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
//