TF3C4_HUMAN
ID TF3C4_HUMAN Reviewed; 822 AA.
AC Q9UKN8; Q5VZJ7;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=General transcription factor 3C polypeptide 4;
DE EC=2.3.1.48;
DE AltName: Full=TF3C-delta;
DE AltName: Full=Transcription factor IIIC 90 kDa subunit;
DE Short=TFIIIC 90 kDa subunit;
DE Short=TFIIIC90;
DE AltName: Full=Transcription factor IIIC subunit delta;
GN Name=GTF3C4;
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], PROTEIN SEQUENCE OF 139-156; 170-179; 614-626
RP AND 643-659, AND INTERACTION WITH GTF3C1; GTF3C2; GTF3C5; BRF1; POLR3C AND
RP POLR3F.
RX PubMed=10523658; DOI=10.1128/mcb.19.11.7697;
RA Hsieh Y.-J., Kundu T.K., Wang Z., Kovelman R., Roeder R.G.;
RT "The TFIIIC90 subunit of TFIIIC interacts with multiple components of the
RT RNA polymerase III machinery and contains a histone-specific
RT acetyltransferase activity.";
RL Mol. Cell. Biol. 19:7697-7704(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Placenta, 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 [5]
RP IDENTIFICATION IN TFIIIC COMPLEX, AND INTERACTION WITH GTF3C6.
RX PubMed=17409385; DOI=10.1074/jbc.m611542200;
RA Dumay-Odelot H., Marck C., Durrieu-Gaillard S., Lefebvre O., Jourdain S.,
RA Prochazkova M., Pflieger A., Teichmann M.;
RT "Identification, molecular cloning, and characterization of the sixth
RT subunit of human transcription factor TFIIIC.";
RL J. Biol. Chem. 282:17179-17189(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-604; SER-611 AND
RP SER-652, AND 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-225 AND LYS-629, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Essential for RNA polymerase III to make a number of small
CC nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-
CC associated (VA) RNA of both cellular and viral origin. Has histone
CC acetyltransferase activity (HAT) with unique specificity for free and
CC nucleosomal H3. May cooperate with GTF3C5 in facilitating the
CC recruitment of TFIIIB and RNA polymerase through direct interactions
CC with BRF1, POLR3C and POLR3F. May be localized close to the A box.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six
CC subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. Interacts
CC with BRF1, GTF3C1, GTF3C2, GTF3C5, GTF3C6, POLR3C and POLR3F.
CC {ECO:0000269|PubMed:10523658, ECO:0000269|PubMed:17409385}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TFIIIC subunit 4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11619.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF142328; AAF05087.1; -; mRNA.
DR EMBL; AL160165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88011.1; -; Genomic_DNA.
DR EMBL; BC011619; AAH11619.1; ALT_SEQ; mRNA.
DR EMBL; BC094774; AAH94774.1; -; mRNA.
DR EMBL; BC104755; AAI04756.1; -; mRNA.
DR EMBL; BC112245; AAI12246.1; -; mRNA.
DR CCDS; CCDS6953.1; -.
DR RefSeq; NP_036336.2; NM_012204.3.
DR AlphaFoldDB; Q9UKN8; -.
DR BioGRID; 114738; 145.
DR CORUM; Q9UKN8; -.
DR IntAct; Q9UKN8; 45.
DR MINT; Q9UKN8; -.
DR STRING; 9606.ENSP00000361219; -.
DR GlyGen; Q9UKN8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UKN8; -.
DR MetOSite; Q9UKN8; -.
DR PhosphoSitePlus; Q9UKN8; -.
DR SwissPalm; Q9UKN8; -.
DR BioMuta; GTF3C4; -.
DR DMDM; 212276467; -.
DR EPD; Q9UKN8; -.
DR jPOST; Q9UKN8; -.
DR MassIVE; Q9UKN8; -.
DR MaxQB; Q9UKN8; -.
DR PaxDb; Q9UKN8; -.
DR PeptideAtlas; Q9UKN8; -.
DR PRIDE; Q9UKN8; -.
DR ProteomicsDB; 84826; -.
DR Antibodypedia; 31705; 216 antibodies from 27 providers.
DR DNASU; 9329; -.
DR Ensembl; ENST00000372146.5; ENSP00000361219.4; ENSG00000125484.12.
DR GeneID; 9329; -.
DR KEGG; hsa:9329; -.
DR MANE-Select; ENST00000372146.5; ENSP00000361219.4; NM_012204.4; NP_036336.2.
DR UCSC; uc010mzv.4; human.
DR CTD; 9329; -.
DR GeneCards; GTF3C4; -.
DR HGNC; HGNC:4667; GTF3C4.
DR HPA; ENSG00000125484; Low tissue specificity.
DR MIM; 604892; gene.
