PSD_DROME
ID PSD_DROME Reviewed; 1601 AA.
AC E1JIT7; A8JR81; A8JR82; A8WHG2; C0PUX2; E2QD55; E2QD56; Q8MRV5;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=PH and SEC7 domain-containing protein {ECO:0000305};
DE AltName: Full=Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6 {ECO:0000303|PubMed:28607459, ECO:0000312|FlyBase:FBgn0051158};
DE Short=Exchange factor for Arf 6 {ECO:0000303|PubMed:28607459, ECO:0000312|FlyBase:FBgn0051158};
GN Name=Efa6 {ECO:0000303|PubMed:28607459, ECO:0000312|FlyBase:FBgn0051158};
GN Synonyms=CG18185 {ECO:0000312|FlyBase:FBgn0051158},
GN CG6941 {ECO:0000312|FlyBase:FBgn0051158},
GN dPsd {ECO:0000303|PubMed:28607459, ECO:0000312|FlyBase:FBgn0051158};
GN ORFNames=CG31158 {ECO:0000312|FlyBase:FBgn0051158};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAM51104.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1017-1601.
RC STRAIN=Berkeley; TISSUE=Embryo {ECO:0000312|EMBL:AAM51104.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:ABX00730.1, ECO:0000312|EMBL:ACN62431.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 329-1601 (ISOFORM C), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1123-1601 (ISOFORM G).
RA Booth B., Carlson J., Frise E., Kapadia B., Park S., Sandler J.,
RA Stapleton M., Wan K., Yu C., Celniker S.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28607459; DOI=10.1038/mp.2017.112;
RG IMAGEN Consortium;
RA Gonzalez D.A., Jia T., Pinzon J.H., Acevedo S.F., Ojelade S.A., Xu B.,
RA Tay N., Desrivieres S., Hernandez J.L., Banaschewski T., Buechel C.,
RA Bokde A.L.W., Conrod P.J., Flor H., Frouin V., Gallinat J., Garavan H.,
RA Gowland P.A., Heinz A., Ittermann B., Lathrop M., Martinot J.L., Paus T.,
RA Smolka M.N., Rodan A.R., Schumann G., Rothenfluh A.;
RT "The Arf6 activator Efa6/PSD3 confers regional specificity and modulates
RT ethanol consumption in Drosophila and humans.";
RL Mol. Psychiatry 23:621-628(2018).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH TUBULIN, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MOTIF, AND
RP MUTAGENESIS OF 233-SER--PRO-236 AND 262-SER--PRO-265.
RX PubMed=31718774; DOI=10.7554/elife.50319;
RA Qu Y., Hahn I., Lees M., Parkin J., Voelzmann A., Dorey K., Rathbone A.,
RA Friel C.T., Allan V.J., Okenve-Ramos P., Sanchez-Soriano N., Prokop A.;
RT "Efa6 protects axons and regulates their growth and branching by inhibiting
RT microtubule polymerisation at the cortex.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: Guanine nucleotide exchange factor for Arf6
CC (PubMed:28607459). Regulates axon growth and branching by inhibiting
CC microtubule polymerisation at the cortex (PubMed:31718774). Together
CC with shot, promotes axonal microtubule bundle integrity
CC (PubMed:31718774). Required for normal ethanol-induced tolerance and
CC preference (PubMed:28607459). Probably by activating Arf6, counteracts
CC ethanol-induced sedation (PubMed:28607459).
CC {ECO:0000269|PubMed:28607459, ECO:0000269|PubMed:31718774}.
CC -!- SUBUNIT: Interacts (via MTED motif) with tubulin.
CC {ECO:0000269|PubMed:31718774}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:31718774}. Cytoplasm {ECO:0000269|PubMed:31718774}.
