IPLA_DICDI
ID IPLA_DICDI Reviewed; 3177 AA.
AC Q9NA13; Q54D11;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor-like protein A;
GN Name=iplA; ORFNames=DDB_G0292564;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=10970875; DOI=10.1093/emboj/19.17.4846;
RA Traynor D., Milne J.L.S., Insall R.H., Kay R.R.;
RT "Ca(2+) signalling is not required for chemotaxis in Dictyostelium.";
RL EMBO J. 19:4846-4854(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12211100; DOI=10.1002/cm.10068;
RA Levi S., Polyakov M.V., Egelhoff T.T.;
RT "Myosin II dynamics in Dictyostelium: determinants for filament assembly
RT and translocation to the cell cortex during chemoattractant responses.";
RL Cell Motil. Cytoskeleton 53:177-188(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15760480; DOI=10.1186/1471-2121-6-13;
RA Schaloske R.H., Lusche D.F., Bezares-Roder K., Happle K., Malchow D.,
RA Schlatterer C.;
RT "Ca2+ regulation in the absence of the iplA gene product in Dictyostelium
RT discoideum.";
RL BMC Cell Biol. 6:13-13(2005).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17077123; DOI=10.1242/jcs.03248;
RA Shanley L.J., Walczysko P., Bain M., MacEwan D.J., Zhao M.;
RT "Influx of extracellular Ca2+ is necessary for electrotaxis in
RT Dictyostelium.";
RL J. Cell Sci. 119:4741-4748(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18196962; DOI=10.4161/auto.5521;
RA Lam D., Golstein P.;
RT "A specific pathway inducing autophagic cell death is marked by an IP3R
RT mutation.";
RL Autophagy 4:349-350(2008).
RN [7]
RP FUNCTION.
RX PubMed=17854889; DOI=10.1016/j.ceca.2007.08.002;
RA Malchow D., Lusche D.F., De Lozanne A., Schlatterer C.;
RT "A fast Ca2+-induced Ca2+-release mechanism in Dictyostelium discoideum.";
RL Cell Calcium 43:521-530(2008).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=18486207; DOI=10.1016/j.ceca.2008.04.001;
RA Ludlow M.J., Traynor D., Fisher P.R., Ennion S.J.;
RT "Purinergic-mediated Ca2+ influx in Dictyostelium discoideum.";
RL Cell Calcium 44:567-579(2008).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18077554; DOI=10.1091/mbc.e07-08-0823;
RA Lam D., Kosta A., Luciani M.F., Golstein P.;
RT "The inositol 1,4,5-trisphosphate receptor is required to signal autophagic
RT cell death.";
RL Mol. Biol. Cell 19:691-700(2008).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19133302; DOI=10.1016/j.bbamcr.2008.12.005;
RA Giusti C., Tresse E., Luciani M.-F., Golstein P.;
RT "Autophagic cell death: Analysis in Dictyostelium.";
RL Biochim. Biophys. Acta 1793:1422-1431(2009).
CC -!- FUNCTION: May be a receptor for inositol 1,4,5 trisphosphate which
CC governs calcium fluxes from the endoplasmic reticulum stores into the
CC cytosol. May be involved in autophagic cell death.
CC {ECO:0000269|PubMed:10970875, ECO:0000269|PubMed:12211100,
CC ECO:0000269|PubMed:15760480, ECO:0000269|PubMed:17077123,
CC ECO:0000269|PubMed:17854889, ECO:0000269|PubMed:18077554,
CC ECO:0000269|PubMed:18196962, ECO:0000269|PubMed:19133302}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expression is low during growth and rises to a
CC peak at 9 hours of development when chemotactic aggregation to cyclic
CC AMP is near its height; levels then decrease through the end of
CC development. {ECO:0000269|PubMed:10970875}.
CC -!- DISRUPTION PHENOTYPE: Null cells show abolition of calcium entry in
CC response to chemoattractant, response to cyclic AMP and normal increase
CC in free cytosolic calcium that follows chemotactic stimulation. Cells
CC show formation of smaller fruiting bodies and abolition of autophagic
CC cell death. Cells show absence of vacuolization.
CC {ECO:0000269|PubMed:10970875, ECO:0000269|PubMed:12211100,
CC ECO:0000269|PubMed:15760480, ECO:0000269|PubMed:17077123,
CC ECO:0000269|PubMed:18077554, ECO:0000269|PubMed:18196962,
CC ECO:0000269|PubMed:18486207, ECO:0000269|PubMed:19133302}.
CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
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DR EMBL; AJ277590; CAB97127.1; -; Genomic_DNA.
DR EMBL; AAFI02000194; EAL61085.1; -; Genomic_DNA.
DR RefSeq; XP_629509.1; XM_629507.1.
DR STRING; 44689.DDB0201571; -.
DR PaxDb; Q9NA13; -.
DR PRIDE; Q9NA13; -.
DR EnsemblProtists; EAL61085; EAL61085; DDB_G0292564.
DR GeneID; 8628760; -.
DR KEGG; ddi:DDB_G0292564; -.
DR dictyBase; DDB_G0292564; iplA.
DR eggNOG; KOG3533; Eukaryota.
