FAB1A_ARATH
ID FAB1A_ARATH Reviewed; 1757 AA.
AC Q0WUR5; Q9SMY5;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase FAB1A;
DE Short=Phosphatidylinositol 3-phosphate 5-kinase;
DE EC=2.7.1.150 {ECO:0000305|PubMed:21173023};
DE AltName: Full=FYVE finger-containing phosphoinositide kinase;
DE AltName: Full=PIKfyve;
DE AltName: Full=Phosphatidylinositol 3-phosphate 5-kinase type III;
DE Short=PIPkin-III;
DE Short=Type III PIP kinase;
DE AltName: Full=Protein FORMS APLOID AND BINUCLEATE CELLS 1A;
GN Name=FAB1A; OrderedLocusNames=At4g33240; ORFNames=F4I10.170;
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=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 [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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND REVIEW.
RX PubMed=12226484; DOI=10.1104/pp.004770;
RA Mueller-Roeber B., Pical C.;
RT "Inositol phospholipid metabolism in Arabidopsis. Characterized and
RT putative isoforms of inositol phospholipid kinase and phosphoinositide-
RT specific phospholipase C.";
RL Plant Physiol. 130:22-46(2002).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19846542; DOI=10.1104/pp.109.146159;
RA Whitley P., Hinz S., Doughty J.;
RT "Arabidopsis FAB1/PIKfyve proteins are essential for development of viable
RT pollen.";
RL Plant Physiol. 151:1812-1822(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=21173023; DOI=10.1104/pp.110.167981;
RA Hirano T., Matsuzawa T., Takegawa K., Sato M.H.;
RT "Loss-of-function and gain-of-function mutations in FAB1A/B impair
RT endomembrane homeostasis, conferring pleiotropic developmental
RT abnormalities in Arabidopsis.";
RL Plant Physiol. 155:797-807(2011).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21412048; DOI=10.4161/psb.6.4.15023;
RA Hirano T., Sato M.H.;
RT "Arabidopsis FAB1A/B is possibly involved in the recycling of auxin
RT transporters.";
RL Plant Signal. Behav. 6:583-585(2011).
CC -!- FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis
CC and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
CC Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on
CC the fifth hydroxyl of the myo-inositol ring, to form
CC phosphatidylinositol 3,5-bisphosphate (By similarity). Plays an
CC important role in maintenance of endomembrane homeostasis including
CC endocytosis, vacuole formation, and vacuolar acidification processes.
CC Required for development of viable pollen. Might mediate recycling of
CC auxin transporters. {ECO:0000250, ECO:0000269|PubMed:19846542,
CC ECO:0000269|PubMed:21173023, ECO:0000269|PubMed:21412048}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:13609,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57923,
CC ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.150;
CC Evidence={ECO:0000305|PubMed:21173023};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex at least
CC composed of ATG18, SAC/FIG4, FAB1 and VAC14. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:21173023};
CC Peripheral membrane protein {ECO:0000269|PubMed:21173023}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Name=1;
CC IsoId=Q0WUR5-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous with highest expression levels in
CC pollen, seed, and senescent leaves. {ECO:0000269|PubMed:19846542}.
CC -!- DISRUPTION PHENOTYPE: Leaf-curling phenotype. Root growth inhibition,
CC root gravitropic response, and hyposensitivity to exogenous auxin.
CC Fab1a and fab1b double mutant displays an abnormal vacuolar phenotype
CC late in pollen development leading to inviable pollen
CC (PubMed:19846542). {ECO:0000269|PubMed:19846542,
CC ECO:0000269|PubMed:21173023, ECO:0000269|PubMed:21412048}.
CC -!- MISCELLANEOUS: [Isoform 1]: A number of isoforms are produced.
CC According to EST sequences.
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; AL035525; CAB36798.1; -; Genomic_DNA.
DR EMBL; AL161583; CAB80041.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86194.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66882.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66883.1; -; Genomic_DNA.
DR EMBL; AK227081; BAE99133.1; -; mRNA.
DR PIR; T05204; T05204.
DR RefSeq; NP_001320122.1; NM_001342205.1. [Q0WUR5-1]
DR RefSeq; NP_001328751.1; NM_001342208.1. [Q0WUR5-1]
DR RefSeq; NP_195050.6; NM_119478.7. [Q0WUR5-1]
DR AlphaFoldDB; Q0WUR5; -.
DR SMR; Q0WUR5; -.
DR STRING; 3702.AT4G33240.1; -.
DR iPTMnet; Q0WUR5; -.
DR PaxDb; Q0WUR5; -.
DR PRIDE; Q0WUR5; -.
DR ProteomicsDB; 230784; -. [Q0WUR5-1]
DR EnsemblPlants; AT4G33240.1; AT4G33240.1; AT4G33240. [Q0WUR5-1]
DR EnsemblPlants; AT4G33240.6; AT4G33240.6; AT4G33240. [Q0WUR5-1]
DR EnsemblPlants; AT4G33240.7; AT4G33240.7; AT4G33240. [Q0WUR5-1]
DR GeneID; 829460; -.
DR Gramene; AT4G33240.1; AT4G33240.1; AT4G33240. [Q0WUR5-1]
DR Gramene; AT4G33240.6; AT4G33240.6; AT4G33240. [Q0WUR5-1]
DR Gramene; AT4G33240.7; AT4G33240.7; AT4G33240. [Q0WUR5-1]
DR KEGG; ath:AT4G33240; -.
DR Araport; AT4G33240; -.
DR TAIR; locus:2125884; AT4G33240.
DR eggNOG; KOG0230; Eukaryota.
