DHX30_MOUSE
ID DHX30_MOUSE Reviewed; 1217 AA.
AC Q99PU8; Q3U4Z4; Q3UFA0; Q3UJS4; Q91WA7; Q99KN7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ATP-dependent RNA helicase DHX30 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000269|PubMed:25219788};
DE AltName: Full=DEAH box protein 30;
GN Name=Dhx30; Synonyms=Helg {ECO:0000303|PubMed:25219788};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=CNS;
RX PubMed=25219788; DOI=10.1089/scd.2014.0077;
RA Zheng H.J., Tsukahara M., Liu E., Ye L., Xiong H., Noguchi S., Suzuki K.,
RA Ji Z.S.;
RT "The novel helicase helG (DHX30) is expressed during gastrulation in mice
RT and has a structure similar to a human DExH box helicase.";
RL Stem Cells Dev. 24:372-383(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, DBA/2J, and NOD; TISSUE=Sympathetic ganglion, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Eye, and Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: RNA-dependent helicase (PubMed:25219788). Plays an important
CC role in the assembly of the mitochondrial large ribosomal subunit (By
CC similarity). Required for optimal function of the zinc-finger antiviral
CC protein ZC3HAV1 (By similarity). Associates with mitochondrial DNA (By
CC similarity). Involved in nervous system development and differentiation
CC through its involvement in the up-regulation of a number of genes which
CC are required for neurogenesis, including GSC, NCAM1, neurogenin, and
CC NEUROD (PubMed:25219788). {ECO:0000250|UniProtKB:Q5BJS0,
CC ECO:0000250|UniProtKB:Q7L2E3, ECO:0000269|PubMed:25219788}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:25219788};
CC -!- SUBUNIT: Identified in a complex with TFAM and SSBP1. Interacts (via N-
CC terminus) with ZC3HAV1 (via N-terminal domain) in an RNA-independent
CC manner. Found in a complex with GRSF1, DDX28, FASTKD2 and FASTKD5.
CC {ECO:0000250|UniProtKB:Q5BJS0, ECO:0000250|UniProtKB:Q7L2E3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25219788}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q7L2E3}. Mitochondrion matrix,
CC mitochondrion nucleoid {ECO:0000250|UniProtKB:Q7L2E3}. Note=Localizes
CC to mitochondrial RNA granules found in close proximity to the
CC mitochondrial nucleoids. Relocalizes to stress granules upon heat
CC stress. {ECO:0000250|UniProtKB:Q7L2E3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99PU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99PU8-2; Sequence=VSP_019747;
CC Name=3;
CC IsoId=Q99PU8-3; Sequence=VSP_019746;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, brain, spleen, lung, liver,
CC skeletal muscle, kidney, and testis. Expression is strongest in the
CC testis and brain, while the lowest levels of expression are found in
CC the spleen and lung. {ECO:0000269|PubMed:25219788}.
CC -!- DEVELOPMENTAL STAGE: Detected at low levels of expression at 3.5 and
CC 6.5 days post coitum (dpc). At 7.5 dpc, it is detected in the ectoderm,
CC mesoderm, and ectoplacental cone. By 8.5 dpc, expression is increased,
CC specifically in the central nervous system, neural plate, and neural
CC tube, which remains constant until 10.5 dpc where it decreases. By 11.5
CC to 15.5 dpc, expression is reduced further in the central nervous
CC system. {ECO:0000269|PubMed:25219788}.
CC -!- PTM: [Isoform 3]: Phosphorylated on Ser-15.
CC {ECO:0000250|UniProtKB:Q7L2E3}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; AB047557; BAB32789.1; -; mRNA.
DR EMBL; AK146326; BAE27081.1; -; mRNA.
DR EMBL; AK148778; BAE28661.1; -; mRNA.
DR EMBL; AK153969; BAE32286.1; -; mRNA.
DR EMBL; BC004082; AAH04082.1; -; mRNA.
DR EMBL; BC016202; AAH16202.1; -; mRNA.
DR CCDS; CCDS23560.1; -. [Q99PU8-1]
DR CCDS; CCDS57705.1; -. [Q99PU8-3]
DR CCDS; CCDS57706.1; -. [Q99PU8-2]
DR RefSeq; NP_001239611.1; NM_001252682.1. [Q99PU8-2]
DR RefSeq; NP_001239612.1; NM_001252683.1. [Q99PU8-3]
DR RefSeq; NP_579925.1; NM_133347.2. [Q99PU8-1]
DR RefSeq; XP_006512361.1; XM_006512298.3. [Q99PU8-1]
DR RefSeq; XP_006512362.1; XM_006512299.1. [Q99PU8-1]
DR RefSeq; XP_006512363.1; XM_006512300.1. [Q99PU8-1]
DR RefSeq; XP_006512364.1; XM_006512301.3. [Q99PU8-1]
DR RefSeq; XP_006512366.1; XM_006512303.1. [Q99PU8-2]
DR RefSeq; XP_006512367.1; XM_006512304.1. [Q99PU8-2]
DR RefSeq; XP_006512368.1; XM_006512305.3. [Q99PU8-2]
DR RefSeq; XP_011241331.1; XM_011243029.2. [Q99PU8-1]
DR RefSeq; XP_017169102.1; XM_017313613.1.
DR RefSeq; XP_017169103.1; XM_017313614.1. [Q99PU8-1]
DR AlphaFoldDB; Q99PU8; -.
DR SMR; Q99PU8; -.
DR BioGRID; 215593; 9.
DR IntAct; Q99PU8; 2.
DR MINT; Q99PU8; -.
DR STRING; 10090.ENSMUSP00000062622; -.
DR iPTMnet; Q99PU8; -.
DR PhosphoSitePlus; Q99PU8; -.
DR SwissPalm; Q99PU8; -.
DR EPD; Q99PU8; -.
DR MaxQB; Q99PU8; -.
DR PaxDb; Q99PU8; -.
DR PeptideAtlas; Q99PU8; -.
DR PRIDE; Q99PU8; -.
DR ProteomicsDB; 279650; -. [Q99PU8-1]
DR ProteomicsDB; 279651; -. [Q99PU8-2]
DR ProteomicsDB; 279652; -. [Q99PU8-3]
DR Antibodypedia; 13009; 173 antibodies from 23 providers.
DR DNASU; 72831; -.
DR Ensembl; ENSMUST00000062368; ENSMUSP00000062622; ENSMUSG00000032480. [Q99PU8-3]
DR Ensembl; ENSMUST00000111991; ENSMUSP00000107622; ENSMUSG00000032480. [Q99PU8-2]
DR Ensembl; ENSMUST00000165596; ENSMUSP00000129174; ENSMUSG00000032480. [Q99PU8-1]
DR Ensembl; ENSMUST00000197928; ENSMUSP00000142549; ENSMUSG00000032480. [Q99PU8-2]
DR Ensembl; ENSMUST00000198425; ENSMUSP00000142659; ENSMUSG00000032480. [Q99PU8-1]
DR Ensembl; ENSMUST00000199529; ENSMUSP00000142489; ENSMUSG00000032480. [Q99PU8-2]
DR Ensembl; ENSMUST00000200066; ENSMUSP00000143371; ENSMUSG00000032480. [Q99PU8-2]
DR GeneID; 72831; -.
DR KEGG; mmu:72831; -.
DR UCSC; uc009rtg.2; mouse. [Q99PU8-3]
DR UCSC; uc009rth.2; mouse. [Q99PU8-1]
DR CTD; 22907; -.
DR MGI; MGI:1920081; Dhx30.
DR VEuPathDB; HostDB:ENSMUSG00000032480; -.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000158279; -.
DR InParanoid; Q99PU8; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; Q99PU8; -.
DR TreeFam; TF352030; -.
DR BioGRID-ORCS; 72831; 17 hits in 73 CRISPR screens.
DR ChiTaRS; Dhx30; mouse.
DR PRO; PR:Q99PU8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q99PU8; protein.
DR Bgee; ENSMUSG00000032480; Expressed in rostral migratory stream and 262 other tissues.
DR ExpressionAtlas; Q99PU8; baseline and differential.
DR Genevisible; Q99PU8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0035770; C:ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; IDA:UniProtKB.