CC Cell membrane {ECO:0000269|PubMed:31718774}; Peripheral membrane
CC protein {ECO:0000269|PubMed:31718774}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:31718774}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=H {ECO:0000312|FlyBase:FBgn0051158};
CC IsoId=E1JIT7-1; Sequence=Displayed;
CC Name=C {ECO:0000312|FlyBase:FBgn0051158};
CC IsoId=E1JIT7-2; Sequence=VSP_060537, VSP_060539;
CC Name=D {ECO:0000312|FlyBase:FBgn0051158};
CC IsoId=E1JIT7-3; Sequence=VSP_060537;
CC Name=G {ECO:0000312|FlyBase:FBgn0051158};
CC IsoId=E1JIT7-4; Sequence=VSP_060537, VSP_060539, VSP_060541;
CC Name=I {ECO:0000312|FlyBase:FBgn0051158};
CC IsoId=E1JIT7-5; Sequence=VSP_060537, VSP_060540;
CC -!- TISSUE SPECIFICITY: Expressed in the head (at protein level).
CC {ECO:0000269|PubMed:28607459, ECO:0000269|PubMed:31718774}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the central nervous system at
CC larval and adult stages. {ECO:0000269|PubMed:31718774}.
CC -!- DISRUPTION PHENOTYPE: Viable but male sterile (PubMed:28607459).
CC Results in enhances preference and sensitivity to ethanol
CC (PubMed:28607459). Fails to develop tolerance to repeated ethanol
CC exposures (PubMed:28607459). Increases axon length and axon branching
CC (PubMed:31718774). RNAi-mediated knockdown increases axon length and
CC axon branching (PubMed:31718774). RNAi-mediated knockdown in a subset
CC of lamina neurons results in axonal swellings and disorganized axonal
CC microtubules (PubMed:31718774). {ECO:0000269|PubMed:28607459,
CC ECO:0000269|PubMed:31718774}.
CC -!- SIMILARITY: Belongs to the PSD family. {ECO:0000305}.
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DR EMBL; AE014297; AAF56027.4; -; Genomic_DNA.
DR EMBL; AE014297; AAO41590.3; -; Genomic_DNA.
DR EMBL; AE014297; ABW08731.1; -; Genomic_DNA.
DR EMBL; AE014297; ABW08732.1; -; Genomic_DNA.
DR EMBL; AE014297; ACZ94987.2; -; Genomic_DNA.
DR EMBL; AY119244; AAM51104.1; -; mRNA.
DR EMBL; BT031108; ABX00730.1; -; mRNA.
DR EMBL; BT072828; ACN62431.1; -; mRNA.
DR RefSeq; NP_001097873.1; NM_001104403.2. [E1JIT7-2]
DR RefSeq; NP_001097874.1; NM_001104404.2. [E1JIT7-3]
DR RefSeq; NP_001163691.2; NM_001170220.2. [E1JIT7-1]
DR RefSeq; NP_732769.3; NM_170027.4. [E1JIT7-4]
DR RefSeq; NP_788718.3; NM_176541.3. [E1JIT7-5]
DR AlphaFoldDB; E1JIT7; -.
DR SMR; E1JIT7; -.
DR STRING; 7227.FBpp0112308; -.
DR PRIDE; E1JIT7; -.
DR EnsemblMetazoa; FBtr0113395; FBpp0112307; FBgn0051158. [E1JIT7-2]
DR EnsemblMetazoa; FBtr0113396; FBpp0112308; FBgn0051158. [E1JIT7-3]
DR EnsemblMetazoa; FBtr0302187; FBpp0291397; FBgn0051158. [E1JIT7-4]
DR EnsemblMetazoa; FBtr0334559; FBpp0306626; FBgn0051158. [E1JIT7-1]
DR EnsemblMetazoa; FBtr0334560; FBpp0306627; FBgn0051158. [E1JIT7-5]
DR GeneID; 42665; -.
DR KEGG; dme:Dmel_CG31158; -.
DR CTD; 42665; -.
DR FlyBase; FBgn0051158; Efa6.
