SRO7_YEAST
ID SRO7_YEAST Reviewed; 1033 AA.
AC Q12038; D6W442;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Lethal(2) giant larvae protein homolog SRO7;
DE AltName: Full=Polarity protein SRO7;
DE AltName: Full=Sodium protection protein 1;
DE AltName: Full=Suppressor of RHO3 protein 7;
GN Name=SRO7; Synonyms=SNI1, SOP1; OrderedLocusNames=YPR032W;
GN ORFNames=YP9367.12;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 CHARACTERIZATION.
RX PubMed=9691031; DOI=10.1093/genetics/149.4.1717;
RA Kagami M., Toh-e A., Matsui Y.;
RT "Sro7p, a Saccharomyces cerevisiae counterpart of the tumor suppressor
RT l(2)gl protein, is related to myosins in function.";
RL Genetics 149:1717-1727(1998).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9837945; DOI=10.1074/jbc.273.50.33610;
RA Larsson K., Bohl F., Sjostrom I., Akhtar N., Strand D., Mechler B.M.,
RA Grabowski R., Adler L.;
RT "The Saccharomyces cerevisiae SOP1 and SOP2 genes, which act in cation
RT homeostasis, can be functionally substituted by the Drosophila
RT lethal(2)giant larvae tumor suppressor gene.";
RL J. Biol. Chem. 273:33610-33618(1998).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SEC9.
RX PubMed=10402465; DOI=10.1083/jcb.146.1.125;
RA Lehman K., Rossi G., Adamo J.E., Brennwald P.;
RT "Yeast homologues of tomosyn and lethal giant larvae function in exocytosis
RT and are associated with the plasma membrane SNARE, Sec9.";
RL J. Cell Biol. 146:125-140(1999).
RN [6]
RP FUNCTION.
RX PubMed=14676322; DOI=10.1073/pnas.2435976100;
RA Warringer J., Ericson E., Fernandez L., Nerman O., Blomberg A.;
RT "High-resolution yeast phenomics resolves different physiological features
RT in the saline response.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15724-15729(2003).
RN [7]
RP INTERACTION WITH MYO2 AND SEC9.
RX PubMed=15964280; DOI=10.1016/j.cub.2005.05.046;
RA Gangar A., Rossi G., Andreeva A., Hales R., Brennwald P.;
RT "Structurally conserved interaction of Lgl family with SNAREs is critical
RT to their cellular function.";
RL Curr. Biol. 15:1136-1142(2005).
RN [8]
RP FUNCTION, AND INTERACTION WITH SEC4 AND SEC9.
RX PubMed=16390997; DOI=10.1083/jcb.200510016;
RA Grosshans B.L., Andreeva A., Gangar A., Niessen S., Yates J.R. III,
RA Brennwald P., Novick P.;
RT "The yeast lgl family member Sro7p is an effector of the secretory Rab
RT GTPase Sec4p.";
RL J. Cell Biol. 172:55-66(2006).
RN [9]
RP FUNCTION.
RX PubMed=17005914; DOI=10.1091/mbc.e05-08-0798;
RA Wadskog I., Forsmark A., Rossi G., Konopka C., Oyen M., Goksor M.,
RA Ronne H., Brennwald P., Adler L.;
RT "The yeast tumor suppressor homologue Sro7p is required for targeting of
RT the sodium pumping ATPase to the cell surface.";
RL Mol. Biol. Cell 17:4988-5003(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591 AND SER-602, 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 [11]
RP FUNCTION, AND INTERACTION WITH MYO2.
RX PubMed=21248204; DOI=10.1091/mbc.e10-07-0570;
RA Rossi G., Brennwald P.;
RT "Yeast homologues of lethal giant larvae and type V myosin cooperate in the
RT regulation of Rab-dependent vesicle clustering and polarized exocytosis.";
RL Mol. Biol. Cell 22:842-857(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 61-962, FUNCTION, WD REPEATS, AND
RP INTERACTION WITH SEC9.
RX PubMed=17392788; DOI=10.1038/nature05635;
RA Hattendorf D.A., Andreeva A., Gangar A., Brennwald P.J., Weis W.I.;
RT "Structure of the yeast polarity protein Sro7 reveals a SNARE regulatory
RT mechanism.";
RL Nature 446:567-571(2007).