DR GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Helicase; Hydrolase;
KW Mitochondrion; Mitochondrion nucleoid; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..1217
FT /note="ATP-dependent RNA helicase DHX30"
FT /id="PRO_0000245539"
FT DOMAIN 76..144
FT /note="DRBM"
FT DOMAIN 467..635
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 677..850
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 176..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 582..585
FT /note="DEAH box"
FT BINDING 480..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L2E3"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L2E3"
FT VAR_SEQ 1..64
FT /note="MVTPVCNSSTWQPKDSSFLSWPEMFSLDSFRKDRTQHRQRQCKLPPPRLPPM
FT CVNPAPGGTITR -> MAAARRLMALAAGVSPRLRPPDPLVASGRQGCSRGFSSSFVRS
FT DGTQEAAEVESEVAPSEPGEGDGSMVN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019746"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019747"
FT CONFLICT 45
FT /note="P -> H (in Ref. 2; BAE27081)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="V -> G (in Ref. 2; BAE27081)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="Q -> E (in Ref. 2; BAE27081)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="R -> C (in Ref. 2; BAE27081)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="E -> D (in Ref. 2; BAE27081)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="L -> M (in Ref. 2; BAE27081)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="D -> G (in Ref. 2; BAE27081)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="R -> W (in Ref. 2; BAE27081/BAE32286)"
FT /evidence="ECO:0000305"
FT CONFLICT 783
FT /note="K -> R (in Ref. 2; BAE27081)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="R -> Q (in Ref. 2; BAE27081)"
FT /evidence="ECO:0000305"
FT CONFLICT 991
FT /note="Y -> H (in Ref. 2; BAE27081)"
FT /evidence="ECO:0000305"
FT CONFLICT 1211
FT /note="M -> V (in Ref. 3; AAH16202)"
FT /evidence="ECO:0000305"
FT MOD_RES Q99PU8-3:15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L2E3"
SQ SEQUENCE 1217 AA; 136668 MW; C6157413C98A1200 CRC64;
MVTPVCNSST WQPKDSSFLS WPEMFSLDSF RKDRTQHRQR QCKLPPPRLP PMCVNPAPGG
TITRASRDLL KEFPQPKNLL NSVIGRALGI SHAKDKLVYV HTNGPKKKKV TLHIKWPKSV
EVEGYGSKKI DAERQAAAAA CQLFKGWGLL GPRNELFDAA KYRVLADRFG SPADSWWRPE
PTMPPTSWRQ LNPENIRPGG PAGLSRSLGR EEEEDEEEEL EEGTIDVTEF LSMTQQDSHN
PLRDSRGGSF EMTDDDSAIR ALTQFPLPKN LLAKVIQIAT SSSTAKNLMQ FHTVGTKTKL
ATLTLLWPCP MTFVAKGRRK AEAENKAAAL ACKKLKSLGL VDRNNEPLTH AMYNLASLRE
LGETQRRPCT IQVPEPILRK IEAFLSHYPV DSSWISPELR LQSDDILPLG KDSGPLSDPI
TGKPYMPLSE AEEVRLSQSL LELWRRRGPI WQEAPQLPVD PHRDTILSAI EQHPVVVISG
DTGCGKTTRI PQLLLERYVT EGRGARCNVI ITQPRRISAV SVAQRVSHEL GPSLRRNVGF
QVRLESKPPA RGGALLFCTV GILLRKLQSN PSLEGVSHVI VDEVHERDVN TDFLLILLKG
LQRLNPALRL VLMSATGDNE RFSRYFGGCP VIKVPGFMYP VKEHYLEDIL AKLGKHQYPH
RHRHHESEDE CALDLDLVTD LVLHIDARGE PGGILCFLPG WQEIKGVQQR LQEALGMHES
KYLILPVHSN IPMMDQKAIF QQPPLGVRKI VLATNIAETS ITVNDIVHVV DSGLHKEERY
DLKTKVSCLE TVWVSRANVI QRRGRAGRCQ SGFAYHLFPR SRLEKMVPFQ VPEILRTPLE
NLVLQAKIHM PEKTAVEFLS KAVDSPNIKA VDEAVILLQE IGVLDQREYL TTLGQRLAHI
STDPRLAKAI VLAAIFRCLH PLLVVVSCLT RDPFSSSLQN RAEVDKVKAL LSHDSGSDHL
AFVRAVAGWE EVLRWQDRTS RENYLEENLL YAPSLRFIHG LIKQFSENIY EAFLVGKPSD
CTLPSAQCNE YSEEEELVKG VLMAGLYPNL IQVRQGKVTR QGKFKPNSVT YRTKSGNILL
HKSTINREAT RLRSRWLTYF MAVKSNGSVF VRDSSQVHPL AVLLLTDGDV HIRDDGRRAT
ISLSDSDLLR LEGDSRTVRL LREFRRALGR MVERSLRSEL AALPLSVQQE HGQLLALLAE
LLRGPCGSFD MRKTADD
