLERL LSMVESERAY
HQRVLQILDQ LEGEMVSERQ RIEAPSTPSS ADSMPPPPSY EEANGVFASQ MHDTSTDSMG
YFLGEVLFPY HGVTDVELSL STGEYVVVRK VTGSGWAEGE CKGKAGWFPY GYIERRERVL
ASKVSEVF