CC -!- FUNCTION: Acts as an allosteric regulator of polarized exocytosis by
CC promoting the targeted fusion of vesicles with the plasma membrane.
CC Coordinates the spatial and temporal nature of both Rab-dependent
CC tethering and SNARE-dependent membrane fusion of exocytic vesicles with
CC the plasma membrane. Required for targeting of the sodium pumping
CC ATPase ENA1 to the Cell Surface, thus being involved in maintenance of
CC ion homeostasis in cells exposed to NaCl stress. May be involved in the
CC targeting of the myosin proteins to their intrinsic pathways. Multicopy
CC suppressor of RHO3. May also participate in the maintenance of cell
CC polarity and bud growth. {ECO:0000269|PubMed:10402465,
CC ECO:0000269|PubMed:14676322, ECO:0000269|PubMed:16390997,
CC ECO:0000269|PubMed:17005914, ECO:0000269|PubMed:17392788,
CC ECO:0000269|PubMed:21248204, ECO:0000269|PubMed:9837945}.
CC -!- SUBUNIT: Interacts with MYO2 and SEC9. {ECO:0000269|PubMed:10402465,
CC ECO:0000269|PubMed:15964280, ECO:0000269|PubMed:16390997,
CC ECO:0000269|PubMed:17392788, ECO:0000269|PubMed:21248204}.
CC -!- INTERACTION:
CC Q12038; P40020: FIR1; NbExp=2; IntAct=EBI-17573, EBI-13431;
CC Q12038; P40357: SEC9; NbExp=10; IntAct=EBI-17573, EBI-16904;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10402465,
CC ECO:0000269|PubMed:9837945}. Cell membrane
CC {ECO:0000269|PubMed:10402465}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10402465}; Cytoplasmic side
CC {ECO:0000269|PubMed:10402465}.
CC -!- SIMILARITY: Belongs to the WD repeat L(2)GL family. {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; Z71255; CAA95028.1; -; Genomic_DNA.
DR EMBL; Z49274; CAA89286.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11458.1; -; Genomic_DNA.
DR PIR; S54506; S54506.
DR RefSeq; NP_015357.1; NM_001184129.1.
DR PDB; 2OAJ; X-ray; 2.40 A; A=61-962.
DR PDBsum; 2OAJ; -.
DR AlphaFoldDB; Q12038; -.
DR SMR; Q12038; -.
DR BioGRID; 36210; 652.
DR DIP; DIP-2581N; -.
DR IntAct; Q12038; 8.
DR MINT; Q12038; -.
DR STRING; 4932.YPR032W; -.
DR iPTMnet; Q12038; -.
DR MaxQB; Q12038; -.
DR PaxDb; Q12038; -.
DR PRIDE; Q12038; -.
DR EnsemblFungi; YPR032W_mRNA; YPR032W; YPR032W.
DR GeneID; 856144; -.
DR KEGG; sce:YPR032W; -.
DR SGD; S000006236; SRO7.
DR VEuPathDB; FungiDB:YPR032W; -.
DR eggNOG; KOG1983; Eukaryota.
DR GeneTree; ENSGT00950000182906; -.
DR HOGENOM; CLU_006030_0_0_1; -.
DR InParanoid; Q12038; -.
DR OMA; YVFGQRR; -.
DR BioCyc; YEAST:G3O-34191-MON; -.
DR EvolutionaryTrace; Q12038; -.
DR PRO; PR:Q12038; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12038; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0045159; F:myosin II binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IDA:SGD.
DR GO; GO:0000149; F:SNARE binding; IPI:SGD.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0030010; P:establishment of cell polarity; IPI:SGD.
