PEX7_HUMAN
ID PEX7_HUMAN Reviewed; 323 AA.
AC O00628; C0H5X6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Peroxisomal targeting signal 2 receptor;
DE Short=PTS2 receptor;
DE AltName: Full=Peroxin-7;
GN Name=PEX7; Synonyms=PTS2R;
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 [MRNA] (ISOFORM 1).
RX PubMed=9090383; DOI=10.1038/ng0497-381;
RA Purdue P.E., Zhang J.W., Skoneczny M., Lazarow P.B.;
RT "Rhizomelic chondrodysplasia punctata is caused by deficiency of human
RT PEX7, a homologue of the yeast PTS2 receptor.";
RL Nat. Genet. 15:381-384(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS RCDP1 ARG-217 AND
RP VAL-218.
RC TISSUE=Retina;
RX PubMed=9090381; DOI=10.1038/ng0497-369;
RA Braverman N., Steel G., Obie C., Moser A., Moser H., Gould S.J., Valle D.;
RT "Human PEX7 encodes the peroxisomal PTS2 receptor and is responsible for
RT rhizomelic chondrodysplasia punctata.";
RL Nat. Genet. 15:369-376(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10673331; DOI=10.1006/geno.1999.6080;
RA Braverman N., Steel G., Lin P., Moser A., Moser H., Valle D.;
RT "PEX7 gene structure, alternative transcripts, and evidence for a founder
RT haplotype for the frequent RCDP allele, L292ter.";
RL Genomics 63:181-192(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Ovary;
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 [7]
RP INTERACTION WITH VWA8.
RX PubMed=30204880; DOI=10.1093/jb/mvy073;
RA Niwa H., Miyauchi-Nanri Y., Okumoto K., Mukai S., Noi K., Ogura T.,
RA Fujiki Y.;
RT "A newly isolated Pex7-binding, atypical PTS2 protein P7BP2 is a novel
RT dynein-type AAA+ protein.";
RL J. Biochem. 164:437-447(2018).
RN [8]
RP VARIANT PBD9B PRO-14.
RX PubMed=12522768; DOI=10.1086/346093;
RA van den Brink D.M., Brites P., Haasjes J., Wierzbicki A.S., Mitchell J.,
RA Lambert-Hamill M., de Belleroche J., Jansen G.A., Waterham H.R.,
RA Wanders R.J.A.;
RT "Identification of PEX7 as the second gene involved in Refsum disease.";
RL Am. J. Hum. Genet. 72:471-477(2003).
CC -!- FUNCTION: Binds to the N-terminal PTS2-type peroxisomal targeting
CC signal and plays an essential role in peroxisomal protein import.
CC {ECO:0000250|UniProtKB:Q8R537}.
CC -!- SUBUNIT: Interacts with PEX5 (By similarity). Interacts with VWA8
CC (PubMed:30204880). {ECO:0000250|UniProtKB:Q8R537,
CC ECO:0000269|PubMed:30204880}.
CC -!- INTERACTION:
CC O00628; O75925: PIAS1; NbExp=3; IntAct=EBI-5238811, EBI-629434;
CC O00628-2; Q8WXF7: ATL1; NbExp=3; IntAct=EBI-25882083, EBI-2410266;
CC O00628-2; Q96EL1: INKA1; NbExp=3; IntAct=EBI-25882083, EBI-10285157;
CC O00628-2; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-25882083, EBI-11959123;
CC O00628-2; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-25882083, EBI-357085;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q8R537}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q8R537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00628-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00628-2; Sequence=VSP_056393;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in pancreas,
CC skeletal muscle and heart.
CC -!- DISEASE: Peroxisome biogenesis disorder complementation group 11 (PBD-
CC CG11) [MIM:614879]: A peroxisomal disorder arising from a failure of
CC protein import into the peroxisomal membrane or matrix. The peroxisome
CC biogenesis disorders (PBD group) are genetically heterogeneous with at
CC least 14 distinct genetic groups as concluded from complementation
CC studies. Include disorders are: Zellweger syndrome (ZWS), neonatal
CC adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and
CC classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and
CC IRD are distinct from RCDP and constitute a clinical continuum of
CC overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS).
