PEX1_MOUSE
ID PEX1_MOUSE Reviewed; 1284 AA.
AC Q5BL07; Q3UEC7; Q9CU85;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Peroxisome biogenesis factor 1;
DE AltName: Full=Peroxin-1;
GN Name=Pex1;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [LARGE SCALE MRNA] OF 1-505 AND 795-1284 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head, and Liver;
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 [3]
RP PHOSPHOLIPID BINDING, AND MUTAGENESIS OF ARG-135 AND LYS-174.
RX PubMed=17018057; DOI=10.1111/j.1742-4658.2006.05494.x;
RA Shiozawa K., Goda N., Shimizu T., Mizuguchi K., Kondo N., Shimozawa N.,
RA Shirakawa M., Hiroaki H.;
RT "The common phospholipid-binding activity of the N-terminal domains of PEX1
RT and VCP/p97.";
RL FEBS J. 273:4959-4971(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 3-181.
RX PubMed=15328346; DOI=10.1074/jbc.m407837200;
RA Shiozawa K., Maita N., Tomii K., Seto A., Goda N., Akiyama Y., Shimizu T.,
RA Shirakawa M., Hiroaki H.;
RT "Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of
RT a putative adaptor-binding domain.";
RL J. Biol. Chem. 279:50060-50068(2004).
CC -!- FUNCTION: Required for stability of PEX5 and protein import into the
CC peroxisome matrix. Anchored by PEX26 to peroxisome membranes, possibly
CC to form heteromeric AAA ATPase complexes required for the import of
CC proteins into peroxisomes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts directly with PEX6. Interacts indirectly with PEX26,
CC via its interaction with PEX6 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Peroxisome membrane
CC {ECO:0000250}. Note=Associated with peroxisomal membranes.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5BL07-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BL07-2; Sequence=VSP_028131;
CC -!- DOMAIN: The N-terminal domain shows evolutionary conservation with that
CC of VCP, and is able to bind phospholipids with a preference for
CC phosphatidylinositol monophosphates.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; BC090845; AAH90845.1; -; mRNA.
DR EMBL; AK017309; BAB30684.1; -; mRNA.
DR EMBL; AK149599; BAE28984.1; -; mRNA.
DR CCDS; CCDS19065.1; -. [Q5BL07-2]
DR CCDS; CCDS80201.1; -. [Q5BL07-1]
DR RefSeq; NP_001280735.1; NM_001293806.1. [Q5BL07-1]
DR RefSeq; NP_082053.1; NM_027777.2. [Q5BL07-2]
DR PDB; 1WLF; X-ray; 2.05 A; A=3-181.
DR PDBsum; 1WLF; -.
DR AlphaFoldDB; Q5BL07; -.
DR SMR; Q5BL07; -.
DR BioGRID; 214674; 3.
DR IntAct; Q5BL07; 3.
DR STRING; 10090.ENSMUSP00000006061; -.
DR iPTMnet; Q5BL07; -.
DR PhosphoSitePlus; Q5BL07; -.
DR EPD; Q5BL07; -.
DR jPOST; Q5BL07; -.
DR MaxQB; Q5BL07; -.
DR PaxDb; Q5BL07; -.
DR PeptideAtlas; Q5BL07; -.
DR PRIDE; Q5BL07; -.
DR ProteomicsDB; 288098; -. [Q5BL07-1]
DR ProteomicsDB; 288099; -. [Q5BL07-2]
DR Antibodypedia; 15612; 194 antibodies from 32 providers.
DR DNASU; 71382; -.
DR Ensembl; ENSMUST00000006061; ENSMUSP00000006061; ENSMUSG00000005907. [Q5BL07-2]
DR Ensembl; ENSMUST00000121291; ENSMUSP00000113304; ENSMUSG00000005907. [Q5BL07-1]
DR GeneID; 71382; -.
DR KEGG; mmu:71382; -.
DR UCSC; uc008whe.2; mouse. [Q5BL07-1]
DR UCSC; uc008whf.2; mouse. [Q5BL07-2]
DR CTD; 5189; -.
DR MGI; MGI:1918632; Pex1.
DR VEuPathDB; HostDB:ENSMUSG00000005907; -.
DR eggNOG; KOG0735; Eukaryota.
DR GeneTree; ENSGT00550000075032; -.
DR HOGENOM; CLU_000688_1_1_1; -.
DR InParanoid; Q5BL07; -.
DR OMA; QGFVNIQ; -.
DR OrthoDB; 1171861at2759; -.
DR PhylomeDB; Q5BL07; -.
DR TreeFam; TF106447; -.
DR BRENDA; 3.6.4.7; 3474.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 71382; 13 hits in 72 CRISPR screens.
DR ChiTaRS; Pex1; mouse.
DR EvolutionaryTrace; Q5BL07; -.
DR PRO; PR:Q5BL07; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q5BL07; protein.
DR Bgee; ENSMUSG00000005907; Expressed in animal zygote and 225 other tissues.
DR ExpressionAtlas; Q5BL07; baseline and differential.
