CADB_ECOLI
ID CADB_ECOLI Reviewed; 444 AA.
AC P0AAE8; P23891; Q2M6H1;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cadaverine/lysine antiporter {ECO:0000305};
GN Name=cadB {ECO:0000303|PubMed:1556085}; OrderedLocusNames=b4132, JW4093;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=JLS821;
RX PubMed=1370290; DOI=10.1128/jb.174.2.530-540.1992;
RA Watson N., Dunyak D.S., Rosey E.L., Slonczewski J.L., Olson E.R.;
RT "Identification of elements involved in transcriptional regulation of the
RT Escherichia coli cad operon by external pH.";
RL J. Bacteriol. 174:530-540(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1556085; DOI=10.1128/jb.174.8.2659-2669.1992;
RA Meng S.-Y., Bennett G.N.;
RT "Nucleotide sequence of the Escherichia coli cad operon: a system for
RT neutralization of low extracellular pH.";
RL J. Bacteriol. 174:2659-2669(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INDUCTION.
RX PubMed=14982633; DOI=10.1046/j.1365-2958.2003.03913.x;
RA Soksawatmaekhin W., Kuraishi A., Sakata K., Kashiwagi K., Igarashi K.;
RT "Excretion and uptake of cadaverine by CadB and its physiological functions
RT in Escherichia coli.";
RL Mol. Microbiol. 51:1401-1412(2004).
RN [7]
RP INDUCTION.
RX PubMed=16491024; DOI=10.1159/000090346;
RA Kuper C., Jung K.;
RT "CadC-mediated activation of the cadBA promoter in Escherichia coli.";
RL J. Mol. Microbiol. Biotechnol. 10:26-39(2005).
RN [8]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, AND
RP MUTAGENESIS OF CYS-12; TRP-41; TRP-43; TYR-55; TYR-57; TYR-73; GLU-76;
RP TYR-89; TYR-90; TYR-107; CYS-125; TYR-174; ASP-185; CYS-196; GLU-204;
RP TYR-235; TYR-246; CYS-282; ARG-299; ASP-303; TYR-310; TYR-366; TYR-368;
RP CYS-370; GLU-377; CYS-389; CYS-394; CYS-397; GLU-408 AND TYR-423.
RX PubMed=16877381; DOI=10.1074/jbc.m600754200;
RA Soksawatmaekhin W., Uemura T., Fukiwake N., Kashiwagi K., Igarashi K.;
RT "Identification of the cadaverine recognition site on the cadaverine-lysine
RT antiporter CadB.";
RL J. Biol. Chem. 281:29213-29220(2006).
RN [10]
RP TRANSCRIPTIONAL REGULATION BY LRP.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21441513; DOI=10.1128/jb.00815-10;
RA Ruiz J., Haneburger I., Jung K.;
RT "Identification of ArgP and Lrp as transcriptional regulators of lysP, the
RT gene encoding the specific lysine permease of Escherichia coli.";
RL J. Bacteriol. 193:2536-2548(2011).
RN [11]
RP REVIEW.
RX PubMed=21796432; DOI=10.1007/s00726-011-0989-9;
RA Tomitori H., Kashiwagi K., Igarashi K.;
RT "Structure and function of polyamine-amino acid antiporters CadB and PotE
RT in Escherichia coli.";
RL Amino Acids 42:733-740(2012).
RN [12]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=29138484; DOI=10.1038/s41467-017-02030-0;
RA Chakraborty S., Winardhi R.S., Morgan L.K., Yan J., Kenney L.J.;
RT "Non-canonical activation of OmpR drives acid and osmotic stress responses
RT in single bacterial cells.";
RL Nat. Commun. 8:1587-1587(2017).
CC -!- FUNCTION: Under acidic conditions, in the presence of lysine, functions
CC as a cadaverine:lysine antiporter that facilitates the excretion of
CC cadaverine and the uptake of lysine (PubMed:1556085, PubMed:14982633).
CC At neutral pH, also catalyzes the uptake of cadaverine via a proton
CC symport mechanism, however the physiological relevance of this uptake
CC activity is probably negligible because the expression of cadB is low
CC at neutral pH (PubMed:14982633). Cadaverine uptake activity is low at
CC acidic pH (PubMed:14982633). {ECO:0000269|PubMed:14982633,
CC ECO:0000269|PubMed:1556085}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cadaverine(in) + L-lysine(out) = cadaverine(out) + L-
CC lysine(in); Xref=Rhea:RHEA:28895, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:58384; Evidence={ECO:0000269|PubMed:14982633,
CC ECO:0000305|PubMed:1556085};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28896;
CC Evidence={ECO:0000269|PubMed:14982633, ECO:0000305|PubMed:1556085};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cadaverine(in) + H(+)(in) = cadaverine(out) + H(+)(out);
CC Xref=Rhea:RHEA:29711, ChEBI:CHEBI:15378, ChEBI:CHEBI:58384;
CC Evidence={ECO:0000269|PubMed:14982633};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29713;
CC Evidence={ECO:0000269|PubMed:14982633};
CC -!- ACTIVITY REGULATION: Uptake of cadaverine at neutral pH is greatly
CC inhibited by carbonyl cyanide m-chlorophenylhydrazone (CCCP), which
CC dissipates the proton motive force, valinomycin, which dissipates the
CC membrane potential, and nigericin, which dissipates the transmembrane
CC pH gradient (PubMed:14982633). Cadaverine uptake at neutral pH is also
CC inhibited by putrescine and lysine (PubMed:14982633). Cadaverine-lysine
CC antiporter activity is not inhibited by CCCP (PubMed:14982633).
