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PAAT_RAT
ID   PAAT_RAT                Reviewed;         444 AA.
AC   Q5XI46;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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; BC083846; AAH83846.1; -; mRNA.
DR   RefSeq; NP_001014047.1; NM_001014025.1.
DR   AlphaFoldDB; Q5XI46; -.
DR   SMR; Q5XI46; -.
DR   STRING; 10116.ENSRNOP00000027956; -.
DR   PhosphoSitePlus; Q5XI46; -.
DR   PaxDb; Q5XI46; -.
DR   Ensembl; ENSRNOT00000027956; ENSRNOP00000027956; ENSRNOG00000020597.
DR   GeneID; 309029; -.
DR   KEGG; rno:309029; -.
DR   UCSC; RGD:1305014; rat.
DR   CTD; 309029; -.
DR   RGD; 1305014; RGD1305014.
DR   eggNOG; ENOG502RUU4; Eukaryota.
DR   GeneTree; ENSGT00390000017384; -.
DR   HOGENOM; CLU_053533_0_0_1; -.
DR   InParanoid; Q5XI46; -.
DR   OMA; QQVQCLV; -.
DR   OrthoDB; 1345490at2759; -.
DR   PhylomeDB; Q5XI46; -.
DR   TreeFam; TF333208; -.
DR   PRO; PR:Q5XI46; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020597; Expressed in cerebellum and 19 other tissues.
DR   Genevisible; Q5XI46; RN.
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; ISO:RGD.
DR   InterPro; IPR028043; PAAT-like.
DR   PANTHER; PTHR14787; PTHR14787; 1.
DR   Pfam; PF14958; DUF4506; 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_0000260087"
FT   REGION          424..444
FT                   /note="Disordered"
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;  48820 MW;  390D3EE4C2505C60 CRC64;
     METAIEDAGL DRGPTLTSSW DAACGALTQS LFLTRTGPRA QDLDFEQLLA PPAQGPDLVS
     LKSSLSPRDE NPCFIYLKCG PNGGEEILSV GILSSARNME VYLGEEYCGT SRGKNVCTVL
     DNSEHEKILL YKKYLKLESP THACKIKLLS FGEEQCVLIS KVVVHLRPRS AKPSPSSPAL
     GSRIDLDNIQ TIMESMGSKL SPGAQQLMDM IRFQQQNCLP IRDQLQSVLG TAGHKHLMAL
     QSSPSSGVVD KASSTPFPFR TGLTPSAITE NLKALIDKST QPSGEGNTTN HNECHLMPQN
     HSLESDLKNA VSSFLPKKAS GSSSVPNSEL LPFLQNLCSQ VNHLRVGHNA RWQENVSKPR
     EGTVGVPLEE QPVCSYLEKI LSKNMEVMEK KLMKHIDERI YQLQEHIDAK MALLVDLLRS
     PNSPSPGMPL RHYDSRERLS NGER
 
 
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