PAAT_MOUSE
ID PAAT_MOUSE Reviewed; 444 AA.
AC Q9D2Q3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=ATPase PAAT {ECO:0000305};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q9H8K7};
DE AltName: Full=Protein associated with ABC transporters {ECO:0000250|UniProtKB:Q9H8K7};
DE Short=PAAT {ECO:0000250|UniProtKB:Q9H8K7};
GN Name=Paat {ECO:0000250|UniProtKB:Q9H8K7};
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].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, and Tongue;
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].
RC STRAIN=FVB/N; TISSUE=Liver;
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).
CC -!- FUNCTION: ATPase that regulates mitochondrial ABC transporters ABCB7,
CC ABCB8/MITOSUR and ABCB10. Regulates mitochondrial ferric concentration
CC and heme biosynthesis and plays a role in the maintenance of
CC mitochondrial homeostasis and cell survival.
CC {ECO:0000250|UniProtKB:Q9H8K7}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q9H8K7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q9H8K7};
CC -!- SUBUNIT: Homodimer. Interacts with ABCB7, ABCB8/MITOSUR and ABCB10.
CC {ECO:0000250|UniProtKB:Q9H8K7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H8K7}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q9H8K7}.
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DR EMBL; AK019097; BAB31544.1; -; mRNA.
DR EMBL; AK088850; BAC40612.1; -; mRNA.
DR EMBL; AK148008; BAE28285.1; -; mRNA.
DR EMBL; BC044749; AAH44749.1; -; mRNA.
DR CCDS; CCDS40159.1; -.
DR RefSeq; NP_080931.1; NM_026655.3.
DR RefSeq; XP_011240190.1; XM_011241888.2.
DR AlphaFoldDB; Q9D2Q3; -.
DR SMR; Q9D2Q3; -.
DR STRING; 10090.ENSMUSP00000050128; -.
DR iPTMnet; Q9D2Q3; -.
DR PhosphoSitePlus; Q9D2Q3; -.
DR EPD; Q9D2Q3; -.
DR jPOST; Q9D2Q3; -.
DR MaxQB; Q9D2Q3; -.
DR PaxDb; Q9D2Q3; -.
DR PeptideAtlas; Q9D2Q3; -.
DR PRIDE; Q9D2Q3; -.
DR Antibodypedia; 32320; 65 antibodies from 14 providers.
DR Ensembl; ENSMUST00000059438; ENSMUSP00000050128; ENSMUSG00000040177.
DR GeneID; 68277; -.
DR KEGG; mmu:68277; -.
DR UCSC; uc009kbg.1; mouse.
DR MGI; MGI:1915527; 2310057M21Rik.
DR VEuPathDB; HostDB:ENSMUSG00000040177; -.
DR eggNOG; ENOG502RUU4; Eukaryota.
DR GeneTree; ENSGT00390000017384; -.
DR HOGENOM; CLU_053533_0_0_1; -.
DR InParanoid; Q9D2Q3; -.
DR OMA; QQVQCLV; -.
DR OrthoDB; 1345490at2759; -.
DR PhylomeDB; Q9D2Q3; -.
DR TreeFam; TF333208; -.
DR BioGRID-ORCS; 68277; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9D2Q3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D2Q3; protein.
DR Bgee; ENSMUSG00000040177; Expressed in occipital region and 246 other tissues.
DR ExpressionAtlas; Q9D2Q3; baseline and differential.
DR Genevisible; Q9D2Q3; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR InterPro; IPR028043; PAAT-like.
DR PANTHER; PTHR14787; PTHR14787; 1.
DR Pfam; PF14958; DUF4506; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Mitochondrion; Phosphoprotein; Reference proteome.
FT CHAIN 1..444
FT /note="ATPase PAAT"
FT /id="PRO_0000260086"
FT REGION 279..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8K7"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8K7"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8K7"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8K7"
SQ SEQUENCE 444 AA; 48743 MW; 40949A5121D57A23 CRC64;
METAIEDAGL DRGPTLTSSW DAACGALTQS LFLTRTGPRA QDLDFEQLLE PPAPSQDPVS
LKSSLSPRDE NPCFIYLNCG PNGGEEILSV GVLSSARNME VYLGEEYCGT SRGKTACTVL
DDSEHEKILL YKKYLKLDSP THACKIKLLS FGEKQCVLVS KVVVHLRPRS ADPSPRSAAL
GSRIDLDNIQ TIMESMGSRL SPGAQQLMSM IRFQQQNRLP IGDQLQSVLG SAGHKHLMAL
QSSPSPAVLD KASSTPFPFR TGLTPSAITE NLKALIDKSA QPSGEGNTTN HDEGHLMPQN
HSLESDLKNA VSSFLPKKAS GSSSVPSSEL LPFLQNLCSQ VNHLRVGHNA RWQENISKPR
EGMVGVPMEE QPVCSYLEKI LSKNMELMEK KLMDHIDERI YQLQEHIDAK MALLVDLLRG
PNSPPPGMPL RHYDSRERLS NGER
