MEXB_PSEAE
ID MEXB_PSEAE Reviewed; 1046 AA.
AC P52002; Q9S505;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Multidrug resistance protein MexB;
DE AltName: Full=Multidrug-efflux transporter MexB;
GN Name=mexB; OrderedLocusNames=PA0426;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAO6609;
RX PubMed=7968531; DOI=10.1111/j.1365-2958.1993.tb00925.x;
RA Poole K., Heinrichs D.E., Neshat S.;
RT "Cloning and sequence analysis of an EnvCD homologue in Pseudomonas
RT aeruginosa: regulation by iron and possible involvement in the secretion of
RT the siderophore pyoverdine.";
RL Mol. Microbiol. 10:529-544(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-128.
RC STRAIN=PA14;
RX PubMed=9989496; DOI=10.1016/s0092-8674(00)80958-7;
RA Mahajan-Miklos S., Tan M.-W., Rahme L.G., Ausubel F.M.;
RT "Molecular mechanisms of bacterial virulence elucidated using a Pseudomonas
RT aeruginosa-Caenorhabditis elegans pathogenesis model.";
RL Cell 96:47-56(1999).
RN [4]
RP PROTEIN SEQUENCE OF 171-185; 240-252; 308-322 AND 818-848, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=15253424; DOI=10.1021/pr034074w;
RA Blonder J., Goshe M.B., Xiao W., Camp D.G. II, Wingerd M., Davis R.W.,
RA Smith R.D.;
RT "Global analysis of the membrane subproteome of Pseudomonas aeruginosa
RT using liquid chromatography-tandem mass spectrometry.";
RL J. Proteome Res. 3:434-444(2004).
RN [5]
RP FUNCTION AS AN ANTIBIOTIC EFFLUX PUMP.
RC STRAIN=PAO6609;
RX PubMed=8226684; DOI=10.1128/jb.175.22.7363-7372.1993;
RA Poole K., Krebes K., McNally C., Neshat S.;
RT "Multiple antibiotic resistance in Pseudomonas aeruginosa: evidence for
RT involvement of an efflux operon.";
RL J. Bacteriol. 175:7363-7372(1993).
RN [6]
RP FUNCTION IN ANTIBIOTIC EFFLUX AND ENERGETIC REQUIREMENTS.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8540696; DOI=10.1128/aac.39.9.1948;
RA Li X.-Z., Nikaido H., Poole K.;
RT "Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa.";
RL Antimicrob. Agents Chemother. 39:1948-1953(1995).
RN [7]
RP FUNCTION IN SOLVENT EFFLUX.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9603892; DOI=10.1128/jb.180.11.2987-2991.1998;
RA Li X.-Z., Zhang L., Poole K.;
RT "Role of the multidrug efflux systems of Pseudomonas aeruginosa in organic
RT solvent tolerance.";
RL J. Bacteriol. 180:2987-2991(1998).
RN [8]
RP TOPOLOGY.
RC STRAIN=PAO4290;
RX PubMed=10187844; DOI=10.1074/jbc.274.15.10517;
RA Guan L., Ehrmann M., Yoneyama H., Nakae T.;
RT "Membrane topology of the xenobiotic-exporting subunit, MexB, of the
RT MexA,B-OprM extrusion pump in Pseudomonas aeruginosa.";
RL J. Biol. Chem. 274:10517-10522(1999).
CC -!- FUNCTION: The inner membrane transporter component of the MexAB-OprM
CC efflux system that confers multidrug resistance. Also functions as the
CC major efflux pump for n-hexane and p-xylene efflux. Over-expression of
CC the pump increases antibiotic and solvent efflux capacities. Implicated
CC in the secretion of the siderophore pyoverdine.
CC -!- FUNCTION: The ability to export antibiotics and solvents is
CC dramatically decreased in the presence of the proton conductor carbonyl
CC cyanide m-chlorophenylhydrazone (CCCP), showing that an energized inner
CC membrane is required for efflux. It is thought that the MexB subunit is
CC a proton antiporter.
CC -!- SUBUNIT: Component of the MexAB-OprM multidrug efflux complex composed
CC of an unknown number of MexA subunits, MexB and an OprM homotrimer. The
CC MexA subunits are thought to form a barrel between the MexB inner
CC membrane transporter and the trimeric OprM outer membrane channel
CC protein which allows substrates to pass directly from the cytoplasm to
CC the external mileu. How the MexA subunits interact with OprM and MexB,
CC and how the OprM channel is opened is unknown.
CC -!- INTERACTION:
CC P52002; P0A9Q1: arcA; Xeno; NbExp=2; IntAct=EBI-6400435, EBI-1119939;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: By growth under severe iron limitation.
CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC (TC 2.A.6) family. {ECO:0000305}.
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DR EMBL; L11616; AAA74437.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03815.1; -; Genomic_DNA.