DR InParanoid; Q0WUR5; -.
DR OrthoDB; 227882at2759; -.
DR PhylomeDB; Q0WUR5; -.
DR BioCyc; ARA:AT4G33240-MON; -.
DR PRO; PR:Q0WUR5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0WUR5; baseline and differential.
DR Genevisible; Q0WUR5; AT.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IGI:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010256; P:endomembrane system organization; IGI:TAIR.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0007033; P:vacuole organization; IGI:TAIR.
DR CDD; cd17300; PIPKc_PIKfyve; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.800.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR044769; PIKfyve_PIPKc.
DR InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF01504; PIP5K; 2.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Endosome; Kinase; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1757
FT /note="1-phosphatidylinositol-3-phosphate 5-kinase FAB1A"
FT /id="PRO_0000421870"
FT DOMAIN 1395..1719
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT ZN_FING 36..102
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 125..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1729..1757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1014..1087
FT /evidence="ECO:0000255"
FT COMPBIAS 125..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..337
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT CONFLICT 279
FT /note="Q -> H (in Ref. 1; CAB36798/CAB80041)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="N -> T (in Ref. 1; CAB36798/CAB80041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1757 AA; 196193 MW; 0F7AF38EE610CD5A CRC64;
MDSQDHKAPG FVDIVKSWIP RKSESSNMSR DFWMPDQSCP VCYECDAQFT VFNRRHHCRL
CGRVFCAKCA ANSIPSPSDE TKDSHEEPER IRVCNYCYKQ WEQGIVPPDN GASIISLHFS
SSPSARSVAS TTSNSSNCTI DSTAGPSPRP KMNPRASRRV SSNMDSEKSE QQNAKSRRSS
DHYGHVLDSS DNQVEFFVNS SGRSDGEADD DDDYQSDFAQ SYAQGNDYYG AINLDEVDHI
YGSHEAHDVG VKIEPNISGF PPDQDLDSLN TETIDKTRQQ ENGWNDVKEG SPPCEESFEP
EVVDFESDGL LWLPPEPENE EDEREAVLSD DDGDEGDRGD WGYLRPSNSF NEKDFHSKDK
SSGAMKNVVE GHFRALVAQL LEVDNLPMVN EGDEEGWLDI ITSLSWEAAT LLKPDTSKSG
GMDPGGYVKV KCIPCGRRSE SMVVKGVVCK KNVAHRRMTS KIEKPRLLIL GGALEYQRIS
NQLSSFDTLL QQEMDHLKMA VAKIDSHNPD ILLVEKSVSR FAQEYLLAKD ISLVLNIKRS
LLERISRCTG AQIVPSIDQL TSPKLGYCDL FHVEKFVETH VSPCQVAKKM AKTLMFFDGC
PKPLGCTILL KGAHEDELKK VKHVIQYGVF AAYHLALETS FLADEGASIH ELPLQTPITV
ALPDKPSMVN RSISTIPGFT VSSAEKSPTT ELRGEPHKAN GDLTGNFTSS KTHFQGKLDG
NDRIDPSERL LHNLDTVYCK PPETITSKDD GLVPTLESRQ LSFHVEEPSV QKDQWSVLSG
ATEQVTDGGY TNDSAVIGNQ NFNRQEQMES SKGDFHPSAS DHQSILVSLS TRCVWKGSVC
ERAHLLRIKY YGSFDKPLGR FLRDNLFDQD QCCPSCTMPA EAHIHCYTHR QGSLTISVKK
LPELLPGQRE GKIWMWHRCL KCPRINGFPP ATRRIVMSDA AWGLSFGKFL ELSFSNHAAA
SRVANCGHSL HRDCLRFYGF GRMVACFRYA SINIYAVTLP PAKLYFNYEN QEWLQKESKE
VIKKAEVLFN EVQEALSQIS AKTMGAGSKG STPNKIKLSL EELAGLLEQR KKEYKDSLQQ
MLNVVKDGQP TIDILLINKL RRLIIFDSYA WDECLAGAAN MVRNNYLEAP KNSAPKVMGR
NVSLEKLSDE KVKSIPTHVA ICNDSLLQDA DYETCLNQGK SFADTSGKFA IPEDVGSDRP
PDCRMEFDPS EGGKDNFVES SQVVKPAHTE SQFQATDLSD TLDAAWIGEQ TTSENGIFRP
PSRAASTNGT QIPDLRLLGS ESELNFKGGP TNDEHTTQVQ LPSPSFYYSL NKNYSLNSRK
HIMAEDRPVY VSSYRELEWR SGARLLLPLG CNDLVLPVYD DEPTSIIAYA LTSSEYKAQM
SGSDKSRDRL DSGGSFSLFD SVNLLSLNSL SDLSVDMSRS LSSADEQVSQ LLHSSLYLKD
LHARISFTDE GPPGKVKYSV TCYYAKEFEA LRMICCPSET DFIRSLGRCR KWGAQGGKSN
VFFAKSLDDR FIIKQVTKTE LESFIKFGPA YFKYLTESIS TKSPTSLAKI LGIYQVSSKH
LKGGKEFKMD VLVMENLLFK RNFTRLYDLK GSTRARYNPD TSGSNTVLLD QNLVEAMPTS
PIFVGSKAKR LLERAVWNDT SFLASIHVMD YSLLVGVDEE RNELVLGIID FMRQYTWDKH
LETWVKTSGL LGGPKNSTPT VISPQQYKKR FRKAMTAYFL MVPDQWSPAA VVPSNSSSAE
VKEEEEKDNP QAVGNKS