DR neXtProt; NX_Q9UKN8; -.
DR OpenTargets; ENSG00000125484; -.
DR PharmGKB; PA29055; -.
DR VEuPathDB; HostDB:ENSG00000125484; -.
DR eggNOG; ENOG502QTDJ; Eukaryota.
DR GeneTree; ENSGT00390000011873; -.
DR HOGENOM; CLU_018536_0_0_1; -.
DR InParanoid; Q9UKN8; -.
DR OMA; WKPSHED; -.
DR OrthoDB; 966939at2759; -.
DR PhylomeDB; Q9UKN8; -.
DR TreeFam; TF328412; -.
DR BRENDA; 2.3.1.48; 2681.
DR PathwayCommons; Q9UKN8; -.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR SignaLink; Q9UKN8; -.
DR SIGNOR; Q9UKN8; -.
DR BioGRID-ORCS; 9329; 524 hits in 1101 CRISPR screens.
DR ChiTaRS; GTF3C4; human.
DR GeneWiki; GTF3C4; -.
DR GenomeRNAi; 9329; -.
DR Pharos; Q9UKN8; Tdark.
DR PRO; PR:Q9UKN8; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9UKN8; protein.
DR Bgee; ENSG00000125484; Expressed in ventricular zone and 178 other tissues.
DR ExpressionAtlas; Q9UKN8; baseline and differential.
DR Genevisible; Q9UKN8; HS.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:HGNC-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0004402; F:histone acetyltransferase activity; TAS:ProtInc.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IDA:GO_Central.
DR GO; GO:0042791; P:5S class rRNA transcription by RNA polymerase III; IC:HGNC-UCL.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IC:HGNC-UCL.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; TAS:ProtInc.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IC:HGNC-UCL.
DR InterPro; IPR045803; DUF5921.
DR InterPro; IPR044230; GTF3C4.
DR InterPro; IPR024761; TFIIIC_delta_N.
DR InterPro; IPR024764; TFIIIC_Znf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15496; PTHR15496; 1.
DR Pfam; PF19336; DUF5921; 1.
DR Pfam; PF12657; TFIIIC_delta; 1.
DR Pfam; PF12660; zf-TFIIIC; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transferase; Ubl conjugation.
FT CHAIN 1..822
FT /note="General transcription factor 3C polypeptide 4"
FT /id="PRO_0000209713"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 629
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 268
FT /note="C -> S (in Ref. 1; AAF05087)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="C -> R (in Ref. 1; AAF05087)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="V -> L (in Ref. 1; AAF05087)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="L -> V (in Ref. 1; AAF05087)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="S -> K (in Ref. 1; AAF05087)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="R -> P (in Ref. 1; AAF05087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 822 AA; 91982 MW; 2546A1E7D87F563C CRC64;
MNTADQARVG PADDGPAPSG EEEGEGGGEA GGKEPAADAA PGPSAAFRLM VTRREPAVKL
QYAVSGLEPL AWSEDHRVSV STARSIAVLE LICDVHNPGQ DLVIHRTSVP APLNSCLLKV
GSKTEVAECK EKFAASKDPT VSQTFMLDRV FNPEGKALPP MRGFKYTSWS PMGCDANGRC
LLAALTMDNR LTIQANLNRL QWVQLVDLTE IYGERLYETS YRLSKNEAPE GNLGDFAEFQ
RRHSMQTPVR MEWSGICTTQ QVKHNNECRD VGSVLLAVLF ENGNIAVWQF QLPFVGKESI
SSCNTIESGI TSPSVLFWWE YEHNNRKMSG LIVGSAFGPI KILPVNLKAV KGYFTLRQPV
ILWKEMDQLP VHSIKCVPLY HPYQKCSCSL VVAARGSYVF WCLLLISKAG LNVHNSHVTG
LHSLPIVSMT ADKQNGTVYT CSSDGKVRQL IPIFTDVALK FEHQLIKLSD VFGSVRTHGI
AVSPCGAYLA IITTEGMING LHPVNKNYQV QFVTLKTFEE AAAQLLESSV QNLFKQVDLI
DLVRWKILKD KHIPQFLQEA LEKKIESSGV TYFWRFKLFL LRILYQSMQK TPSEALWKPT
HEDSKILLVD SPGMGNADDE QQEEGTSSKQ VVKQGLQERS KEGDVEEPTD DSLPTTGDAG
GREPMEEKLL EIQGKIEAVE MHLTREHMKR VLGEVYLHTW ITENTSIPTR GLCNFLMSDE
EYDDRTARVL IGHISKKMNK QTFPEHCSLC KEILPFTDRK QAVCSNGHIW LRCFLTYQSC
QSLIYRRCLL HDSIARHPAP EDPDWIKRLL QSPCPFCDSP VF
