ADIC_ECOLI
ID ADIC_ECOLI Reviewed; 445 AA.
AC P60061; P39268; P39269; Q2M6I9;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Arginine/agmatine antiporter {ECO:0000303|PubMed:12867448};
GN Name=adiC {ECO:0000303|PubMed:12867448, ECO:0000303|PubMed:14594828};
GN Synonyms=aniC, yjdD, yjdE; OrderedLocusNames=b4115, JW4076;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
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 [3]
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 [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION,
RP OPERON, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=12867448; DOI=10.1128/jb.185.15.4402-4409.2003;
RA Gong S., Richard H., Foster J.W.;
RT "YjdE (AdiC) is the arginine:agmatine antiporter essential for arginine-
RT dependent acid resistance in Escherichia coli.";
RL J. Bacteriol. 185:4402-4409(2003).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14594828; DOI=10.1128/jb.185.22.6556-6561.2003;
RA Iyer R., Williams C., Miller C.;
RT "Arginine-agmatine antiporter in extreme acid resistance in Escherichia
RT coli.";
RL J. Bacteriol. 185:6556-6561(2003).
RN [6]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
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 [7]
RP FUNCTION, AND MUTAGENESIS OF TYR-93; TRP-202 AND TRP-293.
RX PubMed=19578361; DOI=10.1038/nature08201;
RA Fang Y., Jayaram H., Shane T., Kolmakova-Partensky L., Wu F., Williams C.,
RA Xiong Y., Miller C.;
RT "Structure of a prokaryotic virtual proton pump at 3.2 A resolution.";
RL Nature 460:1040-1043(2009).
RN [8] {ECO:0007744|PDB:3OB6}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF ASP-101 MUTANT IN OUTWARD-OPEN
RP CONFORMATION IN COMPLEX WITH SUBSTRATE (ARG), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND MUTAGENESIS OF ASN-101 AND TRP-293.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=21368142; DOI=10.1073/pnas.1018081108;
RA Kowalczyk L., Ratera M., Paladino A., Bartoccioni P.,
RA Errasti-Murugarren E., Valencia E., Portella G., Bial S., Zorzano A.,
RA Fita I., Orozco M., Carpena X., Vazquez-Ibar J.L., Palacin M.;
RT "Molecular basis of substrate-induced permeation by an amino acid
RT antiporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:3935-3940(2011).
RN [9] {ECO:0007744|PDB:5J4I, ECO:0007744|PDB:5J4N}
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS)IN OUTWARD-OPEN CONFORMATION IN THE
RP PRESENCE AND ABSENCE OF AGMATINE, SUBUNIT, AND MUTAGENESIS OF MET-104;
RP ILE-205 AND SER-357.
RC STRAIN=K12 / XL1-Blue;
RX PubMed=27582465; DOI=10.1073/pnas.1605442113;
RA Ilgu H., Jeckelmann J.M., Gapsys V., Ucurum Z., de Groot B.L., Fotiadis D.;
RT "Insights into the molecular basis for substrate binding and specificity of
RT the wild-type L-arginine/agmatine antiporter AdiC.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:10358-10363(2016).
CC -!- FUNCTION: Major component of the acid-resistance (AR) system allowing
CC enteric pathogens to survive the acidic environment in the stomach
CC (Probable). Exchanges extracellular arginine for its intracellular
CC decarboxylation product agmatine (Agm) thereby expelling intracellular
CC protons (PubMed:12867448, PubMed:14594828, PubMed:19578361,
CC PubMed:21368142). Probably undergoes several conformational states in
CC order to translocate the substrate across the membrane; keeps the
CC substrate accessible to only 1 side of the membrane at a time by
CC opening and closing 3 membrane-internal gates (Probable).
CC {ECO:0000269|PubMed:12867448, ECO:0000269|PubMed:14594828,
CC ECO:0000269|PubMed:19578361, ECO:0000269|PubMed:21368142,
CC ECO:0000305|PubMed:14594828, ECO:0000305|PubMed:21368142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=agmatine(in) + L-arginine(out) = agmatine(out) + L-
CC arginine(in); Xref=Rhea:RHEA:29651, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:58145; Evidence={ECO:0000269|PubMed:12867448,
CC ECO:0000269|PubMed:14594828, ECO:0000269|PubMed:19578361,
CC ECO:0000269|PubMed:21368142};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29652;
CC Evidence={ECO:0000269|PubMed:12867448, ECO:0000269|PubMed:14594828,
CC ECO:0000269|PubMed:19578361, ECO:0000269|PubMed:21368142};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for Arg {ECO:0000269|PubMed:21368142};
CC Vmax=50 pmol/min/ug enzyme for Arg-Agm exchange
CC {ECO:0000269|PubMed:21368142};
CC pH dependence:
CC Optimum pH is 2.5 for Arg-Agm exchange. {ECO:0000269|PubMed:12867448,
CC ECO:0000269|PubMed:14594828};
CC -!- SUBUNIT: Homodimer; each subunit has its own individual transport
CC capacity. {ECO:0000269|PubMed:21368142, ECO:0000269|PubMed:27582465}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000305|PubMed:12867448}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21368142}.
CC -!- INDUCTION: By acidic conditions, a monocistronic operon (at protein
CC level). {ECO:0000269|PubMed:12867448}.
CC -!- DOMAIN: Each subunit has 12 transmembrane (TM) helices; TM1 and TM6 are
CC interrupted by short non-helical Gly-rich loops in the middle of their
CC transmembrane spans. Each subunit has a central cavity which binds
CC substrate. {ECO:0000269|PubMed:21368142, ECO:0000269|PubMed:27582465}.
CC -!- DISRUPTION PHENOTYPE: Loss of arginine-dependent acid resistance. No
CC coupled transport of arginine and agmatine (PubMed:12867448,
CC PubMed:14594828). No effect on levels of AdiA (PubMed:12867448).
CC {ECO:0000269|PubMed:12867448, ECO:0000269|PubMed:14594828}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97014.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA97015.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97015.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U14003; AAA97014.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC77076.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78117.1; -; Genomic_DNA.
DR PIR; B65221; B65221.
DR PIR; S56343; S56343.
DR RefSeq; NP_418539.1; NC_000913.3.
DR RefSeq; WP_000093154.1; NZ_STEB01000014.1.
DR PDB; 3OB6; X-ray; 3.00 A; A/B=1-445.
DR PDB; 5J4I; X-ray; 2.21 A; A/B=1-445.
DR PDB; 5J4N; X-ray; 2.59 A; A/B=1-445.
DR PDBsum; 3OB6; -.
DR PDBsum; 5J4I; -.
DR PDBsum; 5J4N; -.
DR AlphaFoldDB; P60061; -.
DR SMR; P60061; -.
DR BioGRID; 4263081; 7.
DR DIP; DIP-59619N; -.
DR STRING; 511145.b4115; -.
DR TCDB; 2.A.3.2.5; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P60061; -.
DR PRIDE; P60061; -.
DR ABCD; P60061; 1 sequenced antibody.
DR EnsemblBacteria; AAC77076; AAC77076; b4115.
DR EnsemblBacteria; BAE78117; BAE78117; BAE78117.
DR GeneID; 66671974; -.
DR GeneID; 948628; -.
DR KEGG; ecj:JW4076; -.
DR KEGG; eco:b4115; -.
DR PATRIC; fig|1411691.4.peg.2585; -.
DR EchoBASE; EB2355; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_1_0_6; -.
DR InParanoid; P60061; -.
DR OMA; YDGWILI; -.
DR PhylomeDB; P60061; -.
DR BioCyc; EcoCyc:YJDE-MON; -.
DR BioCyc; MetaCyc:YJDE-MON; -.
DR PRO; PR:P60061; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015297; F:antiporter activity; IDA:EcoCyc.
DR GO; GO:0043862; F:arginine:agmatine antiporter activity; IDA:GO_Central.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0003333; P:amino acid transmembrane transport; IDA:EcoCyc.
DR GO; GO:0051454; P:intracellular pH elevation; IMP:EcoCyc.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Antiport; Cell inner membrane;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..445
FT /note="Arginine/agmatine antiporter"
FT /id="PRO_0000054230"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..24
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:5J4I"
FT TOPO_DOM 25..40
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..62
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:5J4I"
FT TOPO_DOM 63..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..113
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:5J4I"
FT TOPO_DOM 114..123
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..142
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:5J4I"
FT TOPO_DOM 143..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..171
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:5J4I"
FT TOPO_DOM 172..188
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..204
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:5J4I"
FT TOPO_DOM 205..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..247
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:5J4I"
FT TOPO_DOM 248..272
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..301
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:5J4I"
FT TOPO_DOM 302..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..343
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:5J4I"
FT TOPO_DOM 344..346
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..370
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:5J4I"
FT TOPO_DOM 371..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..404
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:5J4I"
FT TOPO_DOM 405..408
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..427
FT /note="Helical"
FT /evidence="ECO:0007744|PDB:5J4I"
FT TOPO_DOM 428..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:15919996"
FT BINDING 23
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000269|PubMed:27582465,
FT ECO:0007744|PDB:5J4N"
FT BINDING 23
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:21368142,
FT ECO:0007744|PDB:3OB6"