DR EMBL; AF092566; AAD45628.1; -; Genomic_DNA.
DR PIR; E83593; E83593.
DR PIR; S39630; S39630.
DR RefSeq; NP_249117.1; NC_002516.2.
DR RefSeq; WP_003107312.1; NZ_QZGE01000016.1.
DR PDB; 2V50; X-ray; 3.00 A; A/B/C/D/E/F=1-1046.
DR PDB; 3W9I; X-ray; 2.71 A; A/B/C/D/E/F=1-1046.
DR PDB; 3W9J; X-ray; 3.15 A; A/B/C/D/E/F=1-1046.
DR PDB; 6IIA; X-ray; 2.91 A; A/B/C/D/E/F=1-1046.
DR PDB; 6IOK; EM; 3.64 A; E/F/G=1-1046.
DR PDB; 6IOL; EM; 3.76 A; E/F/G=1-1046.
DR PDB; 6T7S; EM; 4.50 A; J/K/L=1-1046.
DR PDB; 6TA5; EM; 3.20 A; J/K/L=1-1046.
DR PDB; 6TA6; EM; 3.20 A; J/K/L=1-1046.
DR PDBsum; 2V50; -.
DR PDBsum; 3W9I; -.
DR PDBsum; 3W9J; -.
DR PDBsum; 6IIA; -.
DR PDBsum; 6IOK; -.
DR PDBsum; 6IOL; -.
DR PDBsum; 6T7S; -.
DR PDBsum; 6TA5; -.
DR PDBsum; 6TA6; -.
DR AlphaFoldDB; P52002; -.
DR SMR; P52002; -.
DR DIP; DIP-60510N; -.
DR IntAct; P52002; 2.
DR STRING; 287.DR97_3394; -.
DR ChEMBL; CHEMBL4523990; -.
DR DrugBank; DB14879; Cefiderocol.
DR TCDB; 2.A.6.2.6; the resistance-nodulation-cell division (rnd) superfamily.
DR PaxDb; P52002; -.
DR PRIDE; P52002; -.
DR EnsemblBacteria; AAG03815; AAG03815; PA0426.
DR GeneID; 877852; -.
DR KEGG; pae:PA0426; -.
DR PATRIC; fig|208964.12.peg.448; -.
DR PseudoCAP; PA0426; -.
DR HOGENOM; CLU_002755_1_1_6; -.
DR InParanoid; P52002; -.
DR OMA; LMYMSSS; -.
DR PhylomeDB; P52002; -.
DR BioCyc; PAER208964:G1FZ6-430-MON; -.
DR EvolutionaryTrace; P52002; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2090.10; -; 2.
DR InterPro; IPR027463; AcrB_DN_DC_subdom.
DR InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR004764; HAE1.
DR PANTHER; PTHR32063; PTHR32063; 1.
DR Pfam; PF00873; ACR_tran; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF82714; SSF82714; 2.
DR TIGRFAMs; TIGR00915; 2A0602; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1046
FT /note="Multidrug resistance protein MexB"
FT /id="PRO_0000161844"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10187844"
FT TRANSMEM 10..28
FT /note="Helical"
FT TOPO_DOM 29..339
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10187844"
FT TRANSMEM 340..359
FT /note="Helical"
FT TOPO_DOM 360..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10187844"
FT TRANSMEM 366..385
FT /note="Helical"
FT TOPO_DOM 386..391
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10187844"
FT TRANSMEM 392..413
FT /note="Helical"
FT TOPO_DOM 414..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10187844"
FT TRANSMEM 442..460
FT /note="Helical"
FT TOPO_DOM 461..473
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10187844"
FT TRANSMEM 474..496
FT /note="Helical"
FT TOPO_DOM 497..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10187844"
FT TRANSMEM 539..557
FT /note="Helical"
FT TOPO_DOM 558..871
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10187844"
FT TRANSMEM 872..891
FT /note="Helical"
FT TOPO_DOM 892..897
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10187844"
FT TRANSMEM 898..917
FT /note="Helical"
FT TOPO_DOM 918..923
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10187844"
FT TRANSMEM 924..945
FT /note="Helical"
FT TOPO_DOM 946..972
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10187844"
FT TRANSMEM 973..991
FT /note="Helical"
FT TOPO_DOM 992..1004
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10187844"
FT TRANSMEM 1005..1027
FT /note="Helical"
FT TOPO_DOM 1028..1046
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10187844"
FT CONFLICT 29
FT /note="S -> N (in Ref. 3; AAD45628)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="I -> T (in Ref. 1; AAA74437)"
FT /evidence="ECO:0000305"
FT HELIX 2..7
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 9..27
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 128..143
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6TA5"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:6TA5"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:3W9I"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:2V50"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6IIA"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 284..294
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 299..311
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 330..359
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 362..386
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 392..405
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 407..421
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 427..436
