ATC7_YEAST
ID ATC7_YEAST Reviewed; 1151 AA.
AC P40527; D6VVN3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Probable phospholipid-transporting ATPase NEO1;
DE EC=7.6.2.1;
GN Name=NEO1; OrderedLocusNames=YIL048W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INTERACTION WITH MON2, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15314152; DOI=10.1128/mcb.24.17.7402-7418.2004;
RA Wicky S., Schwarz H., Singer-Krueger B.;
RT "Molecular interactions of yeast Neo1p, an essential member of the Drs2
RT family of aminophospholipid translocases, and its role in membrane
RT trafficking within the endomembrane system.";
RL Mol. Cell. Biol. 24:7402-7418(2004).
RN [4]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-551, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of phospholipids (Potential). Leads to
CC neomycin-resistance when overexpressed. Required for traffic between
CC late Golgi and early endosomes. {ECO:0000269|PubMed:15314152,
CC ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC -!- SUBUNIT: Interacts with MON2. {ECO:0000269|PubMed:15314152}.
CC -!- INTERACTION:
CC P40527; Q03921: DOP1; NbExp=3; IntAct=EBI-3137, EBI-34442;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:15314152};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15314152}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:15314152}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:15314152}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
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; Z38060; CAA86174.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08499.1; -; Genomic_DNA.
DR PIR; S48431; S48431.
DR RefSeq; NP_012216.1; NM_001179398.1.
DR PDB; 7RD6; EM; 3.25 A; A=1-1151.
DR PDB; 7RD7; EM; 3.08 A; A=1-1151.
DR PDB; 7RD8; EM; 5.64 A; A=1-1151.
DR PDBsum; 7RD6; -.
DR PDBsum; 7RD7; -.
DR PDBsum; 7RD8; -.
DR AlphaFoldDB; P40527; -.
DR SMR; P40527; -.
DR BioGRID; 34942; 502.
DR ComplexPortal; CPX-1028; NEO1-MON2-ARL1-DOP1 membrane remodeling complex.
DR DIP; DIP-2548N; -.
DR IntAct; P40527; 7.
DR MINT; P40527; -.
DR STRING; 4932.YIL048W; -.
DR TCDB; 3.A.3.8.18; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; P40527; -.
DR MaxQB; P40527; -.
DR PaxDb; P40527; -.
DR PRIDE; P40527; -.
DR EnsemblFungi; YIL048W_mRNA; YIL048W; YIL048W.
DR GeneID; 854763; -.
DR KEGG; sce:YIL048W; -.
DR SGD; S000001310; NEO1.
DR VEuPathDB; FungiDB:YIL048W; -.
DR eggNOG; KOG0210; Eukaryota.
DR GeneTree; ENSGT00940000168130; -.
DR HOGENOM; CLU_000846_6_0_1; -.
DR InParanoid; P40527; -.
DR OMA; IAITTWH; -.
DR BioCyc; YEAST:G3O-31319-MON; -.
DR Reactome; R-SCE-936837; Ion transport by P-type ATPases.
DR PRO; PR:P40527; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40527; protein.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; ISS:SGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0045332; P:phospholipid translocation; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:SGD.
DR GO; GO:0098629; P:trans-Golgi network membrane organization; IC:ComplexPortal.