FT BINDING 26
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:21368142,
FT ECO:0007744|PDB:3OB6"
FT BINDING 96
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000269|PubMed:27582465,
FT ECO:0007744|PDB:5J4N"
FT BINDING 96
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:21368142,
FT ECO:0007744|PDB:3OB6"
FT BINDING 97
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000269|PubMed:27582465,
FT ECO:0007744|PDB:5J4N"
FT BINDING 101
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000269|PubMed:27582465,
FT ECO:0007744|PDB:5J4N"
FT BINDING 104
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000269|PubMed:27582465"
FT BINDING 202
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:21368142"
FT BINDING 203
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000269|PubMed:27582465"
FT BINDING 205
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000269|PubMed:27582465,
FT ECO:0007744|PDB:5J4N"
FT BINDING 205
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:21368142"
FT BINDING 293
FT /ligand="agmatine"
FT /ligand_id="ChEBI:CHEBI:58145"
FT /evidence="ECO:0000269|PubMed:27582465"
FT BINDING 357
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:21368142"
FT SITE 93
FT /note="Cytoplasmic (distal) gate"
FT /evidence="ECO:0000305|PubMed:27582465"
FT SITE 202
FT /note="Periplasmic (proximal) gate"
FT /evidence="ECO:0000250|UniProtKB:P60063"
FT SITE 208
FT /note="Cytoplasmic (distal) gate"
FT /evidence="ECO:0000305|PubMed:27582465"
FT SITE 293
FT /note="Middle gate"
FT /evidence="ECO:0000250|UniProtKB:P60063"
FT SITE 365
FT /note="Cytoplasmic (distal) gate"
FT /evidence="ECO:0000305|PubMed:27582465"
FT MUTAGEN 93
FT /note="Y->L: Greatly decreased Arg uptake into liposomes."
FT /evidence="ECO:0000269|PubMed:19578361"
FT MUTAGEN 101
FT /note="N->A: Vmax for Arg-Agm exchange 1% of wild-type, KM
FT increases 3-fold."
FT /evidence="ECO:0000269|PubMed:21368142"
FT MUTAGEN 101
FT /note="N->D: Nearly wild-type Arg-Agm exchange."
FT /evidence="ECO:0000269|PubMed:21368142"
FT MUTAGEN 104
FT /note="M->A: 30% decreased affinity for Arg, 50% decreased
FT affinity for Agm."
FT /evidence="ECO:0000269|PubMed:27582465"
FT MUTAGEN 202
FT /note="W->L: Halves Arg uptake into liposomes."
FT /evidence="ECO:0000269|PubMed:19578361"
FT MUTAGEN 205
FT /note="I->A: About wild-type affinity for Arg and Agm."
FT /evidence="ECO:0000269|PubMed:27582465"
FT MUTAGEN 293
FT /note="W->C,H,L: Loss of Arg-Agm exchange."
FT /evidence="ECO:0000269|PubMed:19578361,
FT ECO:0000269|PubMed:21368142"
FT MUTAGEN 293
FT /note="W->F,Y: Less than 20% Arg-Agm exchange activity.
FT Vmax 15% of wild-type rate."
FT /evidence="ECO:0000269|PubMed:21368142"
FT MUTAGEN 357
FT /note="S->A: 20% decreased affinity for Arg, 40% decrease
FT affinity for Agm."
FT /evidence="ECO:0000269|PubMed:27582465"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:5J4I"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 42..66
FT /evidence="ECO:0007829|PDB:5J4I"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 83..112
FT /evidence="ECO:0007829|PDB:5J4I"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 122..142
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 144..168
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:5J4I"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 189..200
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:5J4I"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:5J4I"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 220..249
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 252..257
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 272..306
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 324..338
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 344..360
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 362..376
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 384..403
FT /evidence="ECO:0007829|PDB:5J4I"
FT HELIX 407..428
FT /evidence="ECO:0007829|PDB:5J4I"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:5J4I"
SQ SEQUENCE 445 AA; 46843 MW; 359F70C489A20663 CRC64;
MSSDADAHKV GLIPVTLMVS GNIMGSGVFL LPANLASTGG IAIYGWLVTI IGALGLSMVY
AKMSFLDPSP GGSYAYARRC FGPFLGYQTN VLYWLACWIG NIAMVVIGVG YLSYFFPILK
DPLVLTITCV VVLWIFVLLN IVGPKMITRV QAVATVLALI PIVGIAVFGW FWFRGETYMA
AWNVSGLGTF GAIQSTLNVT LWSFIGVESA SVAAGVVKNP KRNVPIATIG GVLIAAVCYV
LSTTAIMGMI PNAALRVSAS PFGDAARMAL GDTAGAIVSF CAAAGCLGSL GGWTLLAGQT
AKAAADDGLF PPIFARVNKA GTPVAGLIIV GILMTIFQLS SISPNATKEF GLVSSVSVIF
TLVPYLYTCA ALLLLGHGHF GKARPAYLAV TTIAFLYCIW AVVGSGAKEV MWSFVTLMVI
TAMYALNYNR LHKNPYPLDA PISKD
