MALF_ECOLI
ID MALF_ECOLI Reviewed; 514 AA.
AC P02916; Q2M6S1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Maltose/maltodextrin transport system permease protein MalF {ECO:0000305};
GN Name=malF {ECO:0000303|PubMed:6088520}; OrderedLocusNames=b4033, JW3993;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6088520; DOI=10.1016/s0021-9258(18)90597-1;
RA Froshauer S., Beckwith J.;
RT "The nucleotide sequence of the gene for malF protein, an inner membrane
RT component of the maltose transport system of Escherichia coli. Repeated DNA
RT sequences are found in the malE-malF intercistronic region.";
RL J. Biol. Chem. 259:10896-10903(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 469-514.
RX PubMed=3000770; DOI=10.1002/j.1460-2075.1985.tb03928.x;
RA Dassa E., Hofnung M.;
RT "Sequence of gene malG in E. coli K12: homologies between integral membrane
RT components from binding protein-dependent transport systems.";
RL EMBO J. 4:2287-2293(1985).
RN [6]
RP TOPOLOGY.
RX PubMed=16453726;
RA von Heijne G.;
RT "The distribution of positively charged residues in bacterial inner
RT membrane proteins correlates with the trans-membrane topology.";
RL EMBO J. 5:3021-3027(1986).
RN [7]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=2155217; DOI=10.1016/s0021-9258(19)39555-9;
RA Davidson A.L., Nikaido H.;
RT "Overproduction, solubilization, and reconstitution of the maltose
RT transport system from Escherichia coli.";
RL J. Biol. Chem. 265:4254-4260(1990).
RN [8]
RP TOPOLOGY.
RX PubMed=2170984; DOI=10.1073/pnas.87.19.7574;
RA Ehrmann M., Boyd D., Beckwith J.;
RT "Genetic analysis of membrane protein topology by a sandwich gene fusion
RT approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7574-7578(1990).
RN [9]
RP TOPOLOGY.
RX PubMed=1915262; DOI=10.1002/j.1460-2075.1991.tb07826.x;
RA McGovern K., Ehrmann M., Beckwith J.;
RT "Decoding signals for membrane protein assembly using alkaline phosphatase
RT fusions.";
RL EMBO J. 10:2773-2782(1991).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=2026607; DOI=10.1016/s0021-9258(18)31535-7;
RA Davidson A.L., Nikaido H.;
RT "Purification and characterization of the membrane-associated components of
RT the maltose transport system from Escherichia coli.";
RL J. Biol. Chem. 266:8946-8951(1991).
RN [11]
RP MUTAGENESIS OF GLU-401; SER-403; GLY-407 AND PRO-420.
RX PubMed=9214624; DOI=10.1093/emboj/16.11.3066;
RA Mourez M., Hofnung M., Dassa E.;
RT "Subunit interactions in ABC transporters: a conserved sequence in
RT hydrophobic membrane proteins of periplasmic permeases defines an important
RT site of interaction with the ATPase subunits.";
RL EMBO J. 16:3066-3077(1997).
RN [12]
RP MUTAGENESIS OF LEU-334.
RX PubMed=9401026; DOI=10.1128/jb.179.24.7687-7694.1997;
RA Merino G., Shuman H.A.;
RT "Unliganded maltose-binding protein triggers lactose transport in an
RT Escherichia coli mutant with an alteration in the maltose transport
RT system.";
RL J. Bacteriol. 179:7687-7694(1997).
RN [13]
RP MUTAGENESIS OF LEU-372; ASN-376 AND GLY-380.
RX PubMed=8636026; DOI=10.1128/jb.178.8.2255-2262.1996;
RA Ehrle R., Pick C., Ulrich R., Hofmann E., Ehrmann M.;
RT "Characterization of transmembrane domains 6, 7, and 8 of MalF by
RT mutational analysis.";
RL J. Bacteriol. 178:2255-2262(1996).
RN [14]
RP SUBUNIT INTERACTION, AND MUTAGENESIS OF GLU-401 AND SER-403.
RX PubMed=10809785; DOI=10.1074/jbc.275.20.15526;
RA Hunke S., Mourez M., Jehanno M., Dassa E., Schneider E.;
RT "ATP modulates subunit-subunit interactions in an ATP-binding cassette
RT transporter (MalFGK2) determined by site-directed chemical cross-linking.";
RL J. Biol. Chem. 275:15526-15534(2000).
RN [15]
RP 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 [16]
RP SUBUNIT, SUBCELLULAR LOCATION, AND REQUIREMENT FOR YIDC FOR PROTEIN AND
RP COMPLEX FORMATION.
RX PubMed=18456666; DOI=10.1074/jbc.m801481200;
RA Wagner S., Pop O.I., Haan G.J., Baars L., Koningstein G., Klepsch M.M.,
RA Genevaux P., Luirink J., de Gier J.W.;
RT "Biogenesis of MalF and the MalFGK(2) maltose transport complex in
RT Escherichia coli requires YidC.";
RL J. Biol. Chem. 283:17881-17890(2008).
RN [17]
RP REVIEW.
RX PubMed=9529892; DOI=10.1128/mmbr.62.1.204-229.1998;
RA Boos W., Shuman H.;
RT "Maltose/maltodextrin system of Escherichia coli: transport, metabolism,
RT and regulation.";
RL Microbiol. Mol. Biol. Rev. 62:204-229(1998).
CC -!- FUNCTION: Part of the ABC transporter complex MalEFGK involved in
CC maltose/maltodextrin import. Probably responsible for the translocation
CC of the substrate across the membrane. {ECO:0000269|PubMed:2026607,
CC ECO:0000269|PubMed:2155217}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MalK),
CC two transmembrane proteins (MalG and MalF) and a solute-binding protein
CC (MalE). Protein stability and stable complex formation require YidC.
CC {ECO:0000269|PubMed:10809785, ECO:0000269|PubMed:18456666,
CC ECO:0000269|PubMed:2026607, ECO:0000269|PubMed:2155217}.
CC -!- INTERACTION:
CC P02916; P0AEX9: malE; NbExp=5; IntAct=EBI-1118919, EBI-369910;
CC P02916; P68183: malG; NbExp=5; IntAct=EBI-1118919, EBI-6400985;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:18456666}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:18456666};
CC Periplasmic side {ECO:0000269|PubMed:18456666}. Note=A substantial
CC portion of it protrudes into the periplasmic space; inserts in an
CC SRP- and Sec-dependent, YidC-independent fashion into the membrane.
CC -!- MISCELLANEOUS: When MalF EAA loop mutations are made concomitantly with
CC MalG EAA loop mutations, a complete loss of transport and complex
CC formation is observed, except for the Gly-407. This suggests that the
CC MalF-MalG interaction may be important for the proper assembly and also
CC for the correct function of the transporter.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. MalFG subfamily. {ECO:0000305}.
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DR EMBL; J01648; AAB59055.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43127.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77003.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78035.1; -; Genomic_DNA.
DR EMBL; X02871; CAA26627.1; -; Genomic_DNA.
DR PIR; A03414; MMECMF.
DR RefSeq; NP_418457.1; NC_000913.3.
DR RefSeq; WP_001297290.1; NZ_STEB01000022.1.
DR PDB; 2R6G; X-ray; 2.80 A; F=1-514.
DR PDB; 3FH6; X-ray; 4.50 A; F/H=36-514.
DR PDB; 3PUV; X-ray; 2.40 A; F=1-514.
DR PDB; 3PUW; X-ray; 2.30 A; F=1-514.
DR PDB; 3PUX; X-ray; 2.30 A; F=1-514.
DR PDB; 3PUY; X-ray; 3.10 A; F=1-514.
DR PDB; 3PUZ; X-ray; 2.90 A; F=1-514.
DR PDB; 3PV0; X-ray; 3.10 A; F=1-514.
DR PDB; 3RLF; X-ray; 2.20 A; F=1-514.
DR PDB; 4JBW; X-ray; 3.91 A; F/H=1-514.
DR PDB; 4KHZ; X-ray; 2.90 A; F=1-514.
DR PDB; 4KI0; X-ray; 2.38 A; F=1-514.
DR PDBsum; 2R6G; -.
DR PDBsum; 3FH6; -.
DR PDBsum; 3PUV; -.
DR PDBsum; 3PUW; -.
DR PDBsum; 3PUX; -.
DR PDBsum; 3PUY; -.
DR PDBsum; 3PUZ; -.
DR PDBsum; 3PV0; -.
DR PDBsum; 3RLF; -.
DR PDBsum; 4JBW; -.
DR PDBsum; 4KHZ; -.
DR PDBsum; 4KI0; -.
DR AlphaFoldDB; P02916; -.
DR BMRB; P02916; -.
DR SMR; P02916; -.
DR BioGRID; 4261701; 15.
DR ComplexPortal; CPX-1932; Maltose ABC transporter complex.
DR ComplexPortal; CPX-1978; Enzyme IIA-maltose transport inhibitory complex.
DR DIP; DIP-10142N; -.
DR IntAct; P02916; 7.
DR STRING; 511145.b4033; -.
DR TCDB; 3.A.1.1.1; the atp-binding cassette (abc) superfamily.
DR jPOST; P02916; -.
DR PaxDb; P02916; -.
DR PRIDE; P02916; -.
DR EnsemblBacteria; AAC77003; AAC77003; b4033.
DR EnsemblBacteria; BAE78035; BAE78035; BAE78035.
DR GeneID; 58390124; -.
DR GeneID; 948532; -.
DR KEGG; ecj:JW3993; -.
DR KEGG; eco:b4033; -.
DR PATRIC; fig|511145.12.peg.4148; -.
DR EchoBASE; EB0550; -.
DR eggNOG; COG1175; Bacteria.
DR HOGENOM; CLU_016047_20_0_6; -.
DR InParanoid; P02916; -.
DR OMA; DGHNSTK; -.
DR PhylomeDB; P02916; -.
DR BioCyc; EcoCyc:MALF-MON; -.
DR BioCyc; MetaCyc:MALF-MON; -.
DR BRENDA; 7.5.2.1; 2026.
DR EvolutionaryTrace; P02916; -.
DR PRO; PR:P02916; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:EcoCyc.
DR GO; GO:1990154; C:enzyme IIA-maltose transporter complex; IPI:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:1990060; C:maltose transport complex; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015423; F:ABC-type maltose transporter activity; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0042956; P:maltodextrin transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0015768; P:maltose transport; IDA:EcoCyc.
DR GO; GO:1902344; P:negative regulation of maltose transport; IC:ComplexPortal.
DR GO; GO:0034763; P:negative regulation of transmembrane transport; IC:ComplexPortal.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR Gene3D; 1.20.58.370; -; 1.
DR InterPro; IPR030156; MalF-like.
DR InterPro; IPR035277; MalF_N.
DR InterPro; IPR029345; MalF_P2.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR47314:SF1; PTHR47314:SF1; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF14785; MalF_P2; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..514
FT /note="Maltose/maltodextrin transport system permease
FT protein MalF"
FT /id="PRO_0000060068"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..36
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 37..39
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 40..58
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 59..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 67..92
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 93..275
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 276..306
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 307..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 319..336
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 337..369
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 370..392
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 393..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 426..452
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 453..483
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 484..505
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 506..514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 281..505
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT MUTAGEN 334
FT /note="L->W: Ability to transport lactose in a saturable
FT manner."
FT /evidence="ECO:0000269|PubMed:9401026"
FT MUTAGEN 372
FT /note="L->W: Growth on maltose but not on media containing
FT either maltoheptaose or maltoheptaose plus maltose."
FT /evidence="ECO:0000269|PubMed:8636026"
FT MUTAGEN 376
FT /note="N->K,H: No growth on maltose."
FT /evidence="ECO:0000269|PubMed:8636026"
FT MUTAGEN 380
FT /note="G->C,S: No growth on maltose."
FT /evidence="ECO:0000269|PubMed:8636026"
FT MUTAGEN 401
FT /note="E->A,C,K,L: Reduction of transport rate."
FT /evidence="ECO:0000269|PubMed:10809785,
FT ECO:0000269|PubMed:9214624"
FT MUTAGEN 403
FT /note="S->C,D,K,L: Reduction of transport rate."
FT /evidence="ECO:0000269|PubMed:10809785,
FT ECO:0000269|PubMed:9214624"
FT MUTAGEN 407
FT /note="G->A,P: No effect."
FT /evidence="ECO:0000269|PubMed:9214624"
FT MUTAGEN 420
FT /note="P->A: No effect."
FT /evidence="ECO:0000269|PubMed:9214624"
FT HELIX 14..29
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:3RLF"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 40..58
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:3PUW"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 113..127
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:3RLF"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 153..164
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:2R6G"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 200..213
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:3RLF"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:3RLF"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 262..269
FT /evidence="ECO:0007829|PDB:3RLF"
FT TURN 272..276
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 277..306
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:2R6G"
FT HELIX 314..322
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 329..339
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 346..353
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:3PUV"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 365..391
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 397..405
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 418..438
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 441..447
FT /evidence="ECO:0007829|PDB:3RLF"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:3PUW"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:3RLF"
FT HELIX 467..475
FT /evidence="ECO:0007829|PDB:3RLF"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:2R6G"
FT HELIX 484..501
FT /evidence="ECO:0007829|PDB:3RLF"
FT TURN 502..504
FT /evidence="ECO:0007829|PDB:3PV0"
SQ SEQUENCE 514 AA; 57013 MW; 895CEA1986CE5C0B CRC64;
MDVIKKKHWW QSDALKWSVL GLLGLLVGYL VVLMYAQGEY LFAITTLILS SAGLYIFANR
KAYAWRYVYP GMAGMGLFVL FPLVCTIAIA FTNYSSTNQL TFERAQEVLL DRSWQAGKTY
NFGLYPAGDE WQLALSDGET GKNYLSDAFK FGGEQKLQLK ETTAQPEGER ANLRVITQNR
QALSDITAIL PDGNKVMMSS LRQFSGTQPL YTLDGDGTLT NNQSGVKYRP NNQIGFYQSI
TADGNWGDEK LSPGYTVTTG WKNFTRVFTD EGIQKPFLAI FVWTVVFSLI TVFLTVAVGM
VLACLVQWEA LRGKAVYRVL LILPYAVPSF ISILIFKGLF NQSFGEINMM LSALFGVKPA
WFSDPTTART MLIIVNTWLG YPYMMILCMG LLKAIPDDLY EASAMDGAGP FQNFFKITLP
LLIKPLTPLM IASFAFNFNN FVLIQLLTNG GPDRLGTTTP AGYTDLLVNY TYRIAFEGGG
GQDFGLAAAI ATLIFLLVGA LAIVNLKATR MKFD
