PAAT_HUMAN
ID PAAT_HUMAN Reviewed; 445 AA.
AC Q9H8K7; Q0P6C6; Q8N597;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=ATPase PAAT {ECO:0000305};
DE EC=3.6.1.- {ECO:0000269|PubMed:25063848};
DE AltName: Full=Protein associated with ABC transporters {ECO:0000303|PubMed:25063848};
DE Short=PAAT {ECO:0000303|PubMed:25063848};
GN Name=PAAT {ECO:0000303|PubMed:25063848};
GN Synonyms=C10orf88 {ECO:0000312|HGNC:HGNC:25822};
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 [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis, and Uterus;
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=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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-182; SER-254 AND
RP SER-302, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH ABCB7;
RP ABCB8/MITOSUR AND ABCB10.
RX PubMed=25063848; DOI=10.1096/fj.14-254045;
RA Yang X., Yang J., Li L., Sun L., Yi X., Han X., Si W., Yan R., Chen Z.,
RA Xie G., Li W., Shang Y., Liang J.;
RT "PAAT, a novel ATPase and trans-regulator of mitochondrial ABC
RT transporters, is critically involved in the maintenance of mitochondrial
RT homeostasis.";
RL FASEB J. 28:4821-4834(2014).
CC -!- FUNCTION: ATPase that regulates mitochondrial ABC transporters ABCB7,
CC ABCB8/MITOSUR and ABCB10 (PubMed:25063848). Regulates mitochondrial
CC ferric concentration and heme biosynthesis and plays a role in the
CC maintenance of mitochondrial homeostasis and cell survival
CC (PubMed:25063848). {ECO:0000269|PubMed:25063848}.
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:0000269|PubMed:25063848};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000269|PubMed:25063848};
CC -!- SUBUNIT: Homodimer (PubMed:25063848). Interacts with ABCB7,
CC ABCB8/MITOSUR and ABCB10 (PubMed:25063848).
CC {ECO:0000269|PubMed:25063848}.
CC -!- INTERACTION:
CC Q9H8K7; P55212: CASP6; NbExp=3; IntAct=EBI-714785, EBI-718729;
CC Q9H8K7; P28329-3: CHAT; NbExp=3; IntAct=EBI-714785, EBI-25837549;
CC Q9H8K7; P22607: FGFR3; NbExp=3; IntAct=EBI-714785, EBI-348399;
CC Q9H8K7; P06396: GSN; NbExp=3; IntAct=EBI-714785, EBI-351506;
CC Q9H8K7; O75031: HSF2BP; NbExp=3; IntAct=EBI-714785, EBI-7116203;
CC Q9H8K7; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-714785, EBI-739832;
CC Q9H8K7; Q8N448: LNX2; NbExp=3; IntAct=EBI-714785, EBI-2340947;
CC Q9H8K7; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-714785, EBI-16439278;
CC Q9H8K7; Q96KN3: PKNOX2; NbExp=3; IntAct=EBI-714785, EBI-2692890;
CC Q9H8K7; P62826: RAN; NbExp=3; IntAct=EBI-714785, EBI-286642;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25063848}.
CC Mitochondrion {ECO:0000269|PubMed:25063848}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK023552; BAB14609.1; -; mRNA.
DR EMBL; BC032645; AAH32645.1; -; mRNA.
DR CCDS; CCDS7632.1; -.
DR RefSeq; NP_079218.2; NM_024942.3.
DR AlphaFoldDB; Q9H8K7; -.
DR SMR; Q9H8K7; -.
DR BioGRID; 123064; 141.
DR IntAct; Q9H8K7; 38.
DR STRING; 9606.ENSP00000419126; -.
DR iPTMnet; Q9H8K7; -.
DR PhosphoSitePlus; Q9H8K7; -.
DR BioMuta; C10orf88; -.
DR DMDM; 118572224; -.
DR EPD; Q9H8K7; -.
DR jPOST; Q9H8K7; -.
DR MassIVE; Q9H8K7; -.
DR MaxQB; Q9H8K7; -.
DR PaxDb; Q9H8K7; -.
DR PeptideAtlas; Q9H8K7; -.
DR PRIDE; Q9H8K7; -.
DR ProteomicsDB; 81215; -.
DR Antibodypedia; 32320; 65 antibodies from 14 providers.
DR DNASU; 80007; -.
DR Ensembl; ENST00000481909.2; ENSP00000419126.1; ENSG00000119965.13.
DR GeneID; 80007; -.
DR KEGG; hsa:80007; -.
DR MANE-Select; ENST00000481909.2; ENSP00000419126.1; NM_024942.4; NP_079218.2.
DR UCSC; uc001lgw.3; human.
DR CTD; 80007; -.
DR DisGeNET; 80007; -.
DR GeneCards; C10orf88; -.
DR HGNC; HGNC:25822; C10orf88.
DR HPA; ENSG00000119965; Low tissue specificity.
DR neXtProt; NX_Q9H8K7; -.
DR OpenTargets; ENSG00000119965; -.
DR PharmGKB; PA134993933; -.
DR VEuPathDB; HostDB:ENSG00000119965; -.
DR eggNOG; ENOG502RUU4; Eukaryota.
DR GeneTree; ENSGT00390000017384; -.
DR HOGENOM; CLU_053533_0_0_1; -.
DR InParanoid; Q9H8K7; -.
DR OMA; QQVQCLV; -.
DR OrthoDB; 1345490at2759; -.
DR PhylomeDB; Q9H8K7; -.
DR TreeFam; TF333208; -.
DR PathwayCommons; Q9H8K7; -.
DR SignaLink; Q9H8K7; -.
DR BioGRID-ORCS; 80007; 18 hits in 1055 CRISPR screens.
DR ChiTaRS; C10orf88; human.
DR GenomeRNAi; 80007; -.
DR Pharos; Q9H8K7; Tdark.
DR PRO; PR:Q9H8K7; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9H8K7; protein.
DR Bgee; ENSG00000119965; Expressed in cortical plate and 166 other tissues.
DR Genevisible; Q9H8K7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR InterPro; IPR028043; PAAT-like.
DR PANTHER; PTHR14787; PTHR14787; 1.
DR Pfam; PF14958; DUF4506; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Mitochondrion; Phosphoprotein; Reference proteome.
FT CHAIN 1..445
FT /note="ATPase PAAT"
FT /id="PRO_0000260085"
FT REGION 426..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 67
FT /note="N -> D (in Ref. 1; BAB14609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 49249 MW; D541EA1E400E532B CRC64;
METRTEDGGL TRRPTLASSW DVAGGALTHS LLLTRAGLGP GDFDWEELLA PPAPGQDLVI
LKRNHNNKDE NPCFLYLRCG PDGGEEIASI GILSSARNME VYLGEEYCGT SRGKNVCTVL
DDSEHEKIIL YKKNLKLESS THACKIKLLS FGERQCVFIS KVVVHMRSVF ANSSTSSPAL
GSRIDLDKVQ TIMESMGSKL SPGAQQLMDM VRCQQRNCIP IGEQLQSVLG NSGYKHMIGL
QSSSTLGTLN KSSSTPFPFR TGLTSGNVTE NLQTYIDKST QLPGGENSTK LDECKVMPQN
HSFLENDLKN AMASFLPKKV SDNSNIPNSE LLPFLQNLCS QVNHLHVGNK TECQENITKH
GERILGVGME EQSICSYLEK ILSKNMELME KKLMDYIDQR IHELQEHIDD KIALLLDLLQ
NPNSPPTGIP LRHYDSGERL SNGER
