PEX6_MOUSE
ID PEX6_MOUSE Reviewed; 981 AA.
AC Q99LC9; Q6YNQ9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
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 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=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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 379-981.
RC STRAIN=129/SvEv;
RA Chen Y.-M.A., Wang Y.-C., Liu S.-P., Lee C.-M., Tsai T.-F.;
RT "Identification of the mouse GNMT and PEX6 genes.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Liver, Lung, 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).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=27302843; DOI=10.1038/ejhg.2016.62;
RA Smith C.E., Poulter J.A., Levin A.V., Capasso J.E., Price S., Ben-Yosef T.,
RA Sharony R., Newman W.G., Shore R.C., Brookes S.J., Mighell A.J.,
RA Inglehearn C.F.;
RT "Spectrum of PEX1 and PEX6 variants in Heimler syndrome.";
RL Eur. J. Hum. Genet. 24:1565-1571(2016).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=26593283; DOI=10.1002/humu.22934;
RA Zaki M.S., Heller R., Thoenes M., Nuernberg G., Stern-Schneider G.,
RA Nuernberg P., Karnati S., Swan D., Fateen E., Nagel-Wolfrum K.,
RA Mostafa M.I., Thiele H., Wolfrum U., Baumgart-Vogt E., Bolz H.J.;
RT "PEX6 is expressed in photoreceptor cilia and mutated in deafblindness with
RT enamel dysplasia and microcephaly.";
RL Hum. Mutat. 37:170-174(2016).
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). {ECO:0000250}.
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane
CC {ECO:0000250|UniProtKB:Q13608}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000269|PubMed:26593283}. Note=Associated with
CC peroxisomal membranes (By similarity). Localized at the base of the
CC outer segment of photoreceptor cells (PubMed:26593283).
CC {ECO:0000250|UniProtKB:Q13608, ECO:0000269|PubMed:26593283}.
CC -!- TISSUE SPECIFICITY: In the teeth, expressed in ameloblasts and
CC odontoblasts (PubMed:26593283). Expressed in the retina, at higher
CC levels in the ganglion cell layer and photoreceptor layer at the joint
CC between the outer and inner segments (PubMed:26593283,
CC PubMed:27302843). {ECO:0000269|PubMed:26593283,
CC ECO:0000269|PubMed:27302843}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; BC003424; AAH03424.1; -; mRNA.
DR EMBL; AY054409; AAL06143.1; -; Genomic_DNA.
DR CCDS; CCDS28837.1; -.
DR RefSeq; NP_663463.1; NM_145488.1.
DR AlphaFoldDB; Q99LC9; -.
DR SMR; Q99LC9; -.
DR BioGRID; 230326; 7.
DR STRING; 10090.ENSMUSP00000002840; -.
DR iPTMnet; Q99LC9; -.
DR PhosphoSitePlus; Q99LC9; -.
DR EPD; Q99LC9; -.
DR jPOST; Q99LC9; -.
DR MaxQB; Q99LC9; -.
DR PaxDb; Q99LC9; -.
DR PeptideAtlas; Q99LC9; -.
DR PRIDE; Q99LC9; -.
DR ProteomicsDB; 288044; -.
DR Antibodypedia; 16146; 232 antibodies from 33 providers.
DR DNASU; 224824; -.
DR Ensembl; ENSMUST00000002840; ENSMUSP00000002840; ENSMUSG00000002763.
DR GeneID; 224824; -.
DR KEGG; mmu:224824; -.
DR UCSC; uc008cud.1; mouse.
DR CTD; 5190; -.
DR MGI; MGI:2385054; Pex6.
DR VEuPathDB; HostDB:ENSMUSG00000002763; -.
DR eggNOG; KOG0736; Eukaryota.
DR GeneTree; ENSGT00550000074953; -.
DR HOGENOM; CLU_000688_0_8_1; -.
DR InParanoid; Q99LC9; -.
DR OMA; ALQPCIL; -.
DR OrthoDB; 233419at2759; -.
DR PhylomeDB; Q99LC9; -.
DR TreeFam; TF106428; -.
DR BRENDA; 3.6.4.7; 3474.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 224824; 7 hits in 77 CRISPR screens.
DR PRO; PR:Q99LC9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q99LC9; protein.
DR Bgee; ENSMUSG00000002763; Expressed in rostral migratory stream and 253 other tissues.
DR Genevisible; Q99LC9; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0097733; C:photoreceptor cell cilium; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0007031; P:peroxisome organization; ISO:MGI.
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:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0006625; P:protein targeting to peroxisome; ISO:MGI.
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..981
FT /note="Peroxisome assembly factor 2"
FT /id="PRO_0000084608"
FT BINDING 471..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 745..752
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 CONFLICT 520
FT /note="R -> H (in Ref. 2; AAL06143)"
FT /evidence="ECO:0000305"
FT CONFLICT 895
FT /note="A -> P (in Ref. 2; AAL06143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 981 AA; 104549 MW; 955DBBFB130117CF CRC64;
MALAVLRVLD PFPTETPPLA VLLPPGGPWP ATGLGLVLAL RPASESPAKP ALLVAAVEGS
GAQGEQRGPG PPPLLVSRAL LRVLALGPGA RVRARLVRRP PALGWALLAT APGPGLGPRV
GPLLVRRGET LPVPGSRVLE TRPALQGLLG PGTRLAVTEL RGRAKLGQES RDHSHPPPPP
VVSSFAASHS VRRLRGVLGG TGDALGVSRS CLRSLGLFQG EWVWVAQVAE LPNSSQPRLA
QVQVLEPRWE LSERLGPNSG QQPGEPLADG LVFLPATLAF NLGCDPLEVG ELRIQRYLEG
SIAPENKGSC SPLPGPPFAR ELHIEILSSP HYSANGNYDH VLYRHFQTPR VVQEGDVLCV
STAGQVEILE GSLERLPRWR EMFFKVKKTV GEAPEGPASA FLADTTHTSL YLAGTALSHV
PSLPSGRSPP WDSLSPPGLE ALVNELCAIL KPHLQPGGTL LTGTSCVLLQ GPPGSGKTTA
VTAACSRLGL HLLKVPCSSL CADSSRAVET KLQATFSRAR RCRPAVLLLT AVDLLGRDRD
GLGEDARVAA TLRHLLLDED ALSRCPPLMV VATTSRVQDL PTDVQTAFPH ELEVPVLSEA
QRLSILQALT AHLPLGQEVN LPQLARRCAG FVVGDLYALL THTCRAACTR IRASGSAGGL
SEEDEGDLCV AGFPLLAEDF GQALDQLQTA HSQAVGAPRI PSVSWHDVGG LQDVKKEILE
TIQLPLEHPE LLSLGLRRSG LLLHGPPGTG KTLLAKAVAT ECSLTFLSVK GPELINMYVG
QSEENVREVF ARARAAAPCI IFFDELDSLA PSRGRSGDSG GVMDRVVSQL LAELDGLHST
QDVFVIGATN RPDLLDPALL RPGRFDKLVF VGASEDRASQ LRVLSAITRK FKLEASVSLA
NVLDCCPPQL TGADLYSLCS DAMMTALKRR VRDLEEGLEL RSSALLLTME DLLQAAARLQ
PSVSEQELLR YKRIQRKFAA C
