ID PEX5_HUMAN Reviewed; 639 AA. AC P50542; Q15115; Q15266; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 3. DT 09-JAN-2007, entry version 65. DE Peroxisomal targeting signal 1 receptor (Peroxisome receptor 1) DE (Peroxisomal C-terminal targeting signal import receptor) (PTS1-BP) DE (Peroxin-5) (PTS1 receptor). GN Name=PEX5; Synonyms=PXR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT NALD LYS-526. RX MEDLINE=95235555; PubMed=7719337; DOI=10.1038/ng0295-115; RA Dodt G., Braverman N., Wong C., Moser A., Moser H.W., Watkins P., RA Valle D., Gould S.J.; RT "Mutations in the PTS1 receptor gene, PXR1, define complementation RT group 2 of the peroxisome biogenesis disorders."; RL Nat. Genet. 9:115-125(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Liver; RX MEDLINE=95310365; PubMed=7790377; DOI=10.1083/jcb.130.1.51; RA Wiemer E.A.C., Nuttley W.M., Bertolaet B.L., Li X., Francke U., RA Wheelock M.J., Anne U.K., Johnson K.R., Subramani S.; RT "Human peroxisomal targeting signal-1 receptor restores peroxisomal RT protein import in cells from patients with fatal peroxisomal RT disorders."; RL J. Cell Biol. 130:51-65(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX MEDLINE=95221441; PubMed=7706321; DOI=10.1074/jbc.270.13.7731; RA Fransen M., Brees C., Baumgart E., Vanhooren J.C., Baes M., RA Mannaerts G.P., van Veldhoven P.P.; RT "Identification and characterization of the putative human peroxisomal RT C-terminal targeting signal import receptor."; RL J. Biol. Chem. 270:7731-7736(1995). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 272-639. RX PubMed=11101887; DOI=10.1038/81930; RA Gatto G.J. Jr., Geisbrecht B.V., Gould S.J., Berg J.M.; RT "Peroxisomal targeting signal-1 recognition by the TPR domains of RT human PEX5."; RL Nat. Struct. Biol. 7:1091-1095(2000). CC -!- FUNCTION: Binds to the C-terminal PTS1-type tripeptide peroxisomal CC targeting signal (SKL-type) and plays an essential role in CC peroxisomal protein import. CC -!- INTERACTION: CC O00623:PEX12; NbExp=2; IntAct=EBI-597835, EBI-594836; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome; peroxisomal membrane; CC peripheral membrane protein. Note=Its distribution appears to be CC dynamic. It is probably a cycling receptor found mainly in the CC cytoplasm and as well associated to the peroxisomal membrane CC through a docking factor (PEX13). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P50542-1; Sequence=Displayed; CC Name=2; CC IsoId=P50542-2; Sequence=VSP_021880; CC -!- DISEASE: Defects in PEX5 are a cause of Zellweger syndrome-1 (ZWS- CC 1) [MIM:214100]. ZWS-1 is a fatal peroxisome biogenesis disorder CC associated with severe abnormalities in the brain, liver and CC kidney. Death occurs soon after birth. This disease is due to CC defective import mechanisms for peroxisomal matrix enzymes. CC -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor CC family. CC -!- SIMILARITY: Contains 7 TPR repeats. CC -!