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 439..450
FT /evidence="ECO:0007829|PDB:3W9I"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 461..496
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:6IIA"
FT HELIX 513..537
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 539..555
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 571..577
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 584..600
FT /evidence="ECO:0007829|PDB:3W9I"
FT TURN 601..605
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 606..614
FT /evidence="ECO:0007829|PDB:3W9I"
FT TURN 621..623
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 624..631
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 634..636
FT /evidence="ECO:0007829|PDB:3W9I"
FT TURN 639..641
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 645..648
FT /evidence="ECO:0007829|PDB:3W9I"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 652..656
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 659..666
FT /evidence="ECO:0007829|PDB:2V50"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:3W9J"
FT STRAND 676..679
FT /evidence="ECO:0007829|PDB:3W9J"
FT STRAND 682..685
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:2V50"
FT HELIX 692..705
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 716..719
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 726..730
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 732..738
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 742..753
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 756..763
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 766..774
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 776..778
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 779..781
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 782..786
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 789..791
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 793..795
FT /evidence="ECO:0007829|PDB:2V50"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 800..802
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 803..807
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 813..815
FT /evidence="ECO:0007829|PDB:2V50"
FT STRAND 816..827
FT /evidence="ECO:0007829|PDB:3W9I"
FT TURN 836..838
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 839..846
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 847..849
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 860..867
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 868..870
FT /evidence="ECO:0007829|PDB:6TA6"
FT HELIX 875..890
FT /evidence="ECO:0007829|PDB:3W9I"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 898..901
FT /evidence="ECO:0007829|PDB:3W9I"
FT TURN 902..904
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 905..916
FT /evidence="ECO:0007829|PDB:3W9I"
FT TURN 917..919
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 924..939
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 942..951
FT /evidence="ECO:0007829|PDB:3W9I"
FT TURN 953..955
FT /evidence="ECO:0007829|PDB:6TA5"
FT HELIX 958..988
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 995..1023
FT /evidence="ECO:0007829|PDB:3W9I"
FT HELIX 1025..1028
FT /evidence="ECO:0007829|PDB:3W9I"
SQ SEQUENCE 1046 AA; 112791 MW; FF91855338868ED2 CRC64;
MSKFFIDRPI FAWVIALVIM LAGGLSILSL PVNQYPAIAP PAIAVQVSYP GASAETVQDT
VVQVIEQQMN GIDNLRYISS ESNSDGSMTI TVTFEQGTDP DIAQVQVQNK LQLATPLLPQ
EVQRQGIRVT KAVKNFLMVV GVVSTDGSMT KEDLSNYIVS NIQDPLSRTK GVGDFQVFGS
QYSMRIWLDP AKLNSYQLTP GDVSSAIQAQ NVQISSGQLG GLPAVKGQQL NATIIGKTRL
QTAEQFENIL LKVNPDGSQV RLKDVADVGL GGQDYSINAQ FNGSPASGIA IKLATGANAL
DTAKAIRQTI ANLEPFMPQG MKVVYPYDTT PVVSASIHEV VKTLGEAILL VFLVMYLFLQ
NFRATLIPTI AVPVVLLGTF GVLAAFGFSI NTLTMFGMVL AIGLLVDDAI VVVENVERVM
AEEGLSPREA ARKSMGQIQG ALVGIAMVLS AVFLPMAFFG GSTGVIYRQF SITIVSAMAL
SVIVALILTP ALCATMLKPI EKGDHGEHKG GFFGWFNRMF LSTTHGYERG VASILKHRAP
YLLIYVVIVA GMIWMFTRIP TAFLPDEDQG VLFAQVQTPP GSSAERTQVV VDSMREYLLE
KESSSVSSVF TVTGFNFAGR GQSSGMAFIM LKPWEERPGG ENSVFELAKR AQMHFFSFKD
AMVFAFAPPS VLELGNATGF DLFLQDQAGV GHEVLLQARN KFLMLAAQNP ALQRVRPNGM
SDEPQYKLEI DDEKASALGV SLADINSTVS IAWGSSYVND FIDRGRVKRV YLQGRPDARM
NPDDLSKWYV RNDKGEMVPF NAFATGKWEY GSPKLERYNG VPAMEILGEP APGLSSGDAM
AAVEEIVKQL PKGVGYSWTG LSYEERLSGS QAPALYALSL LVVFLCLAAL YESWSIPFSV
MLVVPLGVIG ALLATSMRGL SNDVFFQVGL LTTIGLSAKN AILIVEFAKE LHEQGKGIVE
AAIEACRMRL RPIVMTSLAF ILGVVPLAIS TGAGSGSQHA IGTGVIGGMV TATVLAIFWV
PLFYVAVSTL FKDEASKQQA SVEKGQ