CC {ECO:0000269|PubMed:14982633}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=303 uM for cadaverine (for export activity, at low pH)
CC {ECO:0000269|PubMed:14982633};
CC KM=390 uM for cadaverine (for export activity)
CC {ECO:0000269|PubMed:16877381};
CC KM=20.8 uM for cadaverine (for uptake activity, at neutral pH)
CC {ECO:0000269|PubMed:14982633, ECO:0000269|PubMed:16877381};
CC Vmax=0.313 nmol/min/mg enzyme (for cadaverine export activity, at low
CC pH) {ECO:0000269|PubMed:14982633};
CC Vmax=11.8 nmol/min/mg enzyme (for cadaverine uptake activity, at
CC neutral pH) {ECO:0000269|PubMed:14982633};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:16877381}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Part of the cadB-cadA operon, which is under the control of
CC the Pcad promoter (PubMed:1370290, PubMed:16491024). Expression is
CC regulated by CadC (PubMed:1370290, PubMed:16491024). Highly expressed
CC at acidic pH in the presence of lysine (PubMed:1370290,
CC PubMed:16491024, PubMed:14982633). The global regulator Lrp has also a
CC positive effect on the expression of the cadBA operon when cells are
CC exposed to moderate acidic stress in the presence of lysine
CC (PubMed:21441513). Repressed by H-NS under non-inducing conditions
CC (PubMed:16491024). Repressed at pH 5.6 by OmpR (PubMed:29138484).
CC {ECO:0000269|PubMed:1370290, ECO:0000269|PubMed:14982633,
CC ECO:0000269|PubMed:16491024, ECO:0000269|PubMed:21441513,
CC ECO:0000269|PubMed:29138484}.
CC -!- DOMAIN: Amino acid residues involved in both uptake and excretion, or
CC solely in excretion, are located in the cytoplasmic loops and the
CC cytoplasmic side of transmembrane segments, whereas residues involved
CC in uptake are located in the periplasmic loops and the transmembrane
CC segments. The SH-group of Cys-370 seems to be important for both uptake
CC and excretion and may be necessary for recognition of the NH(2)-group
CC of cadaverine. {ECO:0000269|PubMed:16877381}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows reduced amount of cadaverine in the
CC medium. {ECO:0000269|PubMed:1556085}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2)
CC family. {ECO:0000305}.
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DR EMBL; M67452; AAA23532.1; -; Genomic_DNA.
DR EMBL; M76411; AAA23535.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97032.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77093.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78135.1; -; Genomic_DNA.
DR PIR; A41842; A41842.
DR RefSeq; NP_418556.1; NC_000913.3.
DR RefSeq; WP_000092909.1; NZ_STEB01000014.1.
DR AlphaFoldDB; P0AAE8; -.
DR SMR; P0AAE8; -.
DR BioGRID; 4260780; 7.
DR DIP; DIP-48089N; -.
DR IntAct; P0AAE8; 2.
DR STRING; 511145.b4132; -.
DR TCDB; 2.A.3.2.2; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P0AAE8; -.
DR PRIDE; P0AAE8; -.
DR EnsemblBacteria; AAC77093; AAC77093; b4132.
DR EnsemblBacteria; BAE78135; BAE78135; BAE78135.
DR GeneID; 66671956; -.
DR GeneID; 948654; -.
DR KEGG; ecj:JW4093; -.
DR KEGG; eco:b4132; -.
DR PATRIC; fig|1411691.4.peg.2567; -.
DR EchoBASE; EB0130; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_1_0_6; -.
DR InParanoid; P0AAE8; -.
DR OMA; FAYDGWL; -.
DR PhylomeDB; P0AAE8; -.
DR BioCyc; EcoCyc:CADB-MON; -.
DR BioCyc; MetaCyc:CADB-MON; -.
DR PRO; PR:P0AAE8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0043872; F:lysine:cadaverine antiporter activity; IDA:EcoCyc.
DR GO; GO:0015295; F:solute:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0015839; P:cadaverine transport; IDA:EcoCyc.
DR GO; GO:1990451; P:cellular stress response to acidic pH; IEP:EcoCyc.
DR GO; GO:1903401; P:L-lysine transmembrane transport; IDA:EcoCyc.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004754; Amino_acid_antiprt.
DR Pfam; PF13520; AA_permease_2; 1.
DR TIGRFAMs; TIGR00905; 2A0302; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Antiport; Cell inner membrane; Cell membrane;
KW Membrane; Reference proteome; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..444
FT /note="Cadaverine/lysine antiporter"
FT /id="PRO_0000054244"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16877381"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..34
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:16877381"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16877381"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..122
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:16877381"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16877381"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..192
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:16877381"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16877381"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..272
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:16877381"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16877381"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..353
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:16877381"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16877381"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000305|PubMed:16877381"
FT MUTAGEN 12
FT /note="C->S: Does not affect cadaverine excretion and
FT cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 41
FT /note="W->L: Moderate decrease in cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 43
FT /note="W->L: Strong decrease in cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 55
FT /note="Y->L: Moderate decrease in both cadaverine excretion
FT and cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 57
FT /note="Y->L: Strong decrease in cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 73
FT /note="Y->L: Strong decrease in both cadaverine excretion
FT and cadaverine uptake. 9-fold increase in Km for cadaverine
FT for cadaverine uptake and 10-fold increase in Km for
FT cadaverine for cadaverine excretion."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 76
FT /note="E->Q: Moderate decrease in both cadaverine excretion
FT and cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 89
FT /note="Y->L: Strong decrease in both cadaverine excretion
FT and cadaverine uptake. 10-fold increase in Km for
FT cadaverine for cadaverine uptake and 5-fold increase in Km
FT for cadaverine for cadaverine excretion."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 90
FT /note="Y->L: Strong decrease in both cadaverine excretion
FT and cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 107
FT /note="Y->L: Strong decrease in cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 125
FT /note="C->S: Does not affect cadaverine excretion and
FT cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 174
FT /note="Y->L: Moderate decrease in cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 185
FT /note="D->N: Moderate decrease in cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 196
FT /note="C->S: Moderate decrease in both cadaverine excretion
FT and cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 204
FT /note="E->Q: Strong decrease in both cadaverine excretion
FT and cadaverine uptake. 22-fold increase in Km for
FT cadaverine for cadaverine uptake and 6-fold increase in Km
FT for cadaverine for cadaverine excretion."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 235
FT /note="Y->L: Strong decrease in both cadaverine excretion
FT and cadaverine uptake. 23-fold increase in Km for
FT cadaverine for cadaverine uptake and 7-fold increase in Km
FT for cadaverine for cadaverine excretion."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 246
FT /note="Y->L: Moderate decrease in both cadaverine excretion
FT and cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 282
FT /note="C->S: Moderate decrease in both cadaverine excretion
FT and cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 299
FT /note="R->A: Strong decrease in cadaverine excretion but
FT not in cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 303
FT /note="D->N: Strong decrease in both cadaverine excretion
FT and cadaverine uptake. 24-fold increase in Km for
FT cadaverine for cadaverine uptake and 9-fold increase in Km
FT for cadaverine for cadaverine excretion."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 310
FT /note="Y->L: Moderate decrease in both cadaverine excretion
FT and cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 366
FT /note="Y->L: Strong decrease in cadaverine uptake. 15-fold
FT increase in Km for cadaverine for cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 368
FT /note="Y->L: Strong decrease in cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 370
FT /note="C->S: Strong decrease in both cadaverine excretion
FT and cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 377
FT /note="E->Q: Moderate decrease in both cadaverine excretion
FT and cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 389
FT /note="C->S: Moderate decrease in both cadaverine excretion
FT and cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 394
FT /note="C->S: Moderate decrease in both cadaverine excretion
FT and cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 397
FT /note="C->S: Moderate decrease in both cadaverine excretion
FT and cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 408
FT /note="E->Q: Moderate decrease in cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
FT MUTAGEN 423
FT /note="Y->L: Strong decrease in both cadaverine excretion
FT and cadaverine uptake."
FT /evidence="ECO:0000269|PubMed:16877381"
SQ SEQUENCE 444 AA; 46665 MW; E87913B449B0500A CRC64;
MSSAKKIGLF ACTGVVAGNM MGSGIALLPA NLASIGGIAI WGWIISIIGA MSLAYVYARL
ATKNPQQGGP IAYAGEISPA FGFQTGVLYY HANWIGNLAI GITAVSYLST FFPVLNDPVP
AGIACIAIVW VFTFVNMLGG TWVSRLTTIG LVLVLIPVVM TAIVGWHWFD AATYAANWNT
ADTTDGHAII KSILLCLWAF VGVESAAVST GMVKNPKRTV PLATMLGTGL AGIVYIAATQ
VLSGMYPSSV MAASGAPFAI SASTILGNWA APLVSAFTAF ACLTSLGSWM MLVGQAGVRA
ANDGNFPKVY GEVDSNGIPK KGLLLAAVKM TALMILITLM NSAGGKASDL FGELTGIAVL
LTMLPYFYSC VDLIRFEGVN IRNFVSLICS VLGCVFCFIA LMGASSFELA GTFIVSLIIL
MFYARKMHER QSHSMDNHTA SNAH
