MEP2_YEAST
ID MEP2_YEAST Reviewed; 499 AA.
AC P41948; D6W140;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Ammonium transporter MEP2 {ECO:0000303|PubMed:9234685};
GN Name=MEP2 {ECO:0000303|PubMed:9234685}; Synonyms=AMT2;
GN OrderedLocusNames=YNL142W; ORFNames=N1207, N1820;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Sigma 1278B;
RX PubMed=9234685; DOI=10.1128/mcb.17.8.4282;
RA Marini A.-M., Soussi-Boudekou S., Vissers S., Andre B.;
RT "A family of ammonium transporters in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 17:4282-4293(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8619318; DOI=10.1002/yea.320111210;
RA Mallet L., Bussereau F., Jacquet M.;
RT "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT deaminase gene and 14 new open reading frames.";
RL Yeast 11:1195-1209(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Sigma 1278B;
RX PubMed=9482721; DOI=10.1093/emboj/17.5.1236;
RA Lorenz M.C., Heitman J.;
RT "The MEP2 ammonium permease regulates pseudohyphal differentiation in
RT Saccharomyces cerevisiae.";
RL EMBO J. 17:1236-1247(1998).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF ASN-4; ASN-252;
RP ASN-368 AND ASN-483, AND GLYCOSYLATION AT ASN-4.
RC STRAIN=Sigma 1278B;
RX PubMed=11069679; DOI=10.1046/j.1365-2958.2000.02151.x;
RA Marini A.-M., Andre B.;
RT "In vivo N-glycosylation of the mep2 high-affinity ammonium transporter of
RT Saccharomyces cerevisiae reveals an extracytosolic N-terminus.";
RL Mol. Microbiol. 38:552-564(2000).
RN [7]
RP FUNCTION.
RX PubMed=11486013; DOI=10.1128/mcb.21.17.5733-5741.2001;
RA Soupene E., Ramirez R.M., Kustu S.;
RT "Evidence that fungal MEP proteins mediate diffusion of the uncharged
RT species NH(3) across the cytoplasmic membrane.";
RL Mol. Cell. Biol. 21:5733-5741(2001).
RN [8]
RP FUNCTION, MUTAGENESIS OF ASP-186, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16477434; DOI=10.1007/s00294-006-0062-5;
RA Marini A.-M., Boeckstaens M., Benjelloun F., Cherif-Zahar B., Andre B.;
RT "Structural involvement in substrate recognition of an essential aspartate
RT residue conserved in Mep/Amt and Rh-type ammonium transporters.";
RL Curr. Genet. 49:364-374(2006).
RN [9]
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-186; HIS-194 AND
RP HIS-348.
RX PubMed=18434596; DOI=10.1091/mbc.e08-01-0033;
RA Rutherford J.C., Chua G., Hughes T., Cardenas M.E., Heitman J.;
RT "A Mep2-dependent transcriptional profile links permease function to gene
RT expression during pseudohyphal growth in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 19:3028-3039(2008).
RN [11]
RP FUNCTION, PHOSPHORYLATION AT SER-457, AND SUBCELLULAR LOCATION.
RX PubMed=24476960; DOI=10.1038/ncomms4101;
RA Boeckstaens M., Llinares E., Van Vooren P., Marini A.M.;
RT "The TORC1 effector kinase Npr1 fine tunes the inherent activity of the
RT Mep2 ammonium transport protein.";
RL Nat. Commun. 5:3101-3101(2014).
RN [12]
RP FUNCTION, MUTAGENESIS OF HIS-194; HIS-199; GLY-349 AND SER-457, AND DOMAIN.
RX PubMed=32069286; DOI=10.1371/journal.pgen.1008634;
RA Brito A.S., Neuhaeuser B., Wintjens R., Marini A.M., Boeckstaens M.;
RT "Yeast filamentation signaling is connected to a specific substrate
RT translocation mechanism of the Mep2 transceptor.";
RL PLoS Genet. 16:e1008634-e1008634(2020).
RN [13] {ECO:0007744|PDB:5AEX}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), SUBCELLULAR LOCATION, FUNCTION, AND
RP PHOSPHORYLATION AT SER-457.
RX PubMed=27088325; DOI=10.1038/ncomms11337;
RA van den Berg B., Chembath A., Jefferies D., Basle A., Khalid S.,
RA Rutherford J.C.;
RT "Structural basis for Mep2 ammonium transceptor activation by
RT phosphorylation.";
RL Nat. Commun. 7:11337-11337(2016).
CC -!- FUNCTION: Transporter for ammonium (both charged and uncharged NH3 and
CC NH4) to use as a nitrogen source (PubMed:11069679, PubMed:11486013,
CC PubMed:9234685, PubMed:9482721, PubMed:16477434, PubMed:18434596,
CC PubMed:24476960, PubMed:27088325). The affinity of MEP2 is about twenty
CC times higher than that of MEP1 (PubMed:9482721). MEP3 has the lowest
CC affinity (PubMed:9482721). Under ammonium limitation acts as an
CC ammonium sensor, generating a signal that leads to pseudohyphal
CC (filamentous) growth (PubMed:9482721, PubMed:11069679, PubMed:16477434,
CC PubMed:18434596, PubMed:32069286). {ECO:0000269|PubMed:11069679,
CC ECO:0000269|PubMed:11486013, ECO:0000269|PubMed:16477434,
CC ECO:0000269|PubMed:18434596, ECO:0000269|PubMed:24476960,
CC ECO:0000269|PubMed:27088325, ECO:0000269|PubMed:32069286,
CC ECO:0000269|PubMed:9234685, ECO:0000269|PubMed:9482721}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.34 mM for methylammonium transport
CC {ECO:0000269|PubMed:16477434};
CC Vmax=18.8 nmol/min/mg enzyme for methylammonium transport
CC {ECO:0000269|PubMed:16477434};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11069679,
CC ECO:0000269|PubMed:16477434, ECO:0000269|PubMed:18434596,
CC ECO:0000269|PubMed:24476960, ECO:0000269|PubMed:27088325}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:27088325}.
CC -!- DOMAIN: Within the cytoplasmic CTD, an enhancer domain, limited to
CC residues 428-441, upregulates substrate translocation via the MEP2
CC hydrophobic core, while an autoinhibitory domain, comprised within the
CC 450-485 region and including the NPR1-target serine Ser-457,
CC counteracts the action of the enhancer domain (PubMed:32069286). In
CC between, a linker domain, limited to residues 442-449, appears required
CC for optimal activity when the kinase is present but dispensable when
CC the kinase integrity is altered (PubMed:32069286).
CC {ECO:0000269|PubMed:32069286}.
CC -!- PTM: Phosphorylated at Ser-457 by the TORC1 effector kinase NPR1 under
CC nitrogen-limiting conditions which causes a conformational change in
CC the C-terminal region (CTR) to form an open active conformation
CC (PubMed:24476960, PubMed:27088325). Supplementation of nitrogen source
CC leads to inactivation and instant Ser-457 dephosphorylation via plasma
CC membrane PSR1 and PSR2 redundant phosphatases (PubMed:24476960).
CC {ECO:0000269|PubMed:24476960, ECO:0000269|PubMed:27088325}.
CC -!- PTM: The residue Asn-4 of the protein's N-terminal tail is the only
CC site that is glycosylated. {ECO:0000269|PubMed:11069679}.
CC -!- DISRUPTION PHENOTYPE: Impairs filamentation induction.
CC {ECO:0000269|PubMed:9482721}.
CC -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC family. {ECO:0000305}.
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DR EMBL; X83608; CAA58587.1; -; Genomic_DNA.
DR EMBL; Z46843; CAA86884.1; -; Genomic_DNA.
DR EMBL; Z71418; CAA96025.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10406.1; -; Genomic_DNA.
DR PIR; S51089; S51089.
DR RefSeq; NP_014257.1; NM_001182980.1.
DR PDB; 5AEX; X-ray; 3.20 A; A/B/C/D/E/F/H/I/J=1-499.
DR PDBsum; 5AEX; -.
DR AlphaFoldDB; P41948; -.
DR SMR; P41948; -.
DR BioGRID; 35685; 104.
DR DIP; DIP-4340N; -.
DR IntAct; P41948; 2.
DR STRING; 4932.YNL142W; -.
DR BindingDB; P41948; -.
DR ChEMBL; CHEMBL1741183; -.
DR TCDB; 1.A.11.3.2; the ammonium transporter channel (amt) family.
DR iPTMnet; P41948; -.
DR PaxDb; P41948; -.
DR PRIDE; P41948; -.
DR EnsemblFungi; YNL142W_mRNA; YNL142W; YNL142W.
DR GeneID; 855580; -.
DR KEGG; sce:YNL142W; -.
DR SGD; S000005086; MEP2.
DR VEuPathDB; FungiDB:YNL142W; -.
DR eggNOG; KOG0682; Eukaryota.
DR GeneTree; ENSGT00530000064546; -.
DR HOGENOM; CLU_000445_33_0_1; -.
DR InParanoid; P41948; -.
DR OMA; IWLSIMS; -.
DR BioCyc; YEAST:G3O-33160-MON; -.
DR PRO; PR:P41948; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P41948; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:SGD.
DR GO; GO:0072488; P:ammonium transmembrane transport; IMP:SGD.
DR GO; GO:0019740; P:nitrogen utilization; IMP:SGD.
DR GO; GO:1900430; P:positive regulation of filamentous growth of a population of unicellular organisms; IMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR Gene3D; 1.10.3430.10; -; 1.
DR InterPro; IPR029020; Ammonium/urea_transptr.
DR InterPro; IPR001905; Ammonium_transpt.
DR InterPro; IPR018047; Ammonium_transpt_CS.
DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR PANTHER; PTHR43029; PTHR43029; 1.
DR Pfam; PF00909; Ammonium_transp; 1.
DR TIGRFAMs; TIGR00836; amt; 1.
DR PROSITE; PS01219; AMMONIUM_TRANSP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ammonia transport; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..499
FT /note="Ammonium transporter MEP2"
FT /id="PRO_0000139755"
FT TOPO_DOM 1..31
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:11069679"
FT TRANSMEM 32..52
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..312
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..338
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..393
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..499
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 428..441
FT /note="Enhancer domain"
FT /evidence="ECO:0000269|PubMed:32069286"
FT REGION 442..449
FT /note="Linker domain"
FT /evidence="ECO:0000269|PubMed:32069286"
FT REGION 450..485
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000269|PubMed:32069286"
FT REGION 455..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24476960,
FT ECO:0000269|PubMed:27088325, ECO:0007744|PDB:5AEX"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11069679"
FT MUTAGEN 4
FT /note="N->Q: Impairs glycosylation."
FT /evidence="ECO:0000269|PubMed:11069679"
FT MUTAGEN 186
FT /note="D->A,N: Impairs transport activity."
FT /evidence="ECO:0000269|PubMed:16477434,
FT ECO:0000269|PubMed:18434596"
FT MUTAGEN 186
FT /note="D->E: Decreases the affinity for the substrate."
FT /evidence="ECO:0000269|PubMed:16477434"
FT MUTAGEN 194
FT /note="H->A: Preserves transport activity while impairing
FT the filamentation capacity."
FT /evidence="ECO:0000269|PubMed:18434596"
FT MUTAGEN 194
FT /note="H->E: Leads to increased competence to acidify the
FT submembrane pH while losing the signaling capability."
FT /evidence="ECO:0000269|PubMed:32069286"
FT MUTAGEN 199
FT /note="H->Y: Circumvents the requirement of the CTD to
FT enhance substrate trans-location through the hydrophobic
FT core."
FT /evidence="ECO:0000269|PubMed:32069286"
FT MUTAGEN 252
FT /note="N->Q: Does not affect glycosylation."
FT /evidence="ECO:0000269|PubMed:11069679"
FT MUTAGEN 348
FT /note="H->A: Preserves transport activity while impairing
FT the filamentation capacity."
FT /evidence="ECO:0000269|PubMed:18434596"
FT MUTAGEN 349
FT /note="G->C: Circumvents the requirement of the CTD to
FT enhance substrate trans-location through the hydrophobic
FT core."
FT /evidence="ECO:0000269|PubMed:32069286"
FT MUTAGEN 368
FT /note="N->Q: Does not affect glycosylation."
FT /evidence="ECO:0000269|PubMed:11069679"
FT MUTAGEN 457
FT /note="S->D: Silences the autoinhibition of MEP2,
FT conferring transport activity even in the absence of the
FT NPR1 kinase."
FT /evidence="ECO:0000269|PubMed:32069286"
FT MUTAGEN 483
FT /note="N->Q: Does not affect glycosylation."
FT /evidence="ECO:0000269|PubMed:11069679"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 29..43
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:5AEX"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:5AEX"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 122..142
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:5AEX"
FT TURN 178..183
FT /evidence="ECO:0007829|PDB:5AEX"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 228..247
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:5AEX"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 255..282
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 291..302
FT /evidence="ECO:0007829|PDB:5AEX"
FT TURN 303..309
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 314..330
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 342..362
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 369..374
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 389..415
FT /evidence="ECO:0007829|PDB:5AEX"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:5AEX"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:5AEX"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:5AEX"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:5AEX"
SQ SEQUENCE 499 AA; 53401 MW; 9E81D08018B68D94 CRC64;
MSYNFTGTPT GEGTGGNSLT TDLNTQFDLA NMGWIGVASA GVWIMVPGIG LLYSGLSRKK
HALSLLWASM MASAVCIFQW FFWGYSLAFS HNTRGNGFIG TLEFFGFRNV LGAPSSVSSL
PDILFAVYQG MFAAVTGALM LGGACERARL FPMMVFLFLW MTIVYCPIAC WVWNAEGWLV
KLGSLDYAGG LCVHLTSGHG GLVYALILGK RNDPVTRKGM PKYKPHSVTS VVLGTVFLWF
GWMFFNGGSA GNATIRAWYS IMSTNLAAAC GGLTWMVIDY FRCGRKWTTV GLCSGIIAGL
VGITPAAGFV PIWSAVVIGV VTGAGCNLAV DLKSLLRIDD GLDCYSIHGV GGCIGSVLTG
IFAADYVNAT AGSYISPIDG GWINHHYKQV GYQLAGICAA LAWTVTVTSI LLLTMNAIPF
LKLRLSADEE ELGTDAAQIG EFTYEESTAY IPEPIRSKTS AQMPPPHENI DDKIVGNTDA
EKNSTPSDAS STKNTDHIV