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Rhizomelic chondrodysplasia punctata 1 (RCDP1) [MIM:215100]: A
CC peroxisome biogenesis disorder. It is characterized by severely
CC disturbed endochondral bone formation, rhizomelic shortening of femur
CC and humerus, vertebral disorders, dwarfism, cataract, cutaneous
CC lesions, facial dysmorphism, and severe intellectual disability with
CC spasticity. {ECO:0000269|PubMed:9090381}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Peroxisome biogenesis disorder 9B (PBD9B) [MIM:614879]: A
CC peroxisome biogenesis disorder with unusually mild clinical and
CC biochemical manifestations. Affected individuals manifest a variable
CC phenotype similar to, and in some cases indistinguishable from, classic
CC Refsum disease. Variable features include ocular abnormalities,
CC sensorimotor neuropathy, ichthyosis, deafness, chondrodysplasia
CC punctata without rhizomelia or growth failure.
CC {ECO:0000269|PubMed:12522768}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat peroxin-7 family. {ECO:0000305}.
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DR EMBL; U88871; AAC51238.1; -; mRNA.
DR EMBL; U76560; AAB50556.1; -; mRNA.
DR EMBL; AF180814; AAF37350.1; -; Genomic_DNA.
DR EMBL; AF180806; AAF37350.1; JOINED; Genomic_DNA.
DR EMBL; AF180807; AAF37350.1; JOINED; Genomic_DNA.
DR EMBL; AF180808; AAF37350.1; JOINED; Genomic_DNA.
DR EMBL; AF180809; AAF37350.1; JOINED; Genomic_DNA.
DR EMBL; AF180810; AAF37350.1; JOINED; Genomic_DNA.
DR EMBL; AF180811; AAF37350.1; JOINED; Genomic_DNA.
DR EMBL; AF180812; AAF37350.1; JOINED; Genomic_DNA.
DR EMBL; AF180813; AAF37350.1; JOINED; Genomic_DNA.
DR EMBL; AL121933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47941.1; -; Genomic_DNA.
DR EMBL; BC006268; AAH06268.1; -; mRNA.
DR EMBL; BC031606; AAH31606.1; -; mRNA.
DR CCDS; CCDS5180.1; -. [O00628-1]
DR RefSeq; NP_000279.1; NM_000288.3. [O00628-1]
DR AlphaFoldDB; O00628; -.
DR SMR; O00628; -.
DR BioGRID; 111214; 39.
DR IntAct; O00628; 27.
DR MINT; O00628; -.
DR STRING; 9606.ENSP00000315680; -.
DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family.
DR iPTMnet; O00628; -.
DR PhosphoSitePlus; O00628; -.
DR BioMuta; PEX7; -.
DR EPD; O00628; -.
DR jPOST; O00628; -.
DR MassIVE; O00628; -.
DR MaxQB; O00628; -.
DR PaxDb; O00628; -.
DR PeptideAtlas; O00628; -.
DR PRIDE; O00628; -.
DR ProteomicsDB; 48001; -. [O00628-1]
DR ProteomicsDB; 7570; -.
DR ABCD; O00628; 1 sequenced antibody.
DR Antibodypedia; 33017; 164 antibodies from 34 providers.
DR DNASU; 5191; -.
DR Ensembl; ENST00000318471.5; ENSP00000315680.3; ENSG00000112357.14. [O00628-1]
DR Ensembl; ENST00000541292.6; ENSP00000441004.1; ENSG00000112357.14. [O00628-2]
DR GeneID; 5191; -.
DR KEGG; hsa:5191; -.
DR MANE-Select; ENST00000318471.5; ENSP00000315680.3; NM_000288.4; NP_000279.1.
DR UCSC; uc063rtk.1; human. [O00628-1]
DR CTD; 5191; -.
DR DisGeNET; 5191; -.
DR GeneCards; PEX7; -.
DR GeneReviews; PEX7; -.
DR HGNC; HGNC:8860; PEX7.
DR HPA; ENSG00000112357; Low tissue specificity.
DR MalaCards; PEX7; -.
DR MIM; 215100; phenotype.
DR MIM; 601757; gene.