DR VEuPathDB; VectorBase:FBgn0051158; -.
DR eggNOG; KOG0932; Eukaryota.
DR GeneTree; ENSGT00940000155061; -.
DR HOGENOM; CLU_005163_1_0_1; -.
DR OMA; MCEELEQ; -.
DR OrthoDB; 274195at2759; -.
DR SignaLink; E1JIT7; -.
DR BioGRID-ORCS; 42665; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Efa6; fly.
DR GenomeRNAi; 42665; -.
DR PRO; PR:E1JIT7; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0051158; Expressed in cleaving embryo and 22 other tissues.
DR ExpressionAtlas; E1JIT7; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0044297; C:cell body; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:FlyBase.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0035082; P:axoneme assembly; IMP:UniProtKB.
DR GO; GO:0001745; P:compound eye morphogenesis; IGI:UniProtKB.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IMP:UniProtKB.
DR GO; GO:0032014; P:positive regulation of ARF protein signal transduction; ISS:FlyBase.
DR GO; GO:0097305; P:response to alcohol; IGI:UniProtKB.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR001605; PH_dom-spectrin-type.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF01369; Sec7; 1.
DR PRINTS; PR00683; SPECTRINPH.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Reference proteome.
FT CHAIN 1..1601
FT /note="PH and SEC7 domain-containing protein"
FT /evidence="ECO:0000305"
FT /id="PRO_0000449250"
FT DOMAIN 6..88
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1125..1291
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 1332..1445
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..340
FT /note="Mediates regulation of axon branching and
FT microtubule organization"
FT /evidence="ECO:0000269|PubMed:31718774"
FT REGION 113..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..1601
FT /note="Mediates association to the membrane and rescricts
FT the microtubule-inhibiting activity to the cell cortex"
FT /evidence="ECO:0000269|PubMed:31718774"
FT REGION 1040..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1544..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 323..340
FT /note="Microtubule elimination domain (MTED); Binds tubulin
FT and blocks microtubule polymerization"
FT /evidence="ECO:0000269|PubMed:31718774"
FT COMPBIAS 256..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..505
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..555
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 729..808
FT /note="Missing (in isoform C, isoform D, isoform G and
FT isoform I)"
FT /evidence="ECO:0000305"
FT /id="VSP_060537"
FT VAR_SEQ 881..1014
FT /note="Missing (in isoform C and isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_060539"
FT VAR_SEQ 1595..1601
FT /note="RKEKKKK -> SPPRISVSTNLAWRKIFWDSVCCGVLLCCWHYCTVLTVIP
FT (in isoform I)"
FT /evidence="ECO:0000305"
FT /id="VSP_060540"
FT VAR_SEQ 1596..1601
FT /note="KEKKKK -> WFDVFCCCCPLWRHLIHSKSH (in isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_060541"
FT MUTAGEN 233..236
FT /note="SRIP->AAAA: Depletion of microtubule network leading
FT to axon loss; when associated with 262-A--A-265."
FT /evidence="ECO:0000269|PubMed:31718774"
FT MUTAGEN 262..265
FT /note="SQIP->AAAA: Depletion of microtubule network leading
FT to axon loss; when associated with 233-A--A-236."
