CSOS2_HALNC
ID CSOS2_HALNC Reviewed; 869 AA.
AC O85041; D0KZ90;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Carboxysome assembly protein CsoS2B {ECO:0000303|PubMed:25826651};
DE AltName: Full=Carboxysome shell protein CsoS2B;
GN Name=csoS2 {ECO:0000303|PubMed:9696760}; OrderedLocusNames=Hneap_0920;
OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS neapolitanus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Halothiobacillaceae; Halothiobacillus.
OX NCBI_TaxID=555778;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23641 / c2;
RX PubMed=9696760; DOI=10.1128/jb.180.16.4133-4139.1998;
RA Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.;
RT "Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate
RT carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in
RT expression of form II RuBisCO, loss of carboxysomes, and an increased CO2
RT requirement for growth.";
RL J. Bacteriol. 180:4133-4139(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23641 / c2;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Kerfeld C., Cannon G., Heinhort S.;
RT "Complete sequence of Halothiobacillus neapolitanus c2.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-18, SUBCELLULAR LOCATION, TWO PROTEIN FORMS, AND
RP PUTATIVE GLYCOSYLATION.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=10525740; DOI=10.1007/s002030050765;
RA Baker S.H., Lorbach S.C., Rodriguez-Buey M., Williams D.S., Aldrich H.C.,
RA Shively J.M.;
RT "The correlation of the gene csoS2 of the carboxysome operon with two
RT polypeptides of the carboxysome in Thiobacillus neapolitanus.";
RL Arch. Microbiol. 172:233-239(1999).
RN [4]
RP FUNCTION, PROTEIN ABUNDANCE, AND SUBCELLULAR LOCATION.
RX DOI=10.1007/7171_023;
RA Heinhorst S., Cannon G.C., Shively J.M.;
RT "Carboxysomes and Carboxysome-like Inclusions.";
RL (In) Shively J.M. (eds.);
RL Microbiology Monographs, pp.2:141-164, Springer-Verlag, Berlin (2006).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=18258595; DOI=10.1074/jbc.m709285200;
RA Dou Z., Heinhorst S., Williams E.B., Murin C.D., Shively J.M., Cannon G.C.;
RT "CO2 fixation kinetics of Halothiobacillus neapolitanus mutant carboxysomes
RT lacking carbonic anhydrase suggest the shell acts as a diffusional barrier
RT for CO2.";
RL J. Biol. Chem. 283:10377-10384(2008).
RN [6]
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=22184212; DOI=10.1073/pnas.1108557109;
RA Bonacci W., Teng P.K., Afonso B., Niederholtmeyer H., Grob P., Silver P.A.,
RA Savage D.F.;
RT "Modularity of a carbon-fixing protein organelle.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:478-483(2012).
RN [7]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, TWO PROTEIN FORMS, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=25826651; DOI=10.3390/life5021141;
RA Cai F., Dou Z., Bernstein S.L., Leverenz R., Williams E.B., Heinhorst S.,
RA Shively J., Cannon G.C., Kerfeld C.A.;
RT "Advances in Understanding Carboxysome Assembly in Prochlorococcus and
RT Synechococcus Implicate CsoS2 as a Critical Component.";
RL Life 5:1141-1171(2015).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, RIBOSOMAL FRAMESHIFT, ISOFORMS CSOS2A AND
RP CSOS2B, DOMAIN, AND MASS SPECTROMETRY.
RX PubMed=26608811; DOI=10.1016/j.jmb.2015.11.017;
RA Chaijarasphong T., Nichols R.J., Kortright K.E., Nixon C.F., Teng P.K.,
RA Oltrogge L.M., Savage D.F.;
RT "Programmed Ribosomal Frameshifting Mediates Expression of the alpha-
RT Carboxysome.";
RL J. Mol. Biol. 428:153-164(2016).
RN [9]
RP INTERACTION WITH CBBS, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=30305640; DOI=10.1038/s41598-018-33074-x;
RA Liu Y., He X., Lim W., Mueller J., Lawrie J., Kramer L., Guo J., Niu W.;
RT "Deciphering molecular details in the assembly of alpha-type carboxysome.";
RL Sci. Rep. 8:15062-15062(2018).