DR GO; GO:0006887; P:exocytosis; IMP:SGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:SGD.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR013905; Lgl_C_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08596; Lgl_C; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Exocytosis; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1033
FT /note="Lethal(2) giant larvae protein homolog SRO7"
FT /id="PRO_0000072008"
FT REPEAT 81..114
FT /note="WD 1"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REPEAT 121..156
FT /note="WD 2"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REPEAT 161..197
FT /note="WD 3"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REPEAT 216..249
FT /note="WD 4"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REPEAT 274..309
FT /note="WD 5"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REPEAT 333..397
FT /note="WD 6"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REPEAT 405..440
FT /note="WD 7"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REPEAT 464..538
FT /note="WD 8"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REPEAT 552..631
FT /note="WD 9"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REPEAT 638..673
FT /note="WD 10"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REPEAT 685..736
FT /note="WD 11"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REPEAT 745..799
FT /note="WD 12"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REPEAT 804..851
FT /note="WD 13"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REPEAT 865..888
FT /note="WD 14"
FT /evidence="ECO:0000269|PubMed:17392788"
FT REGION 16..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 381..389
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 455..460
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 464..473
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 474..482
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 505..514
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 517..525
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 528..532
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 535..538
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 539..542
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 551..557
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 558..561
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 562..567
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 572..579
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 603..605
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 622..631
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 637..643
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 647..653
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 656..662
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 663..666
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 667..673
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 674..676
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 685..694
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 698..709
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 712..721
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 727..736
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 745..750
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 751..753
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 761..765
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 766..769
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 775..780
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 782..788
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 795..799
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 804..815
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 817..819
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 821..831
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 834..840
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 841..843
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 846..851
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 858..861
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 872..875
FT /evidence="ECO:0007829|PDB:2OAJ"
FT STRAND 877..888
FT /evidence="ECO:0007829|PDB:2OAJ"
FT TURN 915..917
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 927..935
FT /evidence="ECO:0007829|PDB:2OAJ"
FT HELIX 945..949
FT /evidence="ECO:0007829|PDB:2OAJ"
SQ SEQUENCE 1033 AA; 114513 MW; FFB0901883009815 CRC64;
MFGSKRLKNV KEAFKSLKGQ NSETPIENSK ASFKSKNSKT STISKDAKSS SSLKIPISSN
NKNKIFSLAE TNKYGMSSKP IAAAFDFTQN LLAIATVTGE VHIYGQQQVE VVIKLEDRSA
IKEMRFVKGI YLVVINAKDT VYVLSLYSQK VLTTVFVPGK ITSIDTDASL DWMLIGLQNG
SMIVYDIDRD QLSSFKLDNL QKSSFFPAAR LSPIVSIQWN PRDIGTVLIS YEYVTLTYSL
VENEIKQSFI YELPPFAPGG DFSEKTNEKR TPKVIQSLYH PNSLHIITIH EDNSLVFWDA
NSGHMIMART VFETEINVPQ PDYIRDSSTN AAKISKVYWM CENNPEYTSL LISHKSISRG
DNQSLTMIDL GYTPRYSITS YEGMKNYYAN PKQMKIFPLP TNVPIVNILP IPRQSPYFAG
CHNPGLILLI LGNGEIETML YPSGIFTDKA SLFPQNLSWL RPLATTSMAA SVPNKLWLGA
LSAAQNKDYL LKGGVRTKRQ KLPAEYGTAF ITGHSNGSVR IYDASHGDIQ DNASFEVNLS
RTLNKAKELA VDKISFAAET LELAVSIETG DVVLFKYEVN QFYSVENRPE SGDLEMNFRR
FSLNNTNGVL VDVRDRAPTG VRQGFMPSTA VHANKGKTSA INNSNIGFVG IAYAAGSLML
IDRRGPAIIY MENIREISGA QSACVTCIEF VIMEYGDDGY SSILMVCGTD MGEVITYKIL
PASGGKFDVQ LMDITNVTSK GPIHKIDAFS KETKSSCLAT IPKMQNLSKG LCIPGIVLIT
GFDDIRLITL GKSKSTHKGF KYPLAATGLS YISTVEKNND RKNLTVIITL EINGHLRVFT
IPDFKEQMSE HIPFPIAAKY ITESSVLRNG DIAIRVSEFQ ASLFSTVKEQ DTLAPVSDTL
YINGIRIPYR PQVNSLQWAR GTVYCTPAQL NELLGGVNRP ASKYKESIIA EGSFSERSSD
DNNANHPEHQ YTKPTRKGRN SSYGVLRNVS RAVETRWDAV EDRFNDYATA MGETMNEAVE
QTGKDVMKGA LGF