DR HOGENOM; CLU_225557_0_0_1; -.
DR InParanoid; Q9NA13; -.
DR OMA; GCYINIL; -.
DR Reactome; R-DDI-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-DDI-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-DDI-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-DDI-5578775; Ion homeostasis.
DR Reactome; R-DDI-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR PRO; PR:Q9NA13; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:dictyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:dictyBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0005262; F:calcium channel activity; ISS:dictyBase.
DR GO; GO:0005509; F:calcium ion binding; IMP:dictyBase.
DR GO; GO:0015085; F:calcium ion transmembrane transporter activity; ISS:dictyBase.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IEA:InterPro.
DR GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISS:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0048102; P:autophagic cell death; IMP:dictyBase.
DR GO; GO:0032060; P:bleb assembly; IMP:dictyBase.
DR GO; GO:0006816; P:calcium ion transport; IMP:dictyBase.
DR GO; GO:0097231; P:cell motility in response to calcium ion; IMP:dictyBase.
DR GO; GO:0030244; P:cellulose biosynthetic process; IMP:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0034670; P:chemotaxis to arachidonic acid; IMP:dictyBase.
DR GO; GO:1903665; P:negative regulation of asexual reproduction; IMP:dictyBase.
DR GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:dictyBase.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000493; InsP3_rcpt.
DR InterPro; IPR013662; RIH_assoc-dom.
DR InterPro; IPR000699; RIH_dom.
DR InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
DR Pfam; PF08454; RIH_assoc; 1.
DR Pfam; PF01365; RYDR_ITPR; 2.
DR PRINTS; PR00779; INSP3RECEPTR.
DR SUPFAM; SSF100909; SSF100909; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Calcium; Calcium channel; Calcium transport; Coiled coil;
KW Endoplasmic reticulum; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..3177
FT /note="Inositol 1,4,5-trisphosphate receptor-like protein
FT A"
FT /id="PRO_0000384448"
FT TOPO_DOM 1..1175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1176..1196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1197..2723
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2724..2744
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2745..2769
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2770..2790
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2791..2853
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2854..2874
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2875..2896
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2897..2917
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2918..2995
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2996..3016
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3017..3177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 62..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1715..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2050..2069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2125..2188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3118..3177
FT /evidence="ECO:0000255"
FT COMPBIAS 72..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289..293
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 608..611
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 692..694
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT CARBOHYD 1275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1731
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1736
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1768
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1833