DR Genevisible; Q5BL07; 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; IDA:HGNC-UCL.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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:0060152; P:microtubule-based peroxisome localization; ISO:MGI.
DR GO; GO:0007031; P:peroxisome organization; ISO:MGI.
DR GO; GO:0016558; P:protein import into peroxisome matrix; 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; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015343; PEX-N_a/b.
DR InterPro; IPR015342; PEX-N_psi_beta-barrel.
DR InterPro; IPR025653; Pex1.
DR PANTHER; PTHR23077:SF12; PTHR23077:SF12; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09262; PEX-1N; 1.
DR Pfam; PF09263; PEX-2N; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Lipid-binding;
KW Membrane; Nucleotide-binding; Peroxisome; Peroxisome biogenesis;
KW Peroxisome biogenesis disorder; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..1284
FT /note="Peroxisome biogenesis factor 1"
FT /id="PRO_0000304931"
FT REGION 339..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 600..607
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 882..889
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43933"
FT MOD_RES 1210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43933"
FT MOD_RES 1212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43933"
FT VAR_SEQ 413..452
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028131"
FT MUTAGEN 135
FT /note="R->A: Loss of phospholipid-binding."
FT /evidence="ECO:0000269|PubMed:17018057"
FT MUTAGEN 174
FT /note="K->A: No effect on phospholipid-binding."
FT /evidence="ECO:0000269|PubMed:17018057"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:1WLF"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1WLF"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1WLF"
FT HELIX 33..38
FT /evidence="ECO:0007829|PDB:1WLF"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1WLF"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1WLF"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1WLF"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1WLF"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:1WLF"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1WLF"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:1WLF"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:1WLF"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:1WLF"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:1WLF"
FT STRAND 152..162
FT /evidence="ECO:0007829|PDB:1WLF"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:1WLF"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1WLF"
SQ SEQUENCE 1284 AA; 141428 MW; 29B6C9B6E93FA6EF CRC64;
MWSSDRLAGA GSGGAVVTVA FTNARDCFLH LPRRLVAQLH LLQNQAIEVA SDHQPTYLSW
VEGRHFNDQS ENVAEINRQV GQKLGLSSGD QVFLRPCSHV VSCQQVEVEP LSADDWEILE
LHAISLEQHL LDQIRIVFPK AVVPIWVDQQ TYIFIQIVTL MPAAPYGRLE TNTKLLIQPK
TRQAKESTFP KEGDAHGQVH SYGREQKGLS KELQTRQLHT NSEGITASNG RDPKVPGGPL
KPSWWAVLGS MLSFGPDSKQ ESAWGSLELG AFKNMQSQAA PLEGTFRVCQ VQPPSARTTT
ATSVFHKHCT AHVFPWDQEY FDVEPSFTVT YGKLVKLHSP KQQQDKSKQG VLLPDKEKQL
SKSPDHKQIS SNRSEEAAEA CVLKVVWNGL EELKNATEFT ESLELLHRGK VWIPDDLRKR
LNIEMHAVVR ITPLETTPKI PRSLKLQPRE NLPKDVNEET IKTVFSSWVQ QSATTMLPLV
ISKEERIKLE IKDGLREFSL STVHSQEKEK EEGKTVFVLS SILLQKISVQ VLLEPMIKEE
QSAEIDFLLP SLTLSSLGGV SALGASAMEH ITHSLLGRPL SRQLMALVAG LRNGALLITG
GKGSGKSTFA KAICKEAQDT LDARVETVDC KALRGKRLES IQKALEVAFS EAAWRQPSVI
LLDDLDLIAG LPSVPEQEHS PEAVQSQRLA HALNDMIKEF VSTGSLVALI ATSQLQQSLH
PSLVSAQGIH TFQCVQHLQP PNPEQRCEIL HSVVKNKLGC DISNFPDLDL QCIAKDTEAF
VARDFTVLVD RAIHSSLSRQ HSSSREDLTL TTSDFQKALR GFLPASLRNV NLHKPRDLGW
DKIGGLHEVR QILMDTIQLP AKYPELFANL PIRQRTGILL YGPPGTGKTL LAGVVARESG
MNFISIKGPE LLSKYIGASE QAVRDVFIRA QAAKPCILFF DEFESIAPRR GHDNTGVTDR
VVNQLLTQLD GVEGLQGVYV LAATSRPDLI DPALLRPGRL DKCVYCPPPD QVSRLEILTV
LSKSLALADD VDLQHVASVT DSFTGADLKA LLYNAQLEAL QGRLLPSGLP DGGSSSDSDL
SLSSMVFLNH SSGSDDSAGD GECGLEQSLL SLEMSEILPD ESKFNMYRLY FGSSYESELG
NGTPSDLSSH CLSAPSSVTQ DLPAAPGKDP LFTQHPVFRT PSQEGCQDLT QEQRDQLRAE
ISIIKGRYRS QSGEDESLNQ PGPIKTTFAI SQAHLMTALA HTRPSISEDE GKEFAELYEN
FQNPKKRKNQ SGTVFRTGQK VTLA
