RFC2_HUMAN
ID RFC2_HUMAN Reviewed; 354 AA.
AC P35250; B5BU07; D3DXG3; P32846; Q9BU93;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Replication factor C subunit 2;
DE AltName: Full=Activator 1 40 kDa subunit;
DE Short=A1 40 kDa subunit;
DE AltName: Full=Activator 1 subunit 2;
DE AltName: Full=Replication factor C 40 kDa subunit;
DE Short=RF-C 40 kDa subunit;
DE Short=RFC40;
GN Name=RFC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 232-249.
RX PubMed=1313560; DOI=10.1073/pnas.89.7.2516;
RA Chen M., Pan Z.-Q., Hurwitz J.;
RT "Sequence and expression in Escherichia coli of the 40-kDa subunit of
RT activator 1 (replication factor C) of HeLa cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2516-2520(1992).
RN [2]
RP SEQUENCE REVISION.
RA Hurwitz J.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1), AND POSSIBLE INVOLVEMENT IN WBS.
RX PubMed=11003705; DOI=10.1007/s003350010166;
RA Martindale D.W., Wilson M.D., Wang D., Burke R.D., Chen X., Duronio V.,
RA Koop B.F.;
RT "Comparative genomic sequence analysis of the Williams syndrome region
RT (LIMK1-RFC2) of human chromosome 7q11.23.";
RL Mamm. Genome 11:890-898(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-232.
RG NIEHS SNPs program;
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INTERACTION WITH PRKAR1A.
RX PubMed=15655353;
RA Gupte R.S., Weng Y., Liu L., Lee M.Y.;
RT "The second subunit of the replication factor C complex (RFC40) and the
RT regulatory subunit (RIalpha) of protein kinase A form a protein complex
RT promoting cell survival.";
RL Cell Cycle 4:323-329(2005).
RN [10]
RP INTERACTION WITH DDX11.
RX PubMed=18499658; DOI=10.1074/jbc.m802696200;
RA Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S.,
RA Hurwitz J.;
RT "Studies with the human cohesin establishment factor, ChlR1. Association of
RT ChlR1 with Ctf18-RFC and Fen1.";
RL J. Biol. Chem. 283:20925-20936(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-163 AND LYS-304, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC delta and epsilon requires the action of the accessory proteins
CC proliferating cell nuclear antigen (PCNA) and activator 1. This subunit
CC binds ATP (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can
CC form a complex either with RFC1 or with RAD17. The former interacts
CC with PCNA in the presence of ATP, while the latter has ATPase activity
CC but is not stimulated by PCNA. RFC2 also interacts with PRKAR1A; the
CC complex may be involved in cell survival (PubMed:15655353). Interacts
CC with DDX11 (PubMed:18499658). {ECO:0000269|PubMed:15655353,
CC ECO:0000269|PubMed:18499658}.
CC -!- INTERACTION:
CC P35250; P10644: PRKAR1A; NbExp=7; IntAct=EBI-476409, EBI-476431;
CC P35250; P35251: RFC1; NbExp=4; IntAct=EBI-476409, EBI-476616;
CC P35250; P35249: RFC4; NbExp=8; IntAct=EBI-476409, EBI-476655;
CC P35250-2; O14964: HGS; NbExp=3; IntAct=EBI-12936957, EBI-740220;
CC P35250-2; P25786: PSMA1; NbExp=3; IntAct=EBI-12936957, EBI-359352;
CC P35250-2; Q5VVQ6: YOD1; NbExp=3; IntAct=EBI-12936957, EBI-2510804;
CC P35250-2; Q15915: ZIC1; NbExp=3; IntAct=EBI-12936957, EBI-11963196;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35250-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35250-2; Sequence=VSP_005660;
CC -!- DISEASE: Note=RFC2 is located in the Williams-Beuren syndrome (WBS)
CC critical region. WBS results from a hemizygous deletion of several
CC genes on chromosome 7q11.23, thought to arise as a consequence of
CC unequal crossing over between highly homologous low-copy repeat
CC sequences flanking the deleted region (PubMed:11003705).
CC {ECO:0000269|PubMed:11003705}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rfc2/";
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DR EMBL; M87338; AAB09786.1; -; mRNA.
DR EMBL; AF045555; AAC04860.1; -; Genomic_DNA.
DR EMBL; AF483622; AAL82503.1; -; Genomic_DNA.
DR EMBL; AC005081; AAP22334.1; -; Genomic_DNA.
DR EMBL; AB451243; BAG70057.1; -; mRNA.
DR EMBL; CH471200; EAW69607.1; -; Genomic_DNA.
DR EMBL; CH471200; EAW69608.1; -; Genomic_DNA.
DR EMBL; BC002813; AAH02813.1; -; mRNA.
DR CCDS; CCDS5567.1; -. [P35250-2]
DR CCDS; CCDS5568.1; -. [P35250-1]
DR PIR; A42700; A42700.
DR RefSeq; NP_001265720.1; NM_001278791.1.
DR RefSeq; NP_001265721.1; NM_001278792.1.
DR RefSeq; NP_001265722.1; NM_001278793.1.
DR RefSeq; NP_002905.2; NM_002914.4. [P35250-2]
DR RefSeq; NP_852136.1; NM_181471.2. [P35250-1]
DR PDB; 6VVO; EM; 3.40 A; B=1-354.
DR PDBsum; 6VVO; -.
DR AlphaFoldDB; P35250; -.
DR SMR; P35250; -.
DR BioGRID; 111914; 158.
DR ComplexPortal; CPX-415; DNA replication factor C complex.
DR CORUM; P35250; -.
DR DIP; DIP-34367N; -.
DR IntAct; P35250; 60.
DR MINT; P35250; -.
DR STRING; 9606.ENSP00000055077; -.
DR GlyGen; P35250; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P35250; -.
DR MetOSite; P35250; -.
DR PhosphoSitePlus; P35250; -.
DR BioMuta; RFC2; -.
DR DMDM; 2507300; -.
DR EPD; P35250; -.
DR jPOST; P35250; -.
DR MassIVE; P35250; -.
DR MaxQB; P35250; -.
DR PaxDb; P35250; -.
DR PeptideAtlas; P35250; -.
DR PRIDE; P35250; -.
DR ProteomicsDB; 55014; -. [P35250-1]
DR ProteomicsDB; 55015; -. [P35250-2]
DR Antibodypedia; 14601; 502 antibodies from 33 providers.
DR DNASU; 5982; -.
DR Ensembl; ENST00000055077.8; ENSP00000055077.3; ENSG00000049541.11. [P35250-1]
DR Ensembl; ENST00000352131.7; ENSP00000275627.3; ENSG00000049541.11. [P35250-2]
DR GeneID; 5982; -.
DR KEGG; hsa:5982; -.
DR MANE-Select; ENST00000055077.8; ENSP00000055077.3; NM_181471.3; NP_852136.1.
DR UCSC; uc003uaj.5; human. [P35250-1]
DR CTD; 5982; -.
DR DisGeNET; 5982; -.
DR GeneCards; RFC2; -.
DR HGNC; HGNC:9970; RFC2.
DR HPA; ENSG00000049541; Low tissue specificity.
DR MalaCards; RFC2; -.
DR MIM; 194050; phenotype.
DR MIM; 600404; gene.
DR neXtProt; NX_P35250; -.
DR OpenTargets; ENSG00000049541; -.
DR Orphanet; 904; Williams syndrome.
DR PharmGKB; PA34339; -.
DR VEuPathDB; HostDB:ENSG00000049541; -.
DR eggNOG; KOG0991; Eukaryota.
DR GeneTree; ENSGT00550000075050; -.
DR HOGENOM; CLU_042324_0_1_1; -.
DR InParanoid; P35250; -.
DR OMA; SCNYSSQ; -.
DR OrthoDB; 1071197at2759; -.
DR PhylomeDB; P35250; -.
DR TreeFam; TF300585; -.
DR BRENDA; 3.6.4.B8; 2681.
DR PathwayCommons; P35250; -.
DR Reactome; R-HSA-110312; Translesion synthesis by REV1.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-110320; Translesion Synthesis by POLH.
DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-HSA-5655862; Translesion synthesis by POLK.
DR Reactome; R-HSA-5656121; Translesion synthesis by POLI.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-69091; Polymerase switching.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51.
DR SignaLink; P35250; -.
DR SIGNOR; P35250; -.
DR BioGRID-ORCS; 5982; 701 hits in 1086 CRISPR screens.
DR ChiTaRS; RFC2; human.
DR GeneWiki; RFC2; -.
DR GenomeRNAi; 5982; -.
DR Pharos; P35250; Tbio.
DR PRO; PR:P35250; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P35250; protein.
DR Bgee; ENSG00000049541; Expressed in ventricular zone and 153 other tissues.
DR ExpressionAtlas; P35250; baseline and differential.
DR Genevisible; P35250; HS.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; IDA:UniProtKB.
DR GO; GO:0005663; C:DNA replication factor C complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; TAS:ProtInc.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:GOC.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:UniProtKB.
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; Alternative splicing; ATP-binding;
KW Direct protein sequencing; DNA replication; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Williams-Beuren syndrome.
FT CHAIN 1..354
FT /note="Replication factor C subunit 2"
FT /id="PRO_0000121766"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 163
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 304
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 111..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005660"
FT VARIANT 232
FT /note="A -> V (in dbSNP:rs3135684)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_023126"
FT CONFLICT 244
FT /note="G -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 195..209
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 229..242
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 248..254
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 275..287
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 292..304
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 310..328
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 334..347
FT /evidence="ECO:0007829|PDB:6VVO"
SQ SEQUENCE 354 AA; 39157 MW; B50AC8EEF89F64A9 CRC64;
MEVEAVCGGA GEVEAQDSDP APAFSKAPGS AGHYELPWVE KYRPVKLNEI VGNEDTVSRL
EVFAREGNVP NIIIAGPPGT GKTTSILCLA RALLGPALKD AMLELNASND RGIDVVRNKI
KMFAQQKVTL PKGRHKIIIL DEADSMTDGA QQALRRTMEI YSKTTRFALA CNASDKIIEP
IQSRCAVLRY TKLTDAQILT RLMNVIEKER VPYTDDGLEA IIFTAQGDMR QALNNLQSTF
SGFGFINSEN VFKVCDEPHP LLVKEMIQHC VNANIDEAYK ILAHLWHLGY SPEDIIGNIF
RVCKTFQMAE YLKLEFIKEI GYTHMKIAEG VNSLLQMAGL LARLCQKTMA PVAS
