ADPPT_MOUSE
ID ADPPT_MOUSE Reviewed; 309 AA.
AC Q9CQF6; Q5U5W8; Q9CU40; Q9D827;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase;
DE EC=2.7.8.7 {ECO:0000250|UniProtKB:Q9NRN7};
DE AltName: Full=4'-phosphopantetheinyl transferase;
DE AltName: Full=Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase;
DE Short=AASD-PPT;
GN Name=Aasdhppt;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Embryo, Lung, Medulla oblongata, Pancreas, Small intestine, and
RC Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, 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: Catalyzes the post-translational modification of target
CC proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine
CC moiety from coenzyme A, regardless of whether the CoA is presented in
CC the free thiol form or as an acetyl thioester, to a serine residue of a
CC broad range of acceptors including the acyl carrier domain of FASN.
CC {ECO:0000250|UniProtKB:Q9NRN7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-
CC [ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7;
CC Evidence={ECO:0000250|UniProtKB:Q9NRN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12069;
CC Evidence={ECO:0000250|UniProtKB:Q9NRN7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + apo-[ACP] = acetyl-[ACP] + adenosine 3',5'-
CC bisphosphate + H(+); Xref=Rhea:RHEA:46564, Rhea:RHEA-COMP:9621,
CC Rhea:RHEA-COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:58343, ChEBI:CHEBI:78446;
CC Evidence={ECO:0000250|UniProtKB:Q9NRN7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46565;
CC Evidence={ECO:0000250|UniProtKB:Q9NRN7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9NRN7};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:Q9NRN7};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NRN7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9NRN7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CQF6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CQF6-2; Sequence=VSP_016096;
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.
CC {ECO:0000305}.
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DR EMBL; AK007737; BAB25224.1; -; mRNA.
DR EMBL; AK008554; BAB25740.1; -; mRNA.
DR EMBL; AK010557; BAB27026.1; -; mRNA.
DR EMBL; AK013111; BAB28656.1; -; mRNA.
DR EMBL; AK018191; BAB31116.1; -; mRNA.
DR EMBL; AK076099; BAC36182.1; -; mRNA.
DR EMBL; AK076866; BAC36512.1; -; mRNA.
DR EMBL; AK144671; BAE26000.1; -; mRNA.
DR EMBL; BC038013; AAH38013.1; -; mRNA.
DR EMBL; BC049851; AAH49851.1; -; mRNA.
DR CCDS; CCDS22794.1; -. [Q9CQF6-1]
DR RefSeq; NP_001313288.1; NM_001326359.1. [Q9CQF6-2]
DR RefSeq; NP_080552.3; NM_026276.3. [Q9CQF6-1]
DR AlphaFoldDB; Q9CQF6; -.
DR SMR; Q9CQF6; -.
DR BioGRID; 212313; 6.
DR STRING; 10090.ENSMUSP00000053971; -.
DR iPTMnet; Q9CQF6; -.
DR PhosphoSitePlus; Q9CQF6; -.
DR EPD; Q9CQF6; -.
DR MaxQB; Q9CQF6; -.
DR PaxDb; Q9CQF6; -.
DR PeptideAtlas; Q9CQF6; -.
DR PRIDE; Q9CQF6; -.
DR ProteomicsDB; 281939; -. [Q9CQF6-1]
DR ProteomicsDB; 281940; -. [Q9CQF6-2]
DR Antibodypedia; 18138; 221 antibodies from 26 providers.
DR DNASU; 67618; -.
DR Ensembl; ENSMUST00000051589; ENSMUSP00000053971; ENSMUSG00000025894. [Q9CQF6-1]
DR GeneID; 67618; -.
DR KEGG; mmu:67618; -.
DR UCSC; uc009obe.2; mouse. [Q9CQF6-1]
DR UCSC; uc009obf.2; mouse. [Q9CQF6-2]
DR CTD; 60496; -.
DR MGI; MGI:1914868; Aasdhppt.
DR VEuPathDB; HostDB:ENSMUSG00000025894; -.
DR eggNOG; KOG0945; Eukaryota.
DR GeneTree; ENSGT00390000004663; -.
DR HOGENOM; CLU_057011_3_0_1; -.
DR InParanoid; Q9CQF6; -.
DR OMA; IPWSEIR; -.
DR OrthoDB; 960416at2759; -.
DR PhylomeDB; Q9CQF6; -.
DR TreeFam; TF313753; -.
DR Reactome; R-MMU-199220; Vitamin B5 (pantothenate) metabolism.
DR BioGRID-ORCS; 67618; 24 hits in 73 CRISPR screens.
DR ChiTaRS; Aasdhppt; mouse.
DR PRO; PR:Q9CQF6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CQF6; protein.
DR Bgee; ENSMUSG00000025894; Expressed in manus and 226 other tissues.
DR ExpressionAtlas; Q9CQF6; baseline and differential.
DR Genevisible; Q9CQF6; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; ISO:MGI.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; ISS:UniProtKB.
DR Gene3D; 3.90.470.20; -; 2.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR Pfam; PF01648; ACPS; 1.
DR SUPFAM; SSF56214; SSF56214; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..309
FT /note="L-aminoadipate-semialdehyde dehydrogenase-
FT phosphopantetheinyl transferase"
FT /id="PRO_0000175737"
FT BINDING 47
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT BINDING 86..91
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT BINDING 108..111
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT BINDING 181..185
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN7"
FT VAR_SEQ 124..177
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016096"
FT CONFLICT 32
FT /note="E -> G (in Ref. 2; AAH38013)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="S -> F (in Ref. 1; BAB25740)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 35764 MW; 928EE04A1383AE25 CRC64;
MVFPAKRLCV VPSMEGVRWA FSCGTWLPSR AEWLLAMRSI QPEEKERIGK FVFARDAKAA
LAGRLMIRKL VAEKLNIPWD HIRLQRTSKG KPVLAKDSLN PYPNFNFNIS HQGDYAVLAA
EPEVQVGIDI MKTSFPGRGS IPEFFHIMKR KFTKKEWETI RSFNDEWTQL DMFYRHWALK
ESFIKAIGVG LGFEMQRLEF DVSPLNMDIG QVYKETCLIL DGEEEKEWAF EESKIDEHHF
VAVAVRKPDG SRHQNVSYQD DSKLSQRKFT ILNFNDLVAS AIPMTPEDPS FWDCFCFTEE
ILIRNGTKS
