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PEX6_RAT
ID   PEX6_RAT                Reviewed;         978 AA.
AC   P54777; O55097;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Peroxisome assembly factor 2;
DE            Short=PAF-2;
DE   AltName: Full=Peroxin-6;
DE   AltName: Full=Peroxisomal biogenesis factor 6;
DE   AltName: Full=Peroxisomal-type ATPase 1;
GN   Name=Pex6;
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 [MRNA], AND MUTAGENESIS OF LYS-476 AND LYS-748.
RC   STRAIN=Fischer 344; TISSUE=Liver;
RX   PubMed=7493019; DOI=10.1038/ng1295-395;
RA   Tsukamoto T., Miura S., Nakai T., Yokota S., Shimozawa N., Suzuki Y.,
RA   Orii T., Fujiki Y., Sakai F., Bogaki A., Yasumo H., Osumi T.;
RT   "Peroxisome assembly factor-2, a putative ATPase cloned by functional
RT   complementation on a peroxisome-deficient mammalian cell mutant.";
RL   Nat. Genet. 11:395-401(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley;
RA   Tsukamoto T., Hashiguchi N.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in peroxisome biosynthesis. Required for stability
CC       of the PTS1 receptor. Probably required for protein import into
CC       peroxisomes. Anchored by PEX26 to peroxisome membranes, possibly to
CC       form heteromeric AAA ATPase complexes required for the import of
CC       proteins into peroxisomes (By similarity).
CC       {ECO:0000250|UniProtKB:Q13608}.
CC   -!- SUBUNIT: Interacts directly with PEX26 and PEX1. Mediates the indirect
CC       interaction between PEX1 and PEX26. Interacts with ZFAND6 (By
CC       similarity). {ECO:0000250|UniProtKB:Q13608}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane
CC       {ECO:0000250|UniProtKB:Q13608}. Cell projection, cilium, photoreceptor
CC       outer segment {ECO:0000250|UniProtKB:Q13608}. Note=Associated with
CC       peroxisomal membranes. Localized at the base of the outer segment of
CC       photoreceptor cells (By similarity). {ECO:0000250|UniProtKB:Q13608}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; D63673; BAA09824.1; -; mRNA.
DR   EMBL; D89660; BAA24931.1; -; Genomic_DNA.
DR   RefSeq; NP_476466.1; NM_057125.1.
DR   AlphaFoldDB; P54777; -.
DR   SMR; P54777; -.
DR   BioGRID; 250712; 2.
DR   STRING; 10116.ENSRNOP00000022582; -.
DR   jPOST; P54777; -.
DR   PaxDb; P54777; -.
DR   PRIDE; P54777; -.
DR   ABCD; P54777; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000022582; ENSRNOP00000022582; ENSRNOG00000016655.
DR   GeneID; 117265; -.
DR   KEGG; rno:117265; -.
DR   UCSC; RGD:621637; rat.
DR   CTD; 5190; -.
DR   RGD; 621637; Pex6.
DR   eggNOG; KOG0736; Eukaryota.
DR   GeneTree; ENSGT00550000074953; -.
DR   HOGENOM; CLU_000688_0_8_1; -.
DR   InParanoid; P54777; -.
DR   OMA; ALQPCIL; -.
DR   OrthoDB; 233419at2759; -.
DR   PhylomeDB; P54777; -.
DR   Reactome; R-RNO-9033241; Peroxisomal protein import.
DR   PRO; PR:P54777; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000016655; Expressed in liver and 19 other tissues.
DR   Genevisible; P54777; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC-UCL.
DR   GO; GO:0005777; C:peroxisome; ISO:RGD.
DR   GO; GO:0097733; C:photoreceptor cell cilium; ISS:UniProtKB.
DR   GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; ISO:RGD.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISO:RGD.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0007031; P:peroxisome organization; IMP:RGD.
DR   GO; GO:0016558; P:protein import into peroxisome matrix; IBA:GO_Central.
DR   GO; GO:0016561; P:protein import into peroxisome matrix, translocation; ISO:RGD.
DR   GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR   GO; GO:0006625; P:protein targeting to peroxisome; ISO:RGD.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell projection; Cytoplasm; Membrane; Methylation;
KW   Nucleotide-binding; Peroxisome; Peroxisome biogenesis; Reference proteome;
KW   Repeat.
FT   CHAIN           1..978
FT                   /note="Peroxisome assembly factor 2"
FT                   /id="PRO_0000084609"
FT   BINDING         470..477
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         742..749
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         119
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13608"
FT   MUTAGEN         476
FT                   /note="K->A: No loss of function."
FT                   /evidence="ECO:0000269|PubMed:7493019"
FT   MUTAGEN         748
FT                   /note="K->A: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:7493019"
FT   CONFLICT        299
FT                   /note="D -> G (in Ref. 2; BAA24931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        333
FT                   /note="V -> A (in Ref. 2; BAA24931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="Q -> R (in Ref. 2; BAA24931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        546
FT                   /note="R -> C (in Ref. 2; BAA24931)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   978 AA;  104426 MW;  F723193B7E95EA97 CRC64;
     MALAVLHVLE PFPTETPPLA VLLPPGGPWP VTGVGLVLAL RPASESPAGP ALLVAAVEGS
     GAQCEQRGPG PPPLLVSRTL LRVLALSPGA RVRARPVRRP PALGWALLGT SPGPGLGPRV
     GPLLVRRGET LPVPGSRVLE TRPALQGLLG PGTRLAVTEL QGRTKLDPES RDHNHPPPPP
     VVSSFAVSHS IRQLRGVLGG TGDALGVSRS CLRSLGLFQG EWVWVARVGE LPNTSQPHLA
     QVQVLEPRWD LSARLGPNSG QPGEPLADGL VFVPATLAFN LGCDPLEVGE LRIQRYLEDS
     TAAEDKGSCS LLPGPPFARE LHIEVLPSPH CGVNGKYDHV LYQHFHTPRV VQEGDVLCVS
     TAGQVEILEG SLERLPRWRE VFFKVKKTVG EAPDGPASAF LADTTHTSLY LAGTTLSRVP
     PLPSGRSPPW DSLSPPGLEA LVNELCAVLK PHLQPGGTLL TGTSCVLLQG PPGSGKTTAV
     TAACSRLGLH LLKVPCSSLC ADSSRTVETK LQTTFSRARR CRPVVLLLTA LDLLGRDRDG
     LGEDARVVAT LRHLLLDEDP LSRCPPLMVV ATTSRVQDLP TDVRTAFPHE LEVPVLSESQ
     RLSVLQALTA HLPLGQEVNL SQLARRCAGF VVGDLYALLT HASRAACTRI KAAGLAMSEE
     DEGELCAAGF PLLAEDFGQA LDQLQTAHSQ AVGAPKIPSV SWHDVGGLQD VKKEILETIQ
     LPLEHPELLS LGLRRSGLLL HGPPGTGKTL LAKAVATECS LTFLSVKGPE LINMYVGQSE
     ENVREVFARA RAAAPCIIFF DELDSLAPSR GRSGDSGGVM DRVVSQLLAE LDGLHSTQDV
     FVIGATNRPD LLDPALLRPG RFDKLVFVGA SEDRASQLRV LSAITRKFKL EASVSLMNVL
     DCCPPQLTGA DLYSLCSDAM MTALKRRVRD LEEGLEPRSS ALLLTMEDLL QAAARLQPSV
     SEQELLRYKR IQRKFAAC
 
 
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