RPA12_YEAST
ID RPA12_YEAST Reviewed; 125 AA.
AC P32529; D6VWN4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA12;
DE AltName: Full=A12;
DE AltName: Full=A12.2;
DE AltName: Full=DNA-directed RNA polymerase I 13.7 kDa polypeptide;
GN Name=RPA12; Synonyms=RRN4; OrderedLocusNames=YJR063W; ORFNames=J1747;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8417319; DOI=10.1128/mcb.13.1.114-122.1993;
RA Nogi Y., Yano R., Dodd J., Carles C., Nomura M.;
RT "Gene RRN4 in Saccharomyces cerevisiae encodes the A12.2 subunit of RNA
RT polymerase I and is essential only at high temperatures.";
RL Mol. Cell. Biol. 13:114-122(1993).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP ELECTRON MICROSCOPY OF THE RNA POLYMERASE I COMPLEX.
RX PubMed=12145213; DOI=10.1093/emboj/cdf392;
RA Bischler N., Brino L., Carles C., Riva M., Tschochner H., Mallouh V.,
RA Schultz P.;
RT "Localization of the yeast RNA polymerase I-specific subunits.";
RL EMBO J. 21:4136-4144(2002).
RN [8]
RP IDENTIFICATION IN THE RNA POL I COMPLEX, SUBCELLULAR LOCATION, INTERACTION
RP WITH RPA2, AND MUTAGENESIS OF CYS-10; CYS-13; CYS-30 AND CYS-33.
RX PubMed=11918799; DOI=10.1046/j.1365-2958.2002.02824.x;
RA Van Mullem V., Landrieux E., Vandenhaute J., Thuriaux P.;
RT "Rpa12p, a conserved RNA polymerase I subunit with two functional
RT domains.";
RL Mol. Microbiol. 43:1105-1113(2002).
RN [9]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=12407181; DOI=10.1073/pnas.232580799;
RA Peyroche G., Levillain E., Siaut M., Callebaut I., Schultz P., Sentenac A.,
RA Riva M., Carles C.;
RT "The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship
RT to Rpb4-Rpb7 pol II subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14670-14675(2002).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(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 FUNCTION.
RX PubMed=15073335; DOI=10.1073/pnas.0401393101;
RA Prescott E.M., Osheim Y.N., Jones H.S., Alen C.M., Roan J.G., Reeder R.H.,
RA Beyer A.L., Proudfoot N.J.;
RT "Transcriptional termination by RNA polymerase I requires the small subunit
RT Rpa12p.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6068-6073(2004).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF THE POL I COMPLEX,
RP FUNCTION IN RNA CLEAVAGE, REGION, AND SUBUNIT.
RX PubMed=18160037; DOI=10.1016/j.cell.2007.10.051;
RA Kuhn C.D., Geiger S.R., Baumli S., Gartmann M., Gerber J., Jennebach S.,
RA Mielke T., Tschochner H., Beckmann R., Cramer P.;
RT "Functional architecture of RNA polymerase I.";
RL Cell 131:1260-1272(2007).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX IN COMPLEX WITH
RP ZINC IONS, FUNCTION, ZINC-BINDING, SUBUNIT, AND ZINC FINGER DOMAIN.
RX PubMed=24153184; DOI=10.1038/nature12636;
RA Fernandez-Tornero C., Moreno-Morcillo M., Rashid U.J., Taylor N.M.,
RA Ruiz F.M., Gruene T., Legrand P., Steuerwald U., Muller C.W.;
RT "Crystal structure of the 14-subunit RNA polymerase I.";
RL Nature 502:644-649(2013).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE POL I COMPLEX IN COMPLEX WITH
RP ZINC IONS, FUNCTION, ZINC-BINDING, SUBUNIT, AND ZINC FINGER DOMAIN.
RX PubMed=24153182; DOI=10.1038/nature12712;
RA Engel C., Sainsbury S., Cheung A.C., Kostrewa D., Cramer P.;
RT "RNA polymerase I structure and transcription regulation.";
RL Nature 502:650-655(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA
CC precursors. Besides, RNA polymerase I has intrinsic RNA cleavage
CC activity. Proposed to contribute to the polymerase catalytic activity
CC and form the polymerase active center together with the two largest
CC subunits. Subunit RPA12 contributes a catalytic zinc ribbon that is
CC required for RNA cleavage by Pol I. Involved in transcriptional
CC termination. {ECO:0000269|PubMed:15073335, ECO:0000269|PubMed:18160037,
CC ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:24153184}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8,
CC RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of
CC a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5,
CC RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and
CC RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43
CC form the stalk that mediates interactions with transcription initiation
CC factors and newly synthesized RNA. Interacts with RPA2/RPA135.
CC Peripheral subunit that binds the catalytic zinc ion that is required
CC for RNA cleavage. The heterodimer formed by RPA34 and RPA49 stabilizes
CC subunit RPA12 and stimulates RPA12-dependent RNA cleavage. Involved in
CC the recruitment of RPA49 to Pol I. {ECO:0000269|PubMed:11918799,
CC ECO:0000269|PubMed:12407181, ECO:0000269|PubMed:18160037,
CC ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:24153184}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11918799,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 8450 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000305}.
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DR EMBL; L00708; AAA34992.1; -; Genomic_DNA.
DR EMBL; L35564; AAB59319.1; -; Genomic_DNA.
DR EMBL; Z49563; CAA89591.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39289.1; -; Genomic_DNA.
DR EMBL; AY558313; AAS56639.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08850.1; -; Genomic_DNA.
DR PIR; A48107; A48107.
DR RefSeq; NP_012597.1; NM_001181721.1.
DR PDB; 4C2M; X-ray; 2.80 A; I/X=1-125.
DR PDB; 4C3H; X-ray; 3.27 A; I=1-125.
DR PDB; 4C3I; X-ray; 3.00 A; I=1-125.
DR PDB; 4C3J; X-ray; 3.35 A; I=1-125.
DR PDB; 4YM7; X-ray; 5.50 A; AI/BI/CI/DI/EI/FI=1-125.
DR PDB; 5G5L; EM; 4.80 A; I=1-125.
DR PDB; 5LMX; EM; 4.90 A; I=1-125.
DR PDB; 5M3F; EM; 3.80 A; I=1-125.
DR PDB; 5M3M; EM; 4.00 A; I=1-125.
DR PDB; 5M5W; EM; 3.80 A; I=1-125.
DR PDB; 5M5X; EM; 4.00 A; I=1-125.
DR PDB; 5M5Y; EM; 4.00 A; I=1-125.
DR PDB; 5M64; EM; 4.60 A; I=1-125.
DR PDB; 5N5Y; EM; 7.70 A; I=1-125.
DR PDB; 5N5Z; EM; 7.70 A; I=1-125.
DR PDB; 5N60; EM; 7.70 A; I=1-125.
DR PDB; 5N61; EM; 3.40 A; I=1-125.
DR PDB; 5OA1; EM; 4.40 A; I=1-125.
DR PDB; 5W5Y; EM; 3.80 A; I=1-125.
DR PDB; 5W64; EM; 4.20 A; I=1-125.
DR PDB; 5W65; EM; 4.30 A; I=1-125.
DR PDB; 5W66; EM; 3.90 A; I=1-125.
DR PDB; 6H67; EM; 3.60 A; I=1-125.
DR PDB; 6H68; EM; 4.60 A; I=1-125.
DR PDB; 6HKO; EM; 3.42 A; I=1-125.
DR PDB; 6HLQ; EM; 3.18 A; I=1-125.
DR PDB; 6HLR; EM; 3.18 A; I=1-125.
DR PDB; 6HLS; EM; 3.21 A; I=1-125.
DR PDB; 6RQH; EM; 3.70 A; I=1-125.
DR PDB; 6RQL; EM; 2.90 A; I=1-125.
DR PDB; 6RQT; EM; 4.00 A; I=1-125.
DR PDB; 6RRD; EM; 3.10 A; I=1-125.
DR PDB; 6RUI; EM; 2.70 A; I=1-125.
DR PDB; 6RUO; EM; 3.50 A; I=1-125.
DR PDB; 6RWE; EM; 3.00 A; I=1-125.
DR PDB; 6TPS; EM; 3.54 A; I=1-125.
DR PDBsum; 4C2M; -.
DR PDBsum; 4C3H; -.
DR PDBsum; 4C3I; -.
DR PDBsum; 4C3J; -.
DR PDBsum; 4YM7; -.
DR PDBsum; 5G5L; -.
DR PDBsum; 5LMX; -.
DR PDBsum; 5M3F; -.
DR PDBsum; 5M3M; -.
DR PDBsum; 5M5W; -.
DR PDBsum; 5M5X; -.
DR PDBsum; 5M5Y; -.
DR PDBsum; 5M64; -.
DR PDBsum; 5N5Y; -.
DR PDBsum; 5N5Z; -.
DR PDBsum; 5N60; -.
DR PDBsum; 5N61; -.
DR PDBsum; 5OA1; -.
DR PDBsum; 5W5Y; -.
DR PDBsum; 5W64; -.
DR PDBsum; 5W65; -.
DR PDBsum; 5W66; -.
DR PDBsum; 6H67; -.
DR PDBsum; 6H68; -.
DR PDBsum; 6HKO; -.
DR PDBsum; 6HLQ; -.
DR PDBsum; 6HLR; -.
DR PDBsum; 6HLS; -.
DR PDBsum; 6RQH; -.
DR PDBsum; 6RQL; -.
DR PDBsum; 6RQT; -.
DR PDBsum; 6RRD; -.
DR PDBsum; 6RUI; -.
DR PDBsum; 6RUO; -.
DR PDBsum; 6RWE; -.
DR PDBsum; 6TPS; -.
DR AlphaFoldDB; P32529; -.
DR SMR; P32529; -.
DR BioGRID; 33820; 72.
DR ComplexPortal; CPX-1664; DNA-directed RNA Polymerase I complex.
DR DIP; DIP-236N; -.
DR IntAct; P32529; 27.
DR MINT; P32529; -.
DR STRING; 4932.YJR063W; -.
DR iPTMnet; P32529; -.
DR MaxQB; P32529; -.
DR PaxDb; P32529; -.
DR PRIDE; P32529; -.
DR EnsemblFungi; YJR063W_mRNA; YJR063W; YJR063W.
DR GeneID; 853526; -.
DR KEGG; sce:YJR063W; -.
DR SGD; S000003824; RPA12.
DR VEuPathDB; FungiDB:YJR063W; -.
DR eggNOG; KOG2907; Eukaryota.
DR GeneTree; ENSGT00390000008126; -.
DR HOGENOM; CLU_093932_1_1_1; -.
DR InParanoid; P32529; -.
DR OMA; EMQYHTL; -.
DR BioCyc; YEAST:G3O-31696-MON; -.
DR Reactome; R-SCE-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR PRO; PR:P32529; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P32529; protein.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0001054; F:RNA polymerase I activity; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006379; P:mRNA cleavage; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:ComplexPortal.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IDA:ComplexPortal.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:ComplexPortal.
DR CDD; cd10507; Zn-ribbon_RPA12; 1.
DR InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR InterPro; IPR034004; Zn_ribbon_RPA12_C.
DR InterPro; IPR001222; Znf_TFIIS.
DR PANTHER; PTHR11239; PTHR11239; 1.
DR Pfam; PF02150; RNA_POL_M_15KD; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR SMART; SM00661; RPOL9; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-directed RNA polymerase;
KW Metal-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW Transcription; Zinc; Zinc-finger.
FT CHAIN 1..125
FT /note="DNA-directed RNA polymerase I subunit RPA12"
FT /id="PRO_0000121465"
FT ZN_FING 10..33
FT /note="C4-type"
FT ZN_FING 82..122
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:24153184"
FT REGION 1..69
FT /note="Necessary and sufficient for recruitment into Pol I"
FT REGION 1..60
FT /note="Interaction with RPA2"
FT /evidence="ECO:0000269|PubMed:11918799"
FT REGION 79..125
FT /note="Required for RNA cleavage, but not essential for
FT elongation activity"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT MUTAGEN 10
FT /note="C->S: Severe growth defect."
FT /evidence="ECO:0000269|PubMed:11918799"
FT MUTAGEN 13
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:11918799"
FT MUTAGEN 30
FT /note="C->S: Limited growth defect."
FT /evidence="ECO:0000269|PubMed:11918799"
FT MUTAGEN 33
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:11918799"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:4C2M"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6RWE"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6RUO"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:4C2M"
SQ SEQUENCE 125 AA; 13661 MW; D79372070819987C CRC64;
MSVVGSLIFC LDCGDLLENP NAVLGSNVEC SQCKAIYPKS QFSNLKVVTT TADDAFPSSL
RAKKSVVKTS LKKNELKDGA TIKEKCPQCG NEEMNYHTLQ LRSADEGATV FYTCTSCGYK
FRTNN