- WEB RESOURCE: NAME=GeneReviews; CC URL="http://www.genetests.org/query?gene=PEX5". CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U19721; AAC50103.1; -; mRNA. DR EMBL; Z48054; CAA88131.1; -; mRNA. DR EMBL; X84899; CAA59324.1; -; mRNA. DR PIR; A56126; A56126. DR PDB; 1FCH; X-ray; A/B=235-602. DR PDB; 2C0L; X-ray; A=-. DR PDB; 2C0M; X-ray; A/B/C/F=-. DR IntAct; P50542; -. DR GermOnline; ENSG00000139197; Homo sapiens. DR Ensembl; ENSG00000139197; Homo sapiens. DR KEGG; hsa:5830; -. DR HGNC; HGNC:9719; PEX5. DR MIM; 202370; phenotype. DR MIM; 214100; phenotype. DR MIM; 600414; gene. DR LinkHub; P50542; -. DR ArrayExpress; P50542; -. DR RZPD-ProtExp; A0787; -. DR RZPD-ProtExp; IOH9796; -. DR RZPD-ProtExp; Z0368; -. DR GO; GO:0005778; C:peroxisomal membrane; TAS:ProtInc. DR GO; GO:0005777; C:peroxisome; TAS:ProtInc. DR GO; GO:0005052; F:peroxisome targeting signal-1 binding; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR InterPro; IPR008940; Prenyl_trans. DR InterPro; IPR011990; TPR-like_helical. DR InterPro; IPR001440; TPR_1. DR InterPro; IPR013026; TPR_region. DR Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1. DR Pfam; PF00515; TPR_1; 4. DR SMART; SM00028; TPR; 4. DR PROSITE; PS50005; TPR; 5. DR PROSITE; PS50293; TPR_REGION; 1. KW 3D-structure; Alternative splicing; Disease mutation; Peroxisome; KW Protein transport; Repeat; TPR repeat; Transport; Zellweger syndrome. FT CHAIN 1 639 Peroxisomal targeting signal 1 receptor. FT /FTId=PRO_0000106305. FT REPEAT 335 368 TPR 1. FT REPEAT 369 402 TPR 2. FT REPEAT 403 436 TPR 3. FT REPEAT 452 485 TPR 4. FT REPEAT 488 521 TPR 5. FT REPEAT 522 555 TPR 6. FT REPEAT 556 589 TPR 7. FT VAR_SEQ 215 251 Missing (in isoform 2). FT /FTId=VSP_021880. FT VARIANT 526 526 N -> K (in NALD). FT /FTId=VAR_007543. FT CONFLICT 425 425 T -> I (in Ref. 1). FT HELIX 318 321 FT TURN 331 334 FT HELIX 338 347 FT TURN 348 349 FT HELIX 351 363 FT TURN 366 367 FT HELIX 369 381 FT TURN 382 383 FT HELIX 385 398 FT TURN 400 401 FT HELIX 403 415 FT TURN 416 417 FT HELIX 419 431 FT TURN 432 432 FT TURN 434 436 FT HELIX 437 439 FT TURN 458 459 FT HELIX 460 481 FT TURN 483 484 FT HELIX 488 500 FT TURN 501 502 FT HELIX 504 517 FT TURN 519 520 FT HELIX 522 534 FT TURN 535 536 FT HELIX 538 551 FT TURN 553 554 FT HELIX 556 569 FT TURN 570 570 FT HELIX 572 587 FT TURN 588 588 FT HELIX 601 614 FT TURN 615 615 FT HELIX 617 619 FT HELIX 620 624 FT TURN 625 626 FT HELIX 628 634 FT TURN 635 636 SQ SEQUENCE 639 AA; 70865 MW; 9D6951F58AED31AC CRC64; MAMRELVEAE CGGANPLMKL AGHFTQDKAL RQEGLRPGPW PPGAPASEAA SKPLGVASED ELVAEFLQDQ NAPLVSRAPQ TFKMDDLLAE MQQIEQSNFR QAPQRAPGVA DLALSENWAQ EFLAAGDAVD VTQDYNETDW SQEFISEVTD PLSVSPARWA EEYLEQSEEK LWLGEPEGTA TDRWYDEYHP EEDLQHTASD FVAKVDDPKL ANSEFLKFVR QIGEGQVSLE SGAGSGRAQA EQWAAEFIQQ QGTSDAWVDQ FTRPVNTSAL DMEFERAKSA IESDVDFWDK LQAELEEMAK RDAEAHPWLS DYDDLTSATY DKGYQFEEEN PLRDHPQPFE EGLRRLQEGD LPNAVLLFEA AVQQDPKHME AWQYLGTTQA ENEQELLAIS ALRRCLELKP DNQTALMALA VSFTNESLQR QACETLRDWL RYTPAYAHLV TPAEEGAGGA GLGPSKRILG SLLSDSLFLE VKELFLAAVR LDPTSIDPDV QCGLGVLFNL SGEYDKAVDC FTAALSVRPN DYLLWNKLGA TLANGNQSEE AVAAYRRALE LQPGYIRSRY NLGISCINLG AHREAVEHFL EALNMQRKSR GPRGEGGAMS ENIWSTLRLA LSMLGQSDAY GAADARDLST LLTMFGLPQ //