PSAA_THEVB
ID PSAA_THEVB Reviewed; 755 AA.
AC P0A405; P25896;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1;
DE EC=1.97.1.12 {ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800, ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876};
DE AltName: Full=PsaA;
GN Name=psaA; OrderedLocusNames=tlr0731;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP PRESENCE OF CHLOROPHYLL A' IN PSI.
RX PubMed=12755700; DOI=10.1046/j.1432-1033.2003.03616.x;
RA Nakamura A., Akai M., Yoshida E., Taki T., Watanabe T.;
RT "Reversed-phase HPLC determination of chlorophyll a' and phylloquinone in
RT photosystem I of oxygenic photosynthetic organisms.";
RL Eur. J. Biochem. 270:2446-2458(2003).
RN [3]
RP REVIEW.
RX PubMed=11687205; DOI=10.1016/s0005-2728(01)00195-5;
RA Fromme P., Jordan P., Krauss N.;
RT "Structure of photosystem I.";
RL Biochim. Biophys. Acta 1507:5-31(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=8901876; DOI=10.1038/nsb1196-965;
RA Krauss N., Schubert W.-D., Klukas O., Fromme P., Witt H.T., Saenger W.;
RT "Photosystem I at 4-A resolution represents the first structural model of a
RT joint photosynthetic reaction centre and core antenna system.";
RL Nat. Struct. Biol. 3:965-973(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10066799; DOI=10.1074/jbc.274.11.7351;
RA Klukas O., Schubert W.-D., Jordan P., Krauss N., Fromme P., Witt H.T.,
RA Saenger W.;
RT "Photosystem I, an improved model of the stromal subunits PsaC, PsaD, and
RT PsaE.";
RL J. Biol. Chem. 274:7351-7360(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10066800; DOI=10.1074/jbc.274.11.7361;
RA Klukas O., Schubert W.-D., Jordan P., Krauss N., Fromme P., Witt H.T.,
RA Saenger W.;
RT "Localization of two phylloquinones, QK and QK', in an improved electron
RT density map of photosystem I at 4-A resolution.";
RL J. Biol. Chem. 274:7361-7367(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11418848; DOI=10.1038/35082000;
RA Jordan P., Fromme P., Witt H.T., Klukas O., Saenger W., Krauss N.;
RT "Three-dimensional structure of cyanobacterial photosystem I at 2.5 A
RT resolution.";
RL Nature 411:909-917(2001).
CC -!- FUNCTION: PsaA and PsaB bind P700, the primary electron donor of
CC photosystem I (PSI), as well as the electron acceptors A0, A1 and FX.
CC PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase,
CC converting photonic excitation into a charge separation, which
CC transfers an electron from the donor P700 chlorophyll pair to the
CC spectroscopically characterized acceptors A0, A1, FX, FA and FB in
CC turn. Oxidized P700 is reduced on the lumenal side of the thylakoid
CC membrane by plastocyanin or cytochrome c6.
CC {ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800,
CC ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin]
CC = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:29036,
CC ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:49552; EC=1.97.1.12;
CC Evidence={ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800,
CC ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876};
CC -!- COFACTOR:
CC Note=PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2
CC phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll
CC a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a
CC chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1
CC is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur
CC center. {ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800,
CC ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876};
CC -!- SUBUNIT: The PsaA/B heterodimer binds the P700 chlorophyll special pair
CC and subsequent electron acceptors. PSI consists of a core antenna
CC complex that captures photons, and an electron transfer chain that
CC converts photonic excitation into a charge separation. The
CC cyanobacterial PSI reaction center is composed of one copy each of
CC PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes.
CC {ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800,
CC ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800,
CC ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10066799,
CC ECO:0000269|PubMed:10066800, ECO:0000269|PubMed:11418848,
CC ECO:0000269|PubMed:8901876}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC08282.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000039; BAC08282.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_681520.1; NC_004113.1.
DR PDB; 1C51; X-ray; 4.00 A; -.
DR PDB; 1JB0; X-ray; 2.50 A; A=1-755.
