RFC3_YEAST
ID RFC3_YEAST Reviewed; 340 AA.
AC P38629; D6W0Q3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Replication factor C subunit 3;
DE Short=Replication factor C3;
DE AltName: Full=Activator 1 40 kDa subunit;
GN Name=RFC3; OrderedLocusNames=YNL290W; ORFNames=N0533;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8302859; DOI=10.1073/pnas.91.3.868;
RA Li X., Burgers P.M.J.;
RT "Molecular cloning and expression of the Saccharomyces cerevisiae RFC3
RT gene, an essential component of replication factor C.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:868-872(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION IN THE RFC COMPLEX.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7651383; DOI=10.1128/mcb.15.9.4661;
RA Cullmann G., Fien K., Kobayashi R., Stillman B.;
RT "Characterization of the five replication factor C genes of Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 15:4661-4671(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8553702; DOI=10.1002/yea.320111311;
RA Maurer K.C.T., Urbanus J.H.M., Planta R.J.;
RT "Sequence analysis of a 30 kb DNA segment from yeast chromosome XIV
RT carrying a ribosomal protein gene cluster, the genes encoding a plasma
RT membrane protein and a subunit of replication factor C, and a novel
RT putative serine/threonine protein kinase gene.";
RL Yeast 11:1303-1310(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP INTERACTION WITH RAD24, AND IDENTIFICATION IN THE RAD24-RFC COMPLEX.
RX PubMed=10660302; DOI=10.1016/s0960-9822(99)00263-8;
RA Green C.M., Erdjument-Bromage H., Tempst P., Lowndes N.F.;
RT "A novel Rad24 checkpoint protein complex closely related to replication
RT factor C.";
RL Curr. Biol. 10:39-42(2000).
RN [7]
RP IDENTIFICATION IN THE CTF18-RFC COMPLEX.
RX PubMed=11389843; DOI=10.1016/s1097-2765(01)00254-4;
RA Mayer M.L., Gygi S.P., Aebersold R., Hieter P.;
RT "Identification of RFC(Ctf18p, Ctf8p, Dcc1p): an alternative RFC complex
RT required for sister chromatid cohesion in S. cerevisiae.";
RL Mol. Cell 7:959-970(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH CTF18.
RX PubMed=11486023; DOI=10.1128/mcb.21.17.5838-5845.2001;
RA Naiki T., Kondo T., Nakada D., Matsumoto K., Sugimoto K.;
RT "Chl12 (Ctf18) forms a novel replication factor C-related complex and
RT functions redundantly with Rad24 in the DNA replication checkpoint
RT pathway.";
RL Mol. Cell. Biol. 21:5838-5845(2001).
RN [9]
RP FUNCTION, AND INTERACTION WITH POL30.
RX PubMed=14530260; DOI=10.1074/jbc.m309206200;
RA Yao N., Coryell L., Zhang D., Georgescu R.E., Finkelstein J., Coman M.M.,
RA Hingorani M.M., O'Donnell M.;
RT "Replication factor C clamp loader subunit arrangement within the circular
RT pentamer and its attachment points to proliferating cell nuclear antigen.";
RL J. Biol. Chem. 278:50744-50753(2003).
RN [10]
RP INTERACTION WITH ECO1.
RX PubMed=12665596; DOI=10.1128/mcb.23.8.2999-3007.2003;
RA Kenna M.A., Skibbens R.V.;
RT "Mechanical link between cohesion establishment and DNA replication:
RT Ctf7p/Eco1p, a cohesion establishment factor, associates with three
RT different replication factor C complexes.";
RL Mol. Cell. Biol. 23:2999-3007(2003).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP IDENTIFICATION IN THE RAD24-RFC COMPLEX, AND FUNCTION OF THE RAD24-RFC
RP COMPLEX.
RX PubMed=12604797; DOI=10.1073/pnas.0437148100;
RA Majka J., Burgers P.M.J.;
RT "Yeast Rad17/Mec3/Ddc1: a sliding clamp for the DNA damage checkpoint.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2249-2254(2003).
RN [13]
RP IDENTIFICATION IN THE RFC COMPLEX, IDENTIFICATION IN THE RAD24-RFC COMPLEX,
RP IDENTIFICATION IN THE ELG1-RFC COMPLEX, IDENTIFICATION IN THE CTF18-RFC
RP COMPLEX, AND FUNCTION OF THE CTF18-RFC COMPLEX.
RX PubMed=15964801; DOI=10.1128/mcb.25.13.5445-5455.2005;
RA Bylund G.O., Burgers P.M.;
RT "Replication protein A-directed unloading of PCNA by the Ctf18 cohesion
RT establishment complex.";
RL Mol. Cell. Biol. 25:5445-5455(2005).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH AN ATP ANALOG; RCF1;
RP RCF2; RCF4; RCF5 AND PCNA.
RX PubMed=15201901; DOI=10.1038/nature02585;
RA Bowman G.D., O'Donnell M., Kuriyan J.;
RT "Structural analysis of a eukaryotic sliding DNA clamp-clamp loader
RT complex.";
RL Nature 429:724-730(2004).
CC -!- FUNCTION: Component of ATP-dependent clamp loader (RFC and RFC-like)
CC complexes for DNA clamps, such as the POL30/PCNA homotrimer and the
CC checkpoint clamp DDC1:MEC3:RAD17 complex. During a clamp loading
CC circle, the RFC:clamp complex binds to DNA and the recognition of the
CC double-stranded/single-stranded junction stimulates ATP hydrolysis by
CC RFC. The complex presumably provides bipartite ATP sites in which one
CC subunit supplies a catalytic site for hydrolysis of ATP bound to the
CC neighboring subunit. Dissociation of RFC from the clamp leaves the
CC clamp encircling DNA. Component of the replication factor C (RFC or
CC activator 1) complex which loads POL30/PCNA and acts during elongation
CC of primed DNA templates by DNA polymerase delta and epsilon. RFC has an
CC essential but redundant activity in sister chromatid cohesion
CC establishment. Component of the RFC-like complex CTF18-RFC which is
CC required for efficient establishment of chromosome cohesion during S-
CC phase and may load or unload POL30/PCNA. Component of the RFC-like
CC RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17
CC complex and is involved in DNA repair pathways. Component of the RFC-
CC like ELG1-RFC complex which appears to have a role in DNA replication,
CC replication fork re-start, recombination and repair. RFC3 supplies a
CC catalytic site to the ATP site of RFC4. {ECO:0000269|PubMed:11486023,
CC ECO:0000269|PubMed:12604797, ECO:0000269|PubMed:14530260,
CC ECO:0000269|PubMed:15964801}.
CC -!- SUBUNIT: Replication factor C (RFC) is a heteropentamer of subunits
CC RFC1, RFC2, RFC3, RFC4 and RFC5 and forms a complex with POL30/PCNA in
CC the presence of ATP. Component of the RAD24-RFC complex which consists
CC of RAD14, RFC2, RFC3, RFC4 and RFC5 and associates with the checkpoint
CC clamp DDC1:MEC3:RAD17 complex. Component of the ELG1-RFC complex which
CC consists of ELG1, RFC2, RFC3, RFC4 and RFC5. Component of the CTF18-RFC
CC complex, which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and
CC RFC5. RFC3 interacts with ECO1 and POL30/PCNA.
CC {ECO:0000269|PubMed:10660302, ECO:0000269|PubMed:11389843,
CC ECO:0000269|PubMed:11486023, ECO:0000269|PubMed:12604797,
CC ECO:0000269|PubMed:12665596, ECO:0000269|PubMed:14530260,
CC ECO:0000269|PubMed:15201901, ECO:0000269|PubMed:15964801,
CC ECO:0000269|PubMed:7651383}.
CC -!- INTERACTION:
CC P38629; P49956: CTF18; NbExp=3; IntAct=EBI-15000, EBI-4560;
CC P38629; P38877: CTF8; NbExp=2; IntAct=EBI-15000, EBI-5216;
CC P38629; P32641: RAD24; NbExp=5; IntAct=EBI-15000, EBI-14675;
CC P38629; P40348: RFC2; NbExp=4; IntAct=EBI-15000, EBI-14992;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 3140 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000305}.
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DR EMBL; L18755; AAA34969.1; -; Genomic_DNA.
DR EMBL; U26029; AAC49062.1; -; Genomic_DNA.
DR EMBL; U23084; AAC49110.1; -; Genomic_DNA.
DR EMBL; Z71566; CAA96207.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10269.1; -; Genomic_DNA.
DR PIR; A36988; A36988.
DR RefSeq; NP_014109.1; NM_001183128.1.
DR PDB; 1SXJ; X-ray; 2.85 A; C=1-340.
DR PDB; 7SGZ; EM; 3.17 A; C=1-340.
DR PDB; 7SH2; EM; 3.23 A; C=1-340.
DR PDB; 7ST9; EM; 2.20 A; C=1-340.
DR PDB; 7STB; EM; 2.72 A; C=1-340.
DR PDB; 7STE; EM; 2.73 A; C=1-339.
DR PDB; 7THJ; EM; 3.80 A; C=1-340.
DR PDB; 7THV; EM; 4.00 A; C=1-340.
DR PDB; 7TI8; EM; 3.50 A; C=1-340.
DR PDB; 7TIB; EM; 3.40 A; C=1-340.
DR PDB; 7TIC; EM; 3.90 A; C=1-340.
DR PDB; 7TID; EM; 3.30 A; C=1-340.
DR PDB; 7TKU; EM; 4.00 A; C=1-340.
DR PDBsum; 1SXJ; -.
DR PDBsum; 7SGZ; -.
DR PDBsum; 7SH2; -.
DR PDBsum; 7ST9; -.
DR PDBsum; 7STB; -.
DR PDBsum; 7STE; -.
DR PDBsum; 7THJ; -.
DR PDBsum; 7THV; -.
DR PDBsum; 7TI8; -.
DR PDBsum; 7TIB; -.
DR PDBsum; 7TIC; -.
DR PDBsum; 7TID; -.
DR PDBsum; 7TKU; -.
DR AlphaFoldDB; P38629; -.
DR SMR; P38629; -.
DR BioGRID; 35547; 123.
DR ComplexPortal; CPX-1731; CTF18-RFC complex.
DR ComplexPortal; CPX-1807; Rad17 RFC-like complex.
DR ComplexPortal; CPX-422; ELG1-RFC complex.
DR ComplexPortal; CPX-545; DNA replication factor C complex.
DR DIP; DIP-2529N; -.
DR IntAct; P38629; 40.
DR MINT; P38629; -.
DR STRING; 4932.YNL290W; -.
DR iPTMnet; P38629; -.
DR MaxQB; P38629; -.
DR PaxDb; P38629; -.
DR PRIDE; P38629; -.
DR EnsemblFungi; YNL290W_mRNA; YNL290W; YNL290W.
DR GeneID; 855426; -.
DR KEGG; sce:YNL290W; -.
DR SGD; S000005234; RFC3.
DR VEuPathDB; FungiDB:YNL290W; -.
DR eggNOG; KOG0990; Eukaryota.
DR GeneTree; ENSGT00550000075072; -.
DR HOGENOM; CLU_042324_2_0_1; -.
DR InParanoid; P38629; -.
DR OMA; TRTIFCG; -.
DR BioCyc; YEAST:G3O-33280-MON; -.
DR Reactome; R-SCE-110312; Translesion synthesis by REV1.
DR Reactome; R-SCE-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SCE-110320; Translesion Synthesis by POLH.
DR Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SCE-5655862; Translesion synthesis by POLK.
DR Reactome; R-SCE-5656121; Translesion synthesis by POLI.
DR Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-SCE-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-69091; Polymerase switching.
DR EvolutionaryTrace; P38629; -.
DR PRO; PR:P38629; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P38629; protein.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; IPI:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005663; C:DNA replication factor C complex; IDA:SGD.
DR GO; GO:0031391; C:Elg1 RFC-like complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031389; C:Rad17 RFC-like complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0090618; P:DNA clamp unloading; IDA:ComplexPortal.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IC:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:ComplexPortal.
DR GO; GO:0006272; P:leading strand elongation; IDA:SGD.
DR GO; GO:0006298; P:mismatch repair; TAS:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IC:ComplexPortal.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013748; Rep_factorC_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell cycle; DNA replication;
KW DNA-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..340
FT /note="Replication factor C subunit 3"
FT /id="PRO_0000121756"
FT BINDING 16..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 53..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 171..183
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 212..218
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 229..235
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 241..252
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 274..285
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 293..310
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 316..330
FT /evidence="ECO:0007829|PDB:1SXJ"
SQ SEQUENCE 340 AA; 38204 MW; 0170EDABAB5CEA52 CRC64;
MSTSTEKRSK ENLPWVEKYR PETLDEVYGQ NEVITTVRKF VDEGKLPHLL FYGPPGTGKT
STIVALAREI YGKNYSNMVL ELNASDDRGI DVVRNQIKDF ASTRQIFSKG FKLIILDEAD
AMTNAAQNAL RRVIERYTKN TRFCVLANYA HKLTPALLSR CTRFRFQPLP QEAIERRIAN
VLVHEKLKLS PNAEKALIEL SNGDMRRVLN VLQSCKATLD NPDEDEISDD VIYECCGAPR
PSDLKAVLKS ILEDDWGTAH YTLNKVRSAK GLALIDLIEG IVKILEDYEL QNEETRVHLL
TKLADIEYSI SKGGNDQIQG SAVIGAIKAS FENETVKANV