DR MIM; 614879; phenotype.
DR neXtProt; NX_O00628; -.
DR OpenTargets; ENSG00000112357; -.
DR Orphanet; 773; Refsum disease.
DR Orphanet; 309789; Rhizomelic chondrodysplasia punctata type 1.
DR PharmGKB; PA33202; -.
DR VEuPathDB; HostDB:ENSG00000112357; -.
DR eggNOG; KOG0277; Eukaryota.
DR GeneTree; ENSGT00940000157264; -.
DR HOGENOM; CLU_046581_0_1_1; -.
DR InParanoid; O00628; -.
DR OMA; EKWNYHT; -.
DR PhylomeDB; O00628; -.
DR TreeFam; TF323220; -.
DR PathwayCommons; O00628; -.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SignaLink; O00628; -.
DR SIGNOR; O00628; -.
DR BioGRID-ORCS; 5191; 27 hits in 1085 CRISPR screens.
DR ChiTaRS; PEX7; human.
DR GenomeRNAi; 5191; -.
DR Pharos; O00628; Tbio.
DR PRO; PR:O00628; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O00628; protein.
DR Bgee; ENSG00000112357; Expressed in pigmented layer of retina and 187 other tissues.
DR ExpressionAtlas; O00628; baseline and differential.
DR Genevisible; O00628; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0005053; F:peroxisome matrix targeting signal-2 binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0007031; P:peroxisome organization; IMP:UniProtKB.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IDA:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR044536; PEX7.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR46027; PTHR46027; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cataract; Cytoplasm; Deafness; Disease variant;
KW Ichthyosis; Peroxisome; Peroxisome biogenesis disorder; Protein transport;
KW Reference proteome; Repeat; Retinitis pigmentosa;
KW Rhizomelic chondrodysplasia punctata; Transport; WD repeat.
FT CHAIN 1..323
FT /note="Peroxisomal targeting signal 2 receptor"
FT /id="PRO_0000051116"
FT REPEAT 65..96
FT /note="WD 1"
FT REPEAT 109..141
FT /note="WD 2"
FT REPEAT 153..184
FT /note="WD 3"
FT REPEAT 196..227
FT /note="WD 4"
FT REPEAT 240..271
FT /note="WD 5"
FT REPEAT 284..315
FT /note="WD 6"
FT VAR_SEQ 250..323
FT /note="FSPFHASVLASCSYDFTVRFWNFSKPDSLLETVEHHTEFTCGLDFSLQSPTQ
FT VADCSWDETIKIYDPACLTIPA -> MESCPVTQTRSQLTATSAFWVQAVLLPQPTE
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056393"
FT VARIANT 14
FT /note="T -> P (in PBD9B; dbSNP:rs61753233)"
FT /evidence="ECO:0000269|PubMed:12522768"
FT /id="VAR_016810"
FT VARIANT 217
FT /note="G -> R (in RCDP1; unknown pathological significance;
FT dbSNP:rs121909152)"
FT /evidence="ECO:0000269|PubMed:9090381"
FT /id="VAR_007725"
FT VARIANT 218
FT /note="A -> V (in RCDP1; dbSNP:rs121909151)"
FT /evidence="ECO:0000269|PubMed:9090381"
FT /id="VAR_007726"
SQ SEQUENCE 323 AA; 35892 MW; D405387F7F14B432 CRC64;
MSAVCGGAAR MLRTPGRHGY AAEFSPYLPG RLACATAQHY GIAGCGTLLI LDPDEAGLRL
FRSFDWNDGL FDVTWSENNE HVLITCSGDG SLQLWDTAKA AGPLQVYKEH AQEVYSVDWS
QTRGEQLVVS GSWDQTVKLW DPTVGKSLCT FRGHESIIYS TIWSPHIPGC FASASGDQTL
RIWDVKAAGV RIVIPAHQAE ILSCDWCKYN ENLLVTGAVD CSLRGWDLRN VRQPVFELLG
HTYAIRRVKF SPFHASVLAS CSYDFTVRFW NFSKPDSLLE TVEHHTEFTC GLDFSLQSPT
QVADCSWDET IKIYDPACLT IPA
