P50542 (PEX5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxisomal targeting signal 1 receptor
Short name=PTS1 receptor
Short name=PTS1R

Alternative name(s):
PTS1-BP
Peroxin-5
Peroxisomal C-terminal targeting signal import receptor
Peroxisome receptor 1

Gene names

Name:	PEX5
Synonyms:	PXR1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	639 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to the C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) and plays an essential role in peroxisomal protein import. Ref.1 Ref.2 Ref.3
Subunit structure	Interacts with PEX7 and PEX13 By similarity. Interacts with PEX12 and PEX14. Interacts (Cys-linked ubiquitinated) with ZFAND6. Ref.8 Ref.9 Ref.10
Subcellular location	Cytoplasm. Peroxisome membrane; Peripheral membrane protein. Note: Its distribution appears to be dynamic. It is probably a cycling receptor found mainly in the cytoplasm and as well associated to the peroxisomal membrane through a docking factor (PEX13). Ref.1 Ref.3
Tissue specificity	Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Ref.1 Ref.2 Ref.3
Involvement in disease	Peroxisome biogenesis disorder 2A (PBD2A) [MIM:214110]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and characterized clinically by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Peroxisome biogenesis disorder 2B (PBD2B) [MIM:202370]: A peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.15
Sequence similarities	Belongs to the peroxisomal targeting signal receptor family. Contains 7 TPR repeats.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Membrane Peroxisome
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Peroxisome biogenesis disorder Zellweger syndrome
Domain	Repeat TPR repeat
PTM	Thioester bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell development Inferred from electronic annotation. Source: Compara cerebral cortex cell migration Inferred from electronic annotation. Source: Compara cerebral cortex neuron differentiation Inferred from electronic annotation. Source: Compara endoplasmic reticulum organization Inferred from electronic annotation. Source: Compara fatty acid beta-oxidation Inferred from electronic annotation. Source: Compara mitochondrial membrane organization Inferred from electronic annotation. Source: Compara negative regulation of protein homotetramerization Inferred from direct assay PubMed 21976670. Source: UniProtKB neuromuscular process Inferred from electronic annotation. Source: Compara neuron migration Inferred from electronic annotation. Source: Compara positive regulation of multicellular organism growth Inferred from electronic annotation. Source: Compara protein import into peroxisome matrix Inferred from genetic interaction PubMed 11931631. Source: UniProtKB protein import into peroxisome matrix, docking Inferred from direct assay PubMed 21976670. Source: UniProtKB protein import into peroxisome matrix, translocation Inferred from direct assay PubMed 11336669Ref.1. Source: UniProtKB protein import into peroxisome membrane Inferred from mutant phenotype PubMed 14709540. Source: UniProtKB protein tetramerization Inferred from direct assay PubMed 12456682. Source: UniProtKB very long-chain fatty acid metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA cytosol Inferred from direct assay PubMed 11336669Ref.1. Source: UniProtKB mitochondrion Inferred from electronic annotation. Source: Compara peroxisomal matrix Inferred from direct assay PubMed 11336669. Source: UniProtKB peroxisomal membrane Inferred from direct assay PubMed 21525035PubMed 21525035. Source: UniProtKB protein complex Inferred from direct assay PubMed 19584060. Source: UniProtKB
Molecular_function	peroxisome matrix targeting signal-1 binding Inferred from direct assay PubMed 10514471PubMed 11463335PubMed 12456682Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PEX12	O00623	3	EBI-597835,EBI-594836

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P50542-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P50542-2)

The sequence of this isoform differs from the canonical sequence as follows:
     215-251: Missing.

Isoform 3 (identifier: P50542-3)

The sequence of this isoform differs from the canonical sequence as follows:
     283-290: Missing.

Isoform 4 (identifier: