RFC4_HUMAN
ID RFC4_HUMAN Reviewed; 363 AA.
AC P35249; B4DM41; D3DNV2; Q6FHX7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Replication factor C subunit 4;
DE AltName: Full=Activator 1 37 kDa subunit;
DE Short=A1 37 kDa subunit;
DE AltName: Full=Activator 1 subunit 4;
DE AltName: Full=Replication factor C 37 kDa subunit;
DE Short=RF-C 37 kDa subunit;
DE Short=RFC37;
GN Name=RFC4;
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 PARTIAL PROTEIN SEQUENCE.
RX PubMed=1351677; DOI=10.1073/pnas.89.12.5211;
RA Chen M., Pan Z.-Q., Hurwitz J.;
RT "Studies of the cloned 37-kDa subunit of activator 1 (replication factor C)
RT of HeLa cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5211-5215(1992).
RN [2]
RP SEQUENCE REVISION.
RA Hurwitz J.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-292.
RG NIEHS SNPs program;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
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 1).
RC TISSUE=Lung, and Testis;
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 RAD17.
RX PubMed=11572977; DOI=10.1073/pnas.201373498;
RA Lindsey-Boltz L.A., Bermudez V.P., Hurwitz J., Sancar A.;
RT "Purification and characterization of human DNA damage checkpoint Rad
RT complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11236-11241(2001).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-13, AND IDENTIFICATION
RP 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 [11]
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 [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] SER-354.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 may be involved in the elongation of the multiprimed DNA template.
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. Interacts with CNTD1; this interaction
CC facilitates crossover formation (By similarity).
CC {ECO:0000250|UniProtKB:Q99J62, ECO:0000269|PubMed:11572977}.
CC -!- INTERACTION:
CC P35249; P35250: RFC2; NbExp=8; IntAct=EBI-476655, EBI-476409;
CC P35249; P40938: RFC3; NbExp=11; IntAct=EBI-476655, EBI-1055010;
CC P35249; P40937: RFC5; NbExp=22; IntAct=EBI-476655, EBI-712376;
CC P35249; Q9H4P4: RNF41; NbExp=7; IntAct=EBI-476655, EBI-2130266;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35249-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35249-2; Sequence=VSP_055862, VSP_055863;
CC -!- MISCELLANEOUS: Despite of the presence of a putative ATP-binding motif,
CC this protein does not bind ATP.
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/rfc4/";
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DR EMBL; M87339; AAB09785.1; -; mRNA.
DR EMBL; AF538718; AAM97933.1; -; Genomic_DNA.
DR EMBL; BT006987; AAP35633.1; -; mRNA.
DR EMBL; AK297282; BAG59753.1; -; mRNA.
DR EMBL; CR536561; CAG38798.1; -; mRNA.
DR EMBL; CH471052; EAW78169.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78170.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78171.1; -; Genomic_DNA.
DR EMBL; BC017452; AAH17452.1; -; mRNA.
DR EMBL; BC024022; AAH24022.1; -; mRNA.
DR CCDS; CCDS3283.1; -. [P35249-1]
DR PIR; A45253; A45253.
DR RefSeq; NP_002907.1; NM_002916.3. [P35249-1]
DR RefSeq; NP_853551.1; NM_181573.2. [P35249-1]
DR PDB; 6VVO; EM; 3.40 A; D=1-363.
DR PDBsum; 6VVO; -.
DR AlphaFoldDB; P35249; -.
DR SMR; P35249; -.
DR BioGRID; 111916; 160.
DR ComplexPortal; CPX-415; DNA replication factor C complex.
DR CORUM; P35249; -.
DR DIP; DIP-24267N; -.
DR IntAct; P35249; 61.
DR MINT; P35249; -.
DR STRING; 9606.ENSP00000376272; -.
DR GlyGen; P35249; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P35249; -.
DR PhosphoSitePlus; P35249; -.
DR BioMuta; RFC4; -.
DR DMDM; 1703052; -.
DR EPD; P35249; -.
DR jPOST; P35249; -.
DR MassIVE; P35249; -.
DR MaxQB; P35249; -.
DR PaxDb; P35249; -.
DR PeptideAtlas; P35249; -.
DR PRIDE; P35249; -.
DR ProteomicsDB; 55013; -. [P35249-1]
DR Antibodypedia; 3877; 293 antibodies from 33 providers.
DR DNASU; 5984; -.
DR Ensembl; ENST00000296273.7; ENSP00000296273.2; ENSG00000163918.12. [P35249-1]
DR Ensembl; ENST00000392481.6; ENSP00000376272.2; ENSG00000163918.12. [P35249-1]
DR GeneID; 5984; -.
DR KEGG; hsa:5984; -.
DR MANE-Select; ENST00000296273.7; ENSP00000296273.2; NM_002916.5; NP_002907.1.
DR UCSC; uc003fqz.4; human. [P35249-1]
DR CTD; 5984; -.
DR DisGeNET; 5984; -.
DR GeneCards; RFC4; -.
DR HGNC; HGNC:9972; RFC4.
DR HPA; ENSG00000163918; Low tissue specificity.
DR MIM; 102577; gene.
DR neXtProt; NX_P35249; -.
DR OpenTargets; ENSG00000163918; -.
DR PharmGKB; PA34341; -.
DR VEuPathDB; HostDB:ENSG00000163918; -.
DR eggNOG; KOG0989; Eukaryota.
DR GeneTree; ENSGT00550000074917; -.
DR InParanoid; P35249; -.
DR OMA; KIVMVFS; -.
DR OrthoDB; 1071197at2759; -.
DR PhylomeDB; P35249; -.
DR TreeFam; TF314424; -.
DR BRENDA; 3.6.4.B8; 2681.
DR PathwayCommons; P35249; -.
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; P35249; -.
DR SIGNOR; P35249; -.
DR BioGRID-ORCS; 5984; 687 hits in 1088 CRISPR screens.
DR ChiTaRS; RFC4; human.
DR GeneWiki; RFC4; -.
DR GenomeRNAi; 5984; -.
DR Pharos; P35249; Tbio.
DR PRO; PR:P35249; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P35249; protein.
DR Bgee; ENSG00000163918; Expressed in ventricular zone and 189 other tissues.
DR ExpressionAtlas; P35249; baseline and differential.
DR Genevisible; P35249; 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:0031391; C:Elg1 RFC-like complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:InterPro.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:GOC.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:ProtInc.
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 Reference proteome.
FT CHAIN 1..363
FT /note="Replication factor C subunit 4"
FT /id="PRO_0000121757"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78..85
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:22814378"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 269..303
FT /note="IPAEKIDGVFAACQSGSFDKLEAVVKDLIDEGHAA -> RVLDILNFFLVGF
FT FVAFRKFSSNKYWVFSKCQVLH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055862"
FT VAR_SEQ 304..363
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055863"
FT VARIANT 292
FT /note="V -> A (in dbSNP:rs2066497)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_014307"
FT VARIANT 354
FT /note="T -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036121"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 238..247
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 248..254
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 259..265
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 286..298
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 303..315
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 321..339
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 344..359
FT /evidence="ECO:0007829|PDB:6VVO"
SQ SEQUENCE 363 AA; 39682 MW; 6FEAB3794379F3E0 CRC64;
MQAFLKGTSI STKPPLTKDR GVAASAGSSG ENKKAKPVPW VEKYRPKCVD EVAFQEEVVA
VLKKSLEGAD LPNLLFYGPP GTGKTSTILA AARELFGPEL FRLRVLELNA SDERGIQVVR
EKVKNFAQLT VSGSRSDGKP CPPFKIVILD EADSMTSAAQ AALRRTMEKE SKTTRFCLIC
NYVSRIIEPL TSRCSKFRFK PLSDKIQQQR LLDIAKKENV KISDEGIAYL VKVSEGDLRK
AITFLQSATR LTGGKEITEK VITDIAGVIP AEKIDGVFAA CQSGSFDKLE AVVKDLIDEG
HAATQLVNQL HDVVVENNLS DKQKSIITEK LAEVDKCLAD GADEHLQLIS LCATVMQQLS
QNC