DR PDB; 2PPS; X-ray; 4.00 A; -.
DR PDB; 3PCQ; X-ray; 8.98 A; A=1-755.
DR PDB; 4FE1; X-ray; 4.92 A; A=1-755.
DR PDB; 5ZF0; X-ray; 4.20 A; A1/A2/A3/A4/A5/A6=1-755.
DR PDB; 6LU1; EM; 3.20 A; A=1-755.
DR PDB; 6PFY; X-ray; 2.90 A; A/G/Y=1-755.
DR PDB; 6PGK; X-ray; 2.90 A; A/G/Y=1-755.
DR PDB; 6TRA; EM; 2.85 A; A=1-755.
DR PDB; 6TRC; EM; 2.98 A; 1/A/a=1-755.
DR PDB; 6TRD; EM; 3.16 A; 1/A/a=1-755.
DR PDB; 7BW2; X-ray; 6.50 A; A=1-755.
DR PDB; 7M75; X-ray; 2.75 A; A=1-755.
DR PDB; 7M76; X-ray; 3.00 A; A=1-755.
DR PDB; 7M78; X-ray; 3.00 A; A=1-755.
DR PDBsum; 1C51; -.
DR PDBsum; 1JB0; -.
DR PDBsum; 2PPS; -.
DR PDBsum; 3PCQ; -.
DR PDBsum; 4FE1; -.
DR PDBsum; 5ZF0; -.
DR PDBsum; 6LU1; -.
DR PDBsum; 6PFY; -.
DR PDBsum; 6PGK; -.
DR PDBsum; 6TRA; -.
DR PDBsum; 6TRC; -.
DR PDBsum; 6TRD; -.
DR PDBsum; 7BW2; -.
DR PDBsum; 7M75; -.
DR PDBsum; 7M76; -.
DR PDBsum; 7M78; -.
DR AlphaFoldDB; P0A405; -.
DR SMR; P0A405; -.
DR IntAct; P0A405; 11.
DR STRING; 197221.22294452; -.
DR EnsemblBacteria; BAC08282; BAC08282; BAC08282.
DR KEGG; tel:tlr0731; -.
DR PATRIC; fig|197221.4.peg.771; -.
DR eggNOG; COG2885; Bacteria.
DR OMA; TWAFFHA; -.
DR OrthoDB; 32023at2; -.
DR BRENDA; 1.97.1.12; 7763.
DR EvolutionaryTrace; P0A405; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1130.10; -; 1.
DR HAMAP; MF_00458; PSI_PsaA; 1.
DR InterPro; IPR006243; PSI_PsaA.
DR InterPro; IPR001280; PSI_PsaA/B.
DR InterPro; IPR020586; PSI_PsaA/B_CS.
DR InterPro; IPR036408; PSI_PsaA/B_sf.
DR PANTHER; PTHR30128:SF61; PTHR30128:SF61; 1.
DR Pfam; PF00223; PsaA_PsaB; 1.
DR PIRSF; PIRSF002905; PSI_A; 1.
DR PRINTS; PR00257; PHOTSYSPSAAB.
DR SUPFAM; SSF81558; SSF81558; 1.
DR TIGRFAMs; TIGR01335; psaA; 1.
DR PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Chlorophyll; Chromophore; Electron transport; Iron;
KW Iron-sulfur; Magnesium; Membrane; Metal-binding; Oxidoreductase;
KW Photosynthesis; Photosystem I; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..755
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088591"
FT TOPO_DOM 1..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 65..96
FT /note="Helical; Name=I"
FT TOPO_DOM 97..155
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 156..179
FT /note="Helical; Name=II"
FT TOPO_DOM 180..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 193..217
FT /note="Helical; Name=III"
FT TOPO_DOM 218..293
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 294..311
FT /note="Helical; Name=IV"
FT TOPO_DOM 312..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 353..376
FT /note="Helical; Name=V"
FT TOPO_DOM 377..386
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 387..418
FT /note="Helical; Name=VI"
FT TOPO_DOM 419..436
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 437..468
FT /note="Helical; Name=VII"
FT TOPO_DOM 469..532
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 533..558
FT /note="Helical; Name=VIII"
FT TOPO_DOM 559..590
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 591..619
FT /note="Helical; Name=IX"
FT TOPO_DOM 620..668
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 669..690
FT /note="Helical; Name=X"
FT TOPO_DOM 691..723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 724..753
FT /note="Helical; Name=XI"
FT BINDING 578
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:11418848"
FT BINDING 587
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:11418848"
FT BINDING 680
FT /ligand="chlorophyll a'"
FT /ligand_id="ChEBI:CHEBI:189419"
FT /ligand_label="A1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:11418848"
FT BINDING 688
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:11418848"
FT BINDING 696
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000269|PubMed:10066800,
FT ECO:0000269|PubMed:11418848"
FT BINDING 697
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000269|PubMed:10066800,
FT ECO:0000269|PubMed:11418848"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 25..29
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6TRA"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 65..96
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6TRC"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:7M75"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 155..181
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:6TRA"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:6TRA"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:7M76"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:6PGK"
FT HELIX 294..311
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 325..331
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 338..343
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 344..350
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 352..376
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:7M75"
FT HELIX 387..418
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 429..434
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 437..453
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 456..468
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 485..496
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 533..558
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:6TRA"
FT HELIX 569..572
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:6TRD"
FT HELIX 582..584
FT /evidence="ECO:0007829|PDB:7M75"
FT HELIX 591..620
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 627..629
FT /evidence="ECO:0007829|PDB:6TRC"
FT STRAND 631..633
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 634..637
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 639..642
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:7M75"
FT HELIX 646..651
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 654..657
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 659..663
FT /evidence="ECO:0007829|PDB:1JB0"
FT TURN 665..669
FT /evidence="ECO:0007829|PDB:6TRC"
FT HELIX 670..691
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 694..710
FT /evidence="ECO:0007829|PDB:1JB0"
FT STRAND 716..718
FT /evidence="ECO:0007829|PDB:1JB0"
FT HELIX 724..754
FT /evidence="ECO:0007829|PDB:1JB0"
SQ SEQUENCE 755 AA; 83183 MW; 36A39CCE5D119AEA CRC64;
MTISPPEREP KVRVVVDNDP VPTSFEKWAK PGHFDRTLAR GPQTTTWIWN LHALAHDFDT
HTSDLEDISR KIFSAHFGHL AVVFIWLSGM YFHGAKFSNY EAWLADPTGI KPSAQVVWPI
VGQGILNGDV GGGFHGIQIT SGLFQLWRAS GITNEFQLYC TAIGGLVMAG LMLFAGWFHY
HKRAPKLEWF QNVESMLNHH LAGLLGLGSL AWAGHQIHVS LPINKLLDAG VAAKDIPLPH
EFILNPSLMA ELYPKVDWGF FSGVIPFFTF NWAAYSDFLT FNGGLNPVTG GLWLSDTAHH
HLAIAVLFII AGHMYRTNWG IGHSLKEILE AHKGPFTGAG HKGLYEVLTT SWHAQLAINL
AMMGSLSIIV AQHMYAMPPY PYLATDYPTQ LSLFTHHMWI GGFLVVGGAA HGAIFMVRDY
DPAMNQNNVL DRVLRHRDAI ISHLNWVCIF LGFHSFGLYV HNDTMRAFGR PQDMFSDTGI
QLQPVFAQWV QNLHTLAPGG TAPNAAATAS VAFGGDVVAV GGKVAMMPIV LGTADFMVHH
IHAFTIHVTV LILLKGVLFA RSSRLIPDKA NLGFRFPCDG PGRGGTCQVS GWDHVFLGLF
WMYNCISVVI FHFSWKMQSD VWGTVAPDGT VSHITGGNFA QSAITINGWL RDFLWAQASQ
VIGSYGSALS AYGLLFLGAH FIWAFSLMFL FSGRGYWQEL IESIVWAHNK LKVAPAIQPR
ALSIIQGRAV GVAHYLLGGI ATTWAFFLAR IISVG