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2035
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2048
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 3177 AA; 360531 MW; 381ECEA20A7C84A2 CRC64;
MEEKNVNLKT GDLVTFFSEQ EEEDGYFSKS HDSAVMSNNK SKDCVFKVYP FTQYTARKAL
KKKAKRKLQQ QQADGADANN TNSSSGGGNS NNNNNNNSNS SNNNNSSNNN NNNNNNGTTN
ANGENVNNEV TDLELKQLEE YQDLEDVSNE STLIQLEGRD LVYGQIVQLY QPSSNQFLFA
RNNIVGFRQD GSQKCYFKIT PRFQNQDGCK VFSEDLVLLR HEKTGLFLNQ QNFIIDQGVF
GIGLSENGTF WKMAVSDVDG KSGLNILKAN EPFRLFHREG GFVKVSNDKT TFTYNTKTPS
SINSLFEIEF ENNNLISPLL RSQKDLQLQQ KDNTDQLQQQ QQKDKDKDNP LKQSYGSLSN
SNILLQNNNN NNNNNNSNNN NNSNNNSNNS NGNNSNGNNN NNNSNNIFTS NEVHIGQSFW
IRLVGTKKYL SLKESSDDSL KDNPLIVVTE DQKYSPSATF SFVKRDKANE DVIFGSFVRI
QSLSKQYLHF ISDETFHHNG ELVGSKKYYK NDDFQIKQIP KSQLEDYGFV LSRINKIQNY
LYQSSSNSSS SLMSSINGIG QSSFSSLAGA TTTTTNSGGS NNINNNNNNN NNNNNNNNNN
NNNNNNNNID KKRATVQEIK AIIVEFIKFC TQSEVEDPLD REGTPIKTHQ KLLSHPSHLS
VLLDYLKRLF EPFDPASILF VYRLLKQMAK SNIKNGIIIN EHLDQISPPS IRDKTIPLHF
GAILYEVYKN NNILLEALTE DKVQEFINVI KQKKEPKYME LLSEICICYG KPIVKNQQYL
CDLLLEKNSN LLFKTRVIGG SLEIERQNPA PKWVDITAFA LSVDEKTHRY FEQSLALYSN
VSKGRNYNGI RLVGQRITHK ECLLALKEES LPYSLRGCYI NILIHVYMDC HPQHYVPQIN
YVWNPSIVNN TKTIELLQLY QQYNITGSLH QRNSSIQNPY STVSNGNISI SSNNPISTTN
TTTGSGGGGG GSGFMPTVGP SYGQASSPLS NGAIVNSLAS TNLNNQTPTS LNLFNLNSPN
NTTTTTNNST NNTTNNNTNN NNNNNNTNSL ITSTTHLIQL VSPQQNNNSN NNNNNNILNS
IPTSPIVGST NHGQLSHSGS NQTPLYQQQQ QQQQQQQQQN SLSLFREDDI FSTFVNLEIQ
ADKEPSTTTQ LLISLLSKSE YFSNFNNGFP TSHRPQLAFF HKILIAVGYA FKFGFFRKKE
RVLLKRLRYI LEFEHEPVNT FKEVDLGRTM GGSRMLEDES VIYVSIKIEI VNILHLMLSF
QKKNIMDVFL YDFSNMSQSA FSQPENVKNQ LIDRLTTNYQ RDGHQDLSLC TVLFKLLKHE
NNQLSSLSLS LLNRIYKYRS IYAMLWSPIQ KLFLLPNELT PTYKESLQKM ESLTVTCFAP
LTDDSTQESL RSLAFFIHLV TDSDPIKLVK NQKLLHVIGV HKTIIGVLKI GCSLDDLILD
QSQPQHSQQQ QQQHQQQPIN ISGSIDESSS TIPPLTTTTT TTTTTTTTTT TTQQSINFKS
LLNSKTNSQS IHVAKIFRSC YEFLKVFCRD NRENQKVLFG EIEFLIGHLI RYGNVFGTVE
TLIEVFKNNI ELAINFGNSP YLKLLVKFII NLSIDQLDPM FLRLLSVLIL PCNENSVIEN
QISVTNLFKE YKSKISKLLV PISTMKEVMK DPKLLSKHYN VNSSNVYKLH LALQEILNHS
LNDDGAGIGI GTTVIGGSII GGSITTTAQT NINTITNTPT NNNSNNSNNN NTTNNNGTIS
HRHSNSTNTT QSVYPRLIRS SAKAQIVNSS VEILPKEFVI NLELILLLKA CSHGINTPTE
VICREFLSMG ECFDILIVRS DGNGKENSSL MINETKEYLE NNLLFRFKSA YLSFLHEVFF
NSDTLKGDLL ALQLNHDLWS LIDQFTNQLN HLVTICAMNQ MGQLYYVQMA RNIIIPMVSV
LERFYSQCFY FDKATQIHLT YSGRLMASLM KLYWKDPSLT IPFNQQNTSR YQSSLNMSPT
NYDDSDTSEG GYHPILQGLD PEERVNIYSN LVKCLKAMDR SALSPIVPAS VSTINISNVI
KGCEDVINRT EHPNSRNRTE TIDSSNSSPP LILSKSSSIY IDFTRLNNFV KLSKIRGYTE
IAMMVNQSLS ITPFIISHPN YNSNNSNNGN NNNNNNNGGG GNGNGGTIRS NSYISGGGGG
STTKRRTSRN NSNISDISNS GKGGSTISNR FQNSFSNTFI QQQQIGITNQ RHINSGNTNI
VTTVTSKSTN FLEILVFQLR NSLYDNDEMK INCIRILSSL LYINKERKPD IQNIMTDLYC
HSAVIGLLSS KNIEIQFESL SLLLALLDDS VNVDNPLPNP KVKDDIQSHF SSSPDIQFFR
DIYAMIERAK INLRDTKRNI HRIEHVKMGN NTVLGGNLTS KNSIKSSINN GNNSNNNNNR
NGRVIDGCET NPYSTEFQLL QNIFRVLQLL CQGTTNIFKK SIRSQPDNYK SYDILKEMCQ
FLKILETIVN IDSDSIELGL RFFACMKEIV KNTPENQIAV TNVQVCKAVC NILKKTKEND
PSKELKELKY LDLKIEVVDF LLHVIDKEDP RVMSKLIPEL DYKVIESNTQ VISQRSNHET
NEKSIKLASM TFRLIKILAD NDKSHNIQLE DCLLKCGEHC KSRIGRVELL YQNKLERIYF
PIPNYSRRLI LEDKEQSKIK NDENLLQENL EEHFINNKIS WNKATEKIDA FMDYSEYKLI
ELEHLHNLKL NSMSYYLVSH TDKFKFLSFF LALIINLLLI IYSINSPPDL KQFKSDISDD
YGIASWWAGF LPLTILQTIC CILACVGFFL RKGPVLLYQN WVNYLKTHGH KKNFMFYTND
QRMHSLRQTF KYKFIPLNAK FLMTDLKAVY NILAVICSVL GIIYSPYFFA FHIFQFSLNT
KALSLVLKAI TMNKKTLLVM GVFILQAIYL LSIFSFVWFQ EHYKDDDSEY MCGSLLQCFI
TNLYYGVPSQ GQLIQFIKYN FPNNYLNTTD STGSPTLEPI KTSNTVSARI IGWTVFNVAF
YVVISLILLN VILGIIVDTF GQLRDQRAET EDYKSNVCFI CSIERETFQK NSIEFKKHIE
DDHNKWHYLY FFAYLKERCT NNQMNQLSEL ECSIADGITN RSYISFFPIE MSMSLQGIEN
ANRKKEESID QHAKLLDDVE KKITHNISTQ FNQSISLLID EIKNLRQQVS DLKQQQK
