LHCA5_ARATH
ID LHCA5_ARATH Reviewed; 256 AA.
AC Q9C639; B9DFW4; Q8L9Y7; Q9XF85;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Photosystem I chlorophyll a/b-binding protein 5, chloroplastic {ECO:0000303|PubMed:10366881};
DE Short=Lhca5 {ECO:0000303|PubMed:10366881};
DE AltName: Full=LHCI type III LHCA5 {ECO:0000305};
DE Flags: Precursor;
GN Name=LHCA5 {ECO:0000303|PubMed:10366881};
GN OrderedLocusNames=At1g45474 {ECO:0000312|Araport:AT1G45474};
GN ORFNames=F2G19.4 {ECO:0000312|EMBL:AAG50618.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RX PubMed=10366881; DOI=10.1016/s1360-1385(99)01419-3;
RA Jansson S.;
RT "A guide to the Lhc genes and their relatives in Arabidopsis.";
RL Trends Plant Sci. 4:236-240(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-256.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [8]
RP REVIEW ON PHOTOSYSTEM I ANTENNA.
RX PubMed=12324436; DOI=10.1016/s0006-3495(02)73979-9;
RA Ihalainen J.A., Jensen P.E., Haldrup A., van Stokkum I.H.M.,
RA van Grondelle R., Scheller H.V., Dekker J.P.;
RT "Pigment organization and energy transfer dynamics in isolated photosystem
RT I (PSI) complexes from Arabidopsis thaliana depleted of the PSI-G, PSI-K,
RT PSI-L, or PSI-N subunit.";
RL Biophys. J. 83:2190-2201(2002).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY LIGHT AND COLD, INTERACTION
RP WITH LHCA2 AND LHCA3, AND COFACTOR.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=15356385; DOI=10.1023/b:plan.0000040813.05224.94;
RA Ganeteg U., Klimmek F., Jansson S.;
RT "Lhca5--an LHC-type protein associated with photosystem I.";
RL Plant Mol. Biol. 54:641-651(2004).
RN [10]
RP FUNCTION, COFACTOR, SUBUNIT, INTERACTION WITH LHCA1, AND MISCELLANEOUS.
RX PubMed=15563470; DOI=10.1074/jbc.m411248200;
RA Storf S., Jansson S., Schmid V.H.R.;
RT "Pigment binding, fluorescence properties, and oligomerization behavior of
RT Lhca5, a novel light-harvesting protein.";
RL J. Biol. Chem. 280:5163-5168(2005).
RN [11]
RP INTERACTION WITH LHCA2, AND HOMODIMER.
RC STRAIN=cv. Columbia;
RX PubMed=17107674; DOI=10.1016/j.febslet.2006.10.063;
RA Lucinski R., Schmid V.H., Jansson S., Klimmek F.;
RT "Lhca5 interaction with plant photosystem I.";
RL FEBS Lett. 580:6485-6488(2006).
RN [12]
RP COFACTOR, AND SUBUNIT.
RX PubMed=19139095; DOI=10.1074/jbc.m808395200;
RA Wientjes E., Oostergetel G.T., Jansson S., Boekema E.J., Croce R.;
RT "The role of Lhca complexes in the supramolecular organization of higher
RT plant photosystem I.";
RL J. Biol. Chem. 284:7803-7810(2009).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=19903870; DOI=10.1105/tpc.109.068791;
RA Peng L., Fukao Y., Fujiwara M., Takami T., Shikanai T.;
RT "Efficient operation of NAD(P)H dehydrogenase requires supercomplex
RT formation with photosystem I via minor LHCI in Arabidopsis.";
RL Plant Cell 21:3623-3640(2009).
RN [14]
RP INTERACTION WITH LHCA1, AND FUNCTION.
RX PubMed=21806943; DOI=10.1016/j.bpj.2011.06.045;
RA Wientjes E., van Stokkum I.H.M., van Amerongen H., Croce R.;
RT "The role of the individual Lhcas in photosystem I excitation energy
RT trapping.";
RL Biophys. J. 101:745-754(2011).
RN [15]
RP REVIEW ON NDH-PSI SUPERCOMPLEX.
RX PubMed=21785130; DOI=10.1093/pcp/pcr098;
RA Ifuku K., Endo T., Shikanai T., Aro E.M.;
RT "Structure of the chloroplast NADH dehydrogenase-like complex: nomenclature
RT for nuclear-encoded subunits.";
RL Plant Cell Physiol. 52:1560-1568(2011).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21278308; DOI=10.1104/pp.110.171264;
RA Peng L., Shikanai T.;
RT "Supercomplex formation with photosystem I is required for the
RT stabilization of the chloroplast NADH dehydrogenase-like complex in
RT Arabidopsis.";
RL Plant Physiol. 155:1629-1639(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-33, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER LYS-32, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: The light-harvesting complex (LHC) functions as a light
CC receptor, it captures and delivers excitation energy to photosystems
CC with which it is closely associated (PubMed:15563470, PubMed:21806943).
CC Seems involved in the function of the photosystem I in low light
CC conditions, when other LHCA proteins are less abundant
CC (PubMed:15356385). Required, together with LHCA6, for the formation of
CC a full-size NAD(P)H dehydrogenase-photosystem I supercomplex (NDH-PSI)
CC that triggers cyclic and chlororespiratory electron transport in
CC chloroplast thylakoids, especially under stress conditions (e.g.
CC increased light intensity) (Probable) (PubMed:19903870,
CC PubMed:21278308). {ECO:0000269|PubMed:15356385,
CC ECO:0000269|PubMed:15563470, ECO:0000269|PubMed:19903870,
CC ECO:0000269|PubMed:21278308, ECO:0000269|PubMed:21806943,
CC ECO:0000305|PubMed:21785130}.
CC -!- COFACTOR:
CC Note=Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and
CC carotenoids such as lutein and neoxanthin.
CC {ECO:0000269|PubMed:15356385, ECO:0000269|PubMed:15563470,
CC ECO:0000269|PubMed:19139095};
CC -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins
CC (PubMed:19139095). Homodimer. Heterodimer with LHCA2 and, possibly,
CC LHCA3 (PubMed:15356385, PubMed:17107674). Can substitute to LHCA4 to
CC form a complex with LHCA1 (PubMed:21806943, PubMed:15563470). Binds
CC pigments (PubMed:15563470). Element of the NAD(P)H dehydrogenase-
CC photosystem I supercomplex (NDH-PSI) (PubMed:19903870).
CC {ECO:0000269|PubMed:15356385, ECO:0000269|PubMed:15563470,
CC ECO:0000269|PubMed:17107674, ECO:0000269|PubMed:19139095,
CC ECO:0000269|PubMed:19903870, ECO:0000269|PubMed:21806943}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:15356385}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced by high light (HL) but repressed by low light (LL).
CC Slightly inhibited by cold. {ECO:0000269|PubMed:15356385}.
CC -!- DOMAIN: The N-terminus of the protein extends into the stroma where it
CC is involved with adhesion of granal membranes and post-translational
CC modifications; both are believed to mediate the distribution of
CC excitation energy between photosystems I and II. {ECO:0000305}.
CC -!- PTM: Photoregulated by reversible phosphorylation of its threonine
CC residues. {ECO:0000250|UniProtKB:P12333}.
CC -!- DISRUPTION PHENOTYPE: Slightly lower NDH activity in immature leaves.
CC Smaller version of the NAD(P)H dehydrogenase-photosystem I supercomplex
CC (NDH-PSI) supercomplex (PubMed:19903870). In the double mutant lhca5
CC lhca6, drastic reduction of NDH subunits accumulation upon increased
CC light intensity (PubMed:21278308). {ECO:0000269|PubMed:19903870,
CC ECO:0000269|PubMed:21278308}.
CC -!- MISCELLANEOUS: Light emission at 684 nm upon excitation at 410 and 470
CC nm. {ECO:0000269|PubMed:15563470}.
CC -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC (LHC) protein family. {ECO:0000305}.
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DR EMBL; AF134121; AAD28768.1; -; mRNA.
DR EMBL; AC083835; AAG50618.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32117.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32118.1; -; Genomic_DNA.
DR EMBL; AY062097; AAL32974.1; -; mRNA.
DR EMBL; AY090263; AAL90924.1; -; mRNA.
DR EMBL; AK221694; BAD95402.1; -; mRNA.
DR EMBL; AY088144; AAM65689.1; -; mRNA.
DR EMBL; AK316926; BAH19631.1; -; mRNA.
DR PIR; F96510; F96510.
DR PIR; T52328; T52328.
DR RefSeq; NP_175137.1; NM_103597.5.
DR RefSeq; NP_849778.1; NM_179447.2.
DR PDB; 7WFE; EM; 3.25 A; B5=1-256.
DR PDB; 7WG5; EM; 3.89 A; B5=1-256.
DR PDBsum; 7WFE; -.
DR PDBsum; 7WG5; -.
DR AlphaFoldDB; Q9C639; -.
DR SMR; Q9C639; -.
DR STRING; 3702.AT1G45474.2; -.
DR iPTMnet; Q9C639; -.
DR PaxDb; Q9C639; -.
DR PRIDE; Q9C639; -.
DR ProteomicsDB; 238447; -.
DR EnsemblPlants; AT1G45474.1; AT1G45474.1; AT1G45474.
DR EnsemblPlants; AT1G45474.2; AT1G45474.2; AT1G45474.
DR GeneID; 841099; -.
DR Gramene; AT1G45474.1; AT1G45474.1; AT1G45474.
DR Gramene; AT1G45474.2; AT1G45474.2; AT1G45474.
DR KEGG; ath:AT1G45474; -.
DR Araport; AT1G45474; -.
DR TAIR; locus:2825741; AT1G45474.
DR eggNOG; ENOG502S212; Eukaryota.
DR HOGENOM; CLU_057943_6_1_1; -.
DR InParanoid; Q9C639; -.
DR OMA; RNLPVWY; -.
DR OrthoDB; 1176893at2759; -.
DR PhylomeDB; Q9C639; -.
DR PRO; PR:Q9C639; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C639; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009782; C:photosystem I antenna complex; IDA:TAIR.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031409; F:pigment binding; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0009768; P:photosynthesis, light harvesting in photosystem I; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009644; P:response to high light intensity; IEP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
DR GO; GO:0009645; P:response to low light intensity stimulus; IEP:UniProtKB.
DR InterPro; IPR001344; Chloro_AB-bd_pln.
DR InterPro; IPR022796; Chloroa_b-bind.
DR PANTHER; PTHR21649; PTHR21649; 1.
DR Pfam; PF00504; Chloroa_b-bind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chlorophyll; Chloroplast; Chromophore;
KW Magnesium; Membrane; Metal-binding; Photosynthesis; Photosystem I; Plastid;
KW Reference proteome; Thylakoid; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..32
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 33..256
FT /note="Photosystem I chlorophyll a/b-binding protein 5,
FT chloroplastic"
FT /id="PRO_0000435449"
FT TRANSMEM 94..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 49
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 69
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 88
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 93
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 147
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 150
FT /ligand="chlorophyll b"
FT /ligand_id="ChEBI:CHEBI:61721"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 205
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 206
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 209
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="4"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 211
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07371"
FT BINDING 223
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="5"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT BINDING 238
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="6"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P12333"
FT MOD_RES 33
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 131
FT /note="S -> C (in Ref. 1; AAD28768)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="L -> I (in Ref. 6; AAM65689)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="Q -> K (in Ref. 6; AAM65689)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 256 AA; 27802 MW; A68A682632C01631 CRC64;
MAVVLRGGIT GGFLHHRRDA SSVITRRISS VKAAGGGINP TVAVERATWL PGLNPPPYLD
GNLAGDYGFD PLGLGEDPES LKWYVQAELV HSRFAMLGVA GILFTDLLRT TGIRNLPVWY
EAGAVKFDFA STKTLIVVQF LLMGFAETKR YMDFVSPGSQ AKEGSFFFGL EAALEGLEPG
YPGGPLLNPL GLAKDVQNAH DWKLKEIKNG RLAMMAMLGF FVQASVTHTG PIDNLVEHLS
NPWHKTIIQT LFTSTS