FT /evidence="ECO:0000269|PubMed:31718774"
FT CONFLICT 410
FT /note="K -> KQ (in Ref. 4; ABX00730)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="L -> V (in Ref. 4; ABX00730)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="P -> S (in Ref. 4; ABX00730)"
FT /evidence="ECO:0000305"
FT CONFLICT 1106
FT /note="T -> M (in Ref. 3; AAM51104 and 4; ABX00730)"
FT /evidence="ECO:0000305"
FT CONFLICT 1366
FT /note="L -> V (in Ref. 4; ABX00730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1601 AA; 176440 MW; F39FC9D187C83B72 CRC64;
MSEELKVVLR RSEQHSGFGF SLLGTTGPPH VIYDIVENSP AADCGAVEAG DVILKVNGTD
VHRYTTKEVL KCLRLSEQLV TLELKRDPKL KARIKEQLAN TQSPHYVDIE SPNIYDYHSS
STNSSPNHRP NAGGKGAATT PSQTGLRYKS PTHLPSLRQN SSPLLASGST TTTTTATHTH
SHSRNSSASS TKIKVVETSI TTSTTNVVGL TSPTGSVGGG VGGEATSPTF RPSRIPQALT
KCAVPKPVPV LHSPQNKRPR PSQIPTKAAN GNGNGHTAHL PPQSLQHSNS YSGSPVTRQR
FADREPEREP EPNSAPPQPA KAPRFEAYMM TGDLILNLSR TPQTSNPLPA QAKKIDSLRD
SPSRLVNPRI NGALAPRASG ESSPTSSSSV DSPTNTSSDS VKREAKLLQK QQQQQQQTYQ
QQQQRDSINN SYNRKDSLTN DTLLMCEELE PDEEGEYVLE EDNKQQRQRQ QQQRYRQQQN
QQRYEYYQNE DELEEQEEVE EEREEDQTHY DITNIETYQS GVGRGDDDDS DRQCLVDDDD
DDDAYDDEEN DAGDEDYSTN SLGSGSAKQR LRALKQRTAT RQQQRNRDAV DCAGRSGSGS
SSTTVKSEAG GLGLDETSFS VPTSPISLST PLIDKETANS VPTSPEPSSL VPESSSGAGA
GAVVVRRHNG HVVRKCDAAG FRTSKSEDHL QQIQREGIAA VIPIDIDEDV NSSLNTLLDT
RQDSEDSQSM ATVIVNNSSL ASNNNEGEQT DNRSSSSSSN SSDNNNCSSN TGEPATSETA
TATATIITAT STRTMNCSSK LNYILCKKAS DRDRIVWTYN APLQPHQLAA LQRQQQQQEQ
QFQQQQQQLH QQHLQQQQQL QQQHQQQQQQ QQQQQQQQLY GQQSHSNSHS SSISSSPQHS
AVGSPASPTS VSSSVMSSSG SKGALGLGSS SNGPMAAVQQ QQLREREQGG QVAQPPSGIP
GLLSCPGGGC GNNGGGGGIG GGGNNDQSVS EAISNISSPD YQDDDNLLSS RDILGGMVLS
DPSDSDSTIL VSDAAAHQRQ QLKQQLRAQQ QQQRERERDR DRDREQSEHK VVIQVRGLDS
NSSGGNGTNG RSEEDVVTLT DEPLGTMTVG MRDASPPVSD DGSDVESLHS YHYSPKAVDM
PSAIRLAKRL HSLDGFKKSD VSRHLSKNND FSRAVADEYL KHFTFEKKSL DQALREFLQQ
FSLSGETQER ERVLVHFSKR FLDCNPGTFN SQDAVHTLTC AIMLLNTDLH GQNINRKMSC
AEFVDNLADL NDGENFPKDV LKSLYQAIKT KPLEWALDEE AGDLQQQRAN NSALGNVGLN
PFLDPPELAT AVEYKKGYVM RKCCYDSSFK KTPFGKRSWK MFYCTLRDLV LYLHKDEHGF
RKSQMSDNLH NAIRIHHALA TKANDYTKKQ HVFRLQTADQ AEYLFQTSDS KELQSWVETI
NYVCAAISAP PLEGGVGSQK RFQRPLLPSK QSKLMLKEQL DSHEVQLAQL DQELNEHKKG
PIPSKGLALQ NYKEKESYLQ YELRRYRTYV SILSAKMLAD QQQLELQAQQ PSPASHEEEA
DTFPVGTTAC TPPTPQSINQ KDQQKEQQQQ QPTNRKEKKK K
