RFC2_YEAST
ID RFC2_YEAST Reviewed; 353 AA.
AC P40348; D6VWN9; E9P8U1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Replication factor C subunit 2;
DE Short=Replication factor C2;
DE AltName: Full=Activator 1 41 kDa subunit;
GN Name=RFC2; OrderedLocusNames=YJR068W; ORFNames=J1808;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8202350; DOI=10.1093/nar/22.9.1527;
RA Noskov V., Maki S., Kawasaki Y., Leem S.-H., Ono B., Araki H., Pavlov Y.,
RA Sugino A.;
RT "The RFC2 gene encoding a subunit of replication factor C of Saccharomyces
RT cerevisiae.";
RL Nucleic Acids Res. 22:1527-1535(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 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
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 [8]
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 [9]
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 [10]
RP INTERACTION WITH ELG1.
RX PubMed=12912927; DOI=10.1093/emboj/cdg406;
RA Bellaoui M., Chang M., Ou J., Xu H., Boone C., Brown G.W.;
RT "Elg1 forms an alternative RFC complex important for DNA replication and
RT genome integrity.";
RL EMBO J. 22:4304-4313(2003).
RN [11]
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 [12]
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 [13]
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 [14]
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH AN ATP ANALOG; RCF1;
RP RCF3; 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. RFC2 binds ATP and
CC single-stranded DNA. {ECO:0000269|PubMed:11486023,
CC ECO:0000269|PubMed:12604797, 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. RFC2 interacts with ECO1. {ECO:0000269|PubMed:10660302,
CC ECO:0000269|PubMed:11389843, ECO:0000269|PubMed:11486023,
CC ECO:0000269|PubMed:12604797, ECO:0000269|PubMed:12665596,
CC ECO:0000269|PubMed:12912927, ECO:0000269|PubMed:15201901,
CC ECO:0000269|PubMed:15964801, ECO:0000269|PubMed:7651383}.
CC -!- INTERACTION:
CC P40348; P49956: CTF18; NbExp=2; IntAct=EBI-14992, EBI-4560;
CC P40348; P38877: CTF8; NbExp=2; IntAct=EBI-14992, EBI-5216;
CC P40348; Q12050: ELG1; NbExp=2; IntAct=EBI-14992, EBI-32195;
CC P40348; P32641: RAD24; NbExp=5; IntAct=EBI-14992, EBI-14675;
CC P40348; P38629: RFC3; NbExp=4; IntAct=EBI-14992, EBI-15000;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 4610 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; D28499; BAA05858.1; -; Genomic_DNA.
DR EMBL; U26028; AAC49061.1; -; Genomic_DNA.
DR EMBL; Z49568; CAA89596.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39294.1; -; Genomic_DNA.
DR EMBL; AY557920; AAS56246.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08855.1; -; Genomic_DNA.
DR PIR; S45531; S45531.
DR RefSeq; NP_012602.3; NM_001181726.3.
DR PDB; 1SXJ; X-ray; 2.85 A; D=1-353.
DR PDB; 7SGZ; EM; 3.17 A; D=1-353.
DR PDB; 7SH2; EM; 3.23 A; D=1-353.
DR PDB; 7ST9; EM; 2.20 A; D=1-353.
DR PDB; 7STB; EM; 2.72 A; D=1-353.
DR PDB; 7STE; EM; 2.73 A; D=1-353.
DR PDB; 7THJ; EM; 3.80 A; D=1-353.
DR PDB; 7THV; EM; 4.00 A; D=1-353.
DR PDB; 7TI8; EM; 3.50 A; D=1-353.
DR PDB; 7TIB; EM; 3.40 A; D=1-353.
DR PDB; 7TIC; EM; 3.90 A; D=1-353.
DR PDB; 7TID; EM; 3.30 A; D=1-353.
DR PDB; 7TKU; EM; 4.00 A; D=1-353.
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; P40348; -.
DR SMR; P40348; -.
DR BioGRID; 33825; 365.
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-2528N; -.
DR IntAct; P40348; 53.
DR MINT; P40348; -.
DR STRING; 4932.YJR068W; -.
DR iPTMnet; P40348; -.
DR MaxQB; P40348; -.
DR PaxDb; P40348; -.
DR PRIDE; P40348; -.
DR EnsemblFungi; YJR068W_mRNA; YJR068W; YJR068W.
DR GeneID; 853531; -.
DR KEGG; sce:YJR068W; -.
DR SGD; S000003829; RFC2.
DR VEuPathDB; FungiDB:YJR068W; -.
DR eggNOG; KOG0989; Eukaryota.
DR GeneTree; ENSGT00550000074917; -.
DR HOGENOM; CLU_042324_1_0_1; -.
DR InParanoid; P40348; -.
DR OMA; AHSTRFC; -.
DR BioCyc; YEAST:G3O-31701-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; P40348; -.
DR PRO; PR:P40348; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P40348; protein.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; IPI: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; IEA:InterPro.
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:0000076; P:DNA replication checkpoint signaling; IMP:SGD.
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 GO; GO:0007062; P:sister chromatid cohesion; IPI:SGD.
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 CHAIN 1..353
FT /note="Replication factor C subunit 2"
FT /id="PRO_0000121760"
FT BINDING 28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 65..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CONFLICT 12
FT /note="K -> R (in Ref. 6; AAS56246)"
FT /evidence="ECO:0000305"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 71..88
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 280..292
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 316..333
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 339..352
FT /evidence="ECO:0007829|PDB:1SXJ"
SQ SEQUENCE 353 AA; 39742 MW; 59B2C4223B0D13BF CRC64;
MFEGFGPNKK RKISKLAAEQ SLAQQPWVEK YRPKNLDEVT AQDHAVTVLK KTLKSANLPH
MLFYGPPGTG KTSTILALTK ELYGPDLMKS RILELNASDE RGISIVREKV KNFARLTVSK
PSKHDLENYP CPPYKIIILD EADSMTADAQ SALRRTMETY SGVTRFCLIC NYVTRIIDPL
ASRCSKFRFK ALDASNAIDR LRFISEQENV KCDDGVLERI LDISAGDLRR GITLLQSASK
GAQYLGDGKN ITSTQVEELA GVVPHDILIE IVEKVKSGDF DEIKKYVNTF MKSGWSAASV
VNQLHEYYIT NDNFDTNFKN QISWLLFTTD SRLNNGTNEH IQLLNLLVKI SQL