DR GO; GO:0007033; P:vacuole organization; IMP:SGD.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Endosome; Golgi apparatus; Magnesium; Membrane;
KW Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1151
FT /note="Probable phospholipid-transporting ATPase NEO1"
FT /id="PRO_0000046236"
FT TOPO_DOM 1..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..947
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 948..968
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 969..970
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 971..991
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 992..1020
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1021..1041
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1042..1052
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1053..1073
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1074..1078
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1079..1099
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1100..1109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1110..1130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1131..1151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1151
FT /note="Required for endosomal targeting"
FT COMPBIAS 73..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 503
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:7RD6"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 224..249
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 286..297
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 376..386
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 406..433
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 440..451
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 455..474
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 505..508
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 509..520
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 523..529
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 531..537
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:7RD6"
FT HELIX 561..575
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 595..607
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 610..614
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 616..619
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 621..624
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 630..638
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 642..644
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 646..656
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 659..665
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 667..670
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 671..673
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 680..688
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 689..691
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 693..702
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 704..711
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 734..736
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 741..752
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 757..765
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 769..773
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 778..787
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 823..826
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 828..837
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 839..846
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 848..850
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 852..854
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 859..872
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 877..881
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 884..886
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 887..891
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 893..899
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 901..903
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 906..910
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 911..918
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 920..926
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 928..960
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 961..963
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 966..968
FT /evidence="ECO:0007829|PDB:7RD6"
FT HELIX 972..978
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 979..982
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 983..989
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 997..999
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 1000..1002
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 1005..1010
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 1015..1017
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 1018..1043
FT /evidence="ECO:0007829|PDB:7RD7"
FT STRAND 1046..1049
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 1050..1071
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 1078..1080
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 1081..1092
FT /evidence="ECO:0007829|PDB:7RD7"
FT TURN 1096..1099
FT /evidence="ECO:0007829|PDB:7RD7"
FT HELIX 1110..1137
FT /evidence="ECO:0007829|PDB:7RD7"
SQ SEQUENCE 1151 AA; 130218 MW; DC7225CC9577DBE6 CRC64;
MPNPPSFKSH KQNLFNSNNN QHANSVDSFD LHLDDSFDAA LDSLQINNNP EPLSKHNTVG
DRESFEMRTV DDLDNFSNHS SDSHRKSSNT DTHPLMYDNR LSQDDNFKFT NIASSPPSSS
NNIFSKALSY LKVSNTKNWS KFGSPIELSD QHIEREIHPD TTPVYDRNRY VSNELSNAKY
NAVTFVPTLL YEQFKFFYNL YFLVVALSQA VPALRIGYLS SYIVPLAFVL TVTMAKEAID
DIQRRRRDRE SNNELYHVIT RNRSIPSKDL KVGDLIKVHK GDRIPADLVL LQSSEPSGES
FIKTDQLDGE TDWKLRVACP LTQNLSENDL INRISITASA PEKSIHKFLG KVTYKDSTSN
PLSVDNTLWA NTVLASSGFC IACVVYTGRD TRQAMNTTTA KVKTGLLELE INSISKILCA
CVFALSILLV AFAGFHNDDW YIDILRYLIL FSTIIPVSLR VNLDLAKSVY AHQIEHDKTI
PETIVRTSTI PEDLGRIEYL LSDKTGTLTQ NDMQLKKIHL GTVSYTSETL DIVSDYVQSL
VSSKNDSLNN SKVALSTTRK DMSFRVRDMI LTLAICHNVT PTFEDDELTY QAASPDEIAI
VKFTESVGLS LFKRDRHSIS LLHEHSGKTL NYEILQVFPF NSDSKRMGII VRDEQLDEYW
FMQKGADTVM SKIVESNDWL EEETGNMARE GLRTLVIGRK KLNKKIYEQF QKEYNDASLS
MLNRDQQMSQ VITKYLEHDL ELLGLTGVED KLQKDVKSSI ELLRNAGIKI WMLTGDKVET
ARCVSISAKL ISRGQYVHTI TKVTRPEGAF NQLEYLKINR NACLLIDGES LGMFLKHYEQ
EFFDVVVHLP TVIACRCTPQ QKADVALVIR KMTGKRVCCI GDGGNDVSMI QCADVGVGIV
GKEGKQASLA ADFSITQFCH LTELLLWHGR NSYKRSAKLA QFVMHRGLII AICQAVYSIC
SLFEPIALYQ GWLMVGYATC YTMAPVFSLT LDHDIEESLT KIYPELYKEL TEGKSLSYKT
FFVWVLLSLF QGSVIQLFSQ AFTSLLDTDF TRMVAISFTA LVVNELIMVA LEIYTWNKTM
LVTEIATLLF YIVSVPFLGD YFDLGYMTTV NYYAGLLVIL LISIFPVWTA KAIYRRLHPP
SYAKVQEFAT P