RN [10]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=31406332; DOI=10.1038/s41564-019-0520-8;
RA Desmarais J.J., Flamholz A.I., Blikstad C., Dugan E.J., Laughlin T.G.,
RA Oltrogge L.M., Chen A.W., Wetmore K., Diamond S., Wang J.Y., Savage D.F.;
RT "DABs are inorganic carbon pumps found throughout prokaryotic phyla.";
RL Nat. Microbiol. 4:2204-2215(2019).
RN [11]
RP FUNCTION, INTERACTION WITH RUBISCO, DOMAIN, AND MUTAGENESIS OF
RP 18-LYS--ARG-25; 93-ARG--ARG-100; 174-ARG--ARG-181 AND 220-ARG--ARG-227.
RX PubMed=32123388; DOI=10.1038/s41594-020-0387-7;
RA Oltrogge L.M., Chaijarasphong T., Chen A.W., Bolin E.R., Marqusee S.,
RA Savage D.F.;
RT "Multivalent interactions between CsoS2 and Rubisco mediate alpha-
RT carboxysome formation.";
RL Nat. Struct. Mol. Biol. 27:281-287(2020).
RN [12]
RP FUNCTION IN ASSEMBLY, DOMAIN, DISRUPTION PHENOTYPE, BIOTECHNOLOGY,
RP ENCAPSULATION SIGNAL, AND MUTAGENESIS OF 839-PRO--GLY-869.
RX PubMed=33116131; DOI=10.1038/s41467-020-19280-0;
RA Li T., Jiang Q., Huang J., Aitchison C.M., Huang F., Yang M., Dykes G.F.,
RA He H.L., Wang Q., Sprick R.S., Cooper A.I., Liu L.N.;
RT "Reprogramming bacterial protein organelles as a nanoreactor for hydrogen
RT production.";
RL Nat. Commun. 11:5448-5448(2020).
CC -!- FUNCTION: Required for alpha-carboxysome (Cb) assembly, mediates
CC interaction between RuBisCO and the Cb shell (PubMed:25826651,
CC PubMed:32123388) (Probable). The 3 C-terminal repeats act as the
CC encapsulation signal to target proteins to the Cb; they are necessary
CC and sufficient to target both CsoS2 and foreign proteins to the Cb
CC (PubMed:33116131). The N-terminal repeats of this (probably)
CC intrinsically disordered protein bind simultaneously to both subunits
CC of RuBisCO; minimally 2 N-repeats are necessary for RuBisCO assembly
CC into the Cb in vivo. Probably also interacts with the major shell
CC proteins (CsoS1); that interaction would increase the local
CC concentration of CsoS2 so that it can condense RuBisCO and full
CC carboxysomes can be formed (PubMed:32123388). The long form is
CC essential for Cb formation while the short form is not
CC (PubMed:26608811). There are estimated to be 143 CsoS2A and 186 CsoS2B
CC proteins per Cb (Ref.4). {ECO:0000269|PubMed:25826651,
CC ECO:0000269|PubMed:26608811, ECO:0000269|PubMed:32123388,
CC ECO:0000269|PubMed:33116131, ECO:0000269|Ref.4,
CC ECO:0000305|PubMed:33116131}.
CC -!- FUNCTION: Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form
CC without cargo protein. CsoS2 is essential for Cb formation and is also
CC capable of targeting foreign proteins to the Cb. The Cb shell assembles
CC with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of
CC the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms
CC pseudohexamers that probably control metabolite flux into and out of
CC the shell. {ECO:0000269|PubMed:25826651, ECO:0000269|PubMed:26608811,
CC ECO:0000269|PubMed:32123388, ECO:0000269|PubMed:33116131}.
CC -!- SUBUNIT: Probably interacts with the carboxysome (Cb) major shell
CC protein CsoS1; this complex probably also interacts with RuBisCO
CC (Probable). Interacts with CbbS (the small subunit of RuBisCO) but not
CC the large subunit (CbbL) (PubMed:30305640). RuBisCO interacts with the
CC N-terminal repeats of this protein; mutating the third and tenth basic
CC residue of each N-repeat prevents binding. Binding is sensitive to
CC ionic strength. A fusion of a single N-terminal repeat to the C-
CC terminus of the large subunit of RuBisCO (cbbL) shows the repeat can
CC lie between a CbbL dimer, making minor contacts to CbbS; thus each
CC RuBisCO holoenzyme could bind 8 repeats. At least 2 N-repeats are
CC required for RuBisCO assembly into the Cb (PubMed:32123388).
CC {ECO:0000269|PubMed:30305640, ECO:0000269|PubMed:32123388,
CC ECO:0000305|PubMed:25826651}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:10525740,
CC ECO:0000269|PubMed:18258595, ECO:0000269|PubMed:25826651,
CC ECO:0000269|PubMed:26608811}. Note=Immunogold staining shows this is a
CC shell protein (PubMed:10525740). C-terminally tagged protein
CC immunoprecipitates whole carboxysomes, showing the C-terminus is on the
CC exterior (PubMed:25826651). This bacterium makes alpha-type
CC carboxysomes (Ref.4, PubMed:18258595). {ECO:0000269|PubMed:10525740,
CC ECO:0000269|PubMed:18258595, ECO:0000269|PubMed:25826651,
CC ECO:0000269|Ref.4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=The production of the two protein products from this region
CC is due to programmed -1 ribosomal frameshifting. In vivo about half
CC the protein product is frameshifted. {ECO:0000269|PubMed:26608811,
CC ECO:0000305|PubMed:10525740, ECO:0000305|PubMed:25826651};
CC Name=CsoS2B;
CC IsoId=O85041-1; Sequence=Displayed;
CC Name=CsoS2A;
CC IsoId=O85041-2; Sequence=VSP_060905, VSP_060906;
CC -!- DOMAIN: Has 3 domains; the N-terminal domain has 4 short repeats and
CC binds RuBisCO. The central region has 6 longer repeats (Probable)
CC (PubMed:32123388). The C-terminal domain has 3 repeats and a highly
CC conserved C-terminal peptide (Probable). The 3 C-repeats serve as the
CC encapsulation signal for the alpha-carboxysome (Cb), and are able to
CC target foreign proteins to this organelle. Proteins can be targeted to
CC the Cb by a single C-repeat, however more repeats yields more efficient
CC targeting. The C-terminal peptide (CTP) is not required for cargo
CC targeting and is probably on the outside of the Cb (PubMed:33116131,
CC PubMed:25826651). {ECO:0000269|PubMed:25826651,
CC ECO:0000269|PubMed:32123388, ECO:0000269|PubMed:33116131,
CC ECO:0000305|PubMed:25826651, ECO:0000305|PubMed:26608811}.
CC -!- PTM: Seen in gels as 2 forms (of 85 and 130 kDa, equal amounts of each)
CC which have the same N-terminus, called respectively CsoS2A and CsoS2B
CC (PubMed:10525740). Partial tryptic digestion and mass spectrometric
CC analysis, as well as the presence of the shorter form even when a C-
CC terminally tagged version is engineered, suggests CsoS2A is shorter at
CC the C-terminus, but its sequence is not known (Probable). It has been
CC shown these 2 forms are produced by ribosomal frameshifting
CC (PubMed:26608811). {ECO:0000269|PubMed:10525740,
CC ECO:0000269|PubMed:26608811, ECO:0000305|PubMed:25826651}.
CC -!- MASS SPECTROMETRY: Mass=92.3; Method=MALDI; Note=Expressed in E.coli,
CC CsoS2B (full-length) form.; Evidence={ECO:0000269|PubMed:26608811};
CC -!- MASS SPECTROMETRY: Mass=60.8; Method=MALDI; Note=Expressed in E.coli,
CC CsoS2A (short) form.; Evidence={ECO:0000269|PubMed:26608811};
CC -!- DISRUPTION PHENOTYPE: Does not grow in air but does grow in 2% CO(2),
CC called a high-CO(2) requiring phenotype, hcr. Cells do not make
CC carboxysomes (PubMed:25826651). Also absolutely required for
CC carboxysome formation in E.coli (PubMed:33116131). Required for growth
CC in ambient air (PubMed:31406332). {ECO:0000269|PubMed:25826651,
CC ECO:0000269|PubMed:31406332, ECO:0000269|PubMed:33116131}.
CC -!- BIOTECHNOLOGY: Expression of 10 genes for alpha-carboxysome (Cb)
CC proteins (cbbL-cbbS-csoS2-csoS3-csoS4A-csoS4B-csoS1C-csoS1A-csoS1B-
CC csoS1D) in E.coli generates compartments that resemble Cb, contain
CC RuBisCO and have its catalytic activity, showing it is possible to make
CC artificial, functional Cb using these 10 genes. Cargo proteins can be
CC targeted to these organelles (PubMed:22184212, PubMed:30305640).
CC Artificial Cb assembly in E.coli requires csoS2-csoS4A-csoS4B-csoS1C-
CC csoS1A-csoS1B-csoS1D (but not the gene for carbonic anhydrase, csoS3).
CC Targeting proteins to the organelle requires at least one of the CsoS2
CC C-repeats; 3 repeats gives the best localization. A nanoreactor of the
CC Cb shell proteins has been engineered which generates H(2) using a
CC ferredoxin-hydrogenase fusion (AC P07839-Q9FYU1) and a
CC flavodoxin/ferredoxin--NADP reductase (AC A0A0K3QZA5) targeted
CC separately to the Cb; the hydrogenase has first to be matured and
CC activated by HydGXEF (AC Q8EAH9, Q8EAH8, Q8EAH7 and Q8EAH6
CC respectively). Encapsulation increases H(2) production about 20% during
CC anaerobic growth, and over 4-fold more during aerobic growth
CC (PubMed:33116131). {ECO:0000269|PubMed:22184212,
CC ECO:0000269|PubMed:30305640, ECO:0000269|PubMed:33116131}.
CC -!- SIMILARITY: Belongs to the CsoS2 family. {ECO:0000305}.
CC -!- CAUTION: Both Cso2A and Cso2B were originally thought to be
CC glycosylated (PubMed:10525740). Later experiments do not show any
CC evidence of glycosylation (PubMed:26608811).
CC {ECO:0000269|PubMed:10525740, ECO:0000269|PubMed:26608811}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACX95763.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF038430; AAC32551.1; -; Genomic_DNA.
DR EMBL; CP001801; ACX95763.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; O85041; -.
DR STRING; 555778.Hneap_0920; -.
DR EnsemblBacteria; ACX95763; ACX95763; Hneap_0920.
DR KEGG; hna:Hneap_0920; -.
DR eggNOG; ENOG502Z8T4; Bacteria.
DR HOGENOM; CLU_016451_0_0_6; -.
DR Proteomes; UP000009102; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0043886; F:structural constituent of carboxysome; IEA:InterPro.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR InterPro; IPR020990; CSOS2.
DR Pfam; PF12288; CsoS2_M; 3.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Carbon dioxide fixation; Carboxysome;
KW Direct protein sequencing; Reference proteome; Repeat;
KW Ribosomal frameshifting.
FT CHAIN 1..869
FT /note="Carboxysome assembly protein CsoS2B"
FT /id="PRO_0000452067"
FT REPEAT 16..35
FT /note="N-repeat 1"
FT /evidence="ECO:0000269|PubMed:25826651,
FT ECO:0000269|PubMed:32123388"
FT REPEAT 91..110
FT /note="N-repeat 2"
FT /evidence="ECO:0000269|PubMed:25826651,
FT ECO:0000269|PubMed:32123388"
FT REPEAT 172..191
FT /note="N-repeat 3"
FT /evidence="ECO:0000269|PubMed:25826651,
FT ECO:0000269|PubMed:32123388"
FT REPEAT 218..237
FT /note="N-repeat 4"
FT /evidence="ECO:0000269|PubMed:25826651,
FT ECO:0000269|PubMed:32123388"
FT REPEAT 260..309
FT /note="M-repeat 1"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 319..368
FT /note="M-repeat 2"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 379..419
FT /note="M-repeat 3"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 435..484
FT /note="M-repeat 4"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 494..539
FT /note="M-repeat 5"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 545..594
FT /note="M-repeat 6"
FT /evidence="ECO:0000269|PubMed:25826651"
FT REPEAT 604..651
FT /note="C-repeat 1"
FT /evidence="ECO:0000269|PubMed:26608811"
FT REPEAT 690..730
FT /note="C-repeat 2"
FT /evidence="ECO:0000269|PubMed:26608811"
FT REPEAT 773..813
FT /note="C-repeat 3"
FT /evidence="ECO:0000269|PubMed:26608811"
FT REGION 1..259
FT /note="N-terminal domain"
FT /evidence="ECO:0000305|PubMed:25826651,
FT ECO:0000305|PubMed:32123388"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..603
FT /note="Middle region"
FT /evidence="ECO:0000305|PubMed:25826651,
FT ECO:0000305|PubMed:32123388"
FT REGION 556..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..838
FT /note="C-terminal domain"
FT /evidence="ECO:0000305|PubMed:25826651,
FT ECO:0000305|PubMed:32123388"
FT REGION 831..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..869
FT /note="C-terminal peptide (CTP)"
FT /evidence="ECO:0000305|PubMed:26608811,
FT ECO:0000305|PubMed:32123388"
FT COMPBIAS 33..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 568..571
FT /note="MSGD -> DVR (in isoform CsoS2A)"
FT /id="VSP_060905"
FT VAR_SEQ 572..869
FT /note="Missing (in isoform CsoS2A)"
FT /id="VSP_060906"
FT MUTAGEN 18..25
FT /note="KELARARR->AELARARA: Prevents RuBisCO binding; when
FT associated with all 4 N-repeat mutations."
FT /evidence="ECO:0000269|PubMed:32123388"
FT MUTAGEN 93..100
FT /note="RDLCRQRR->ADLCRQRA: Prevents RuBisCO binding; when
FT associated with all 4 N-repeat mutations."
FT /evidence="ECO:0000269|PubMed:32123388"
FT MUTAGEN 174..181
FT /note="RDICRARR->ADICRARA: Prevents RuBisCO binding; when
FT associated with all 4 N-repeat mutations."
FT /evidence="ECO:0000269|PubMed:32123388"
FT MUTAGEN 220..227
FT /note="RDAAKRHR->ADAAKRHA: Prevents RuBisCO binding; when
FT associated with all 4 N-repeat mutations."
FT /evidence="ECO:0000269|PubMed:32123388"
FT MUTAGEN 839..869
FT /note="Missing: Forms normal carboxysomes (in artificial
FT E.coli carboxysomes)."
FT /evidence="ECO:0000269|PubMed:33116131"
FT CONFLICT 111..114
FT /note="AKTT -> VKTN (in Ref. 2; ACX95763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 869 AA; 91934 MW; A2C48415DDF7589C CRC64;
MPSQSGMNPA DLSGLSGKEL ARARRAALSK QGKAAVSNKT ASVNRSTKQA ASSINTNQVR
SSVNEVPTDY QMADQLCSTI DHADFGTESN RVRDLCRQRR EALSTIGKKA AKTTGKPSGR
VRPQQSVVHN DAMIENAGDT NQSSSTSLNN ELSEICSIAD DMPERFGSQA KTVRDICRAR
RQALSERGTR AVPPKPQSQG GPGRNGYQID GYLDTALHGR DAAKRHREML CQYGRGTAPS
CKPTGRVKNS VQSGNAAPKK VETGHTLSGG SVTGTQVDRK SHVTGNEPGT CRAVTGTEYV
GTEQFTSFCN TSPKPNATKV NVTTTARGRP VSGTEVSRTE KVTGNESGVC RNVTGTEYMS
NEAHFSLCGT AAKPSQADKV MFGATARTHQ VVSGSDEFRP SSVTGNESGA KRTITGSQYA
DEGLARLTIN GAPAKVARTH TFAGSDVTGT EIGRSTRVTG DESGSCRSIS GTEYLSNEQF
QSFCDTKPQR SPFKVGQDRT NKGQSVTGNL VDRSELVTGN EPGSCSRVTG SQYGQSKICG
GGVGKVRSMR TLRGTSVSGQ QLDHAPKMSG DERGGCMPVT GNEYYGREHF EPFCTSTPEP
EAQSTEQSLT CEGQIISGTS VDASDLVTGN EIGEQQLISG DAYVGAQQTG CLPTSPRFNQ
TGNVQSMGFK NTNQPEQNFA PGEVMPTDFS IQTPARSAQN RITGNDIAPS GRITGPGMLA
TGLITGTPEF RHAARELVGS PQPMAMAMAN RNKAAQAPVV QPEVVATQEK PELVCAPRSD
QMDRVSGEGK ERCHITGDDW SVNKHITGTA GQWASGRNPS MRGNARVVET SAFANRNVPK
PEKPGSKITG SSGNDTQGSL ITYSGGARG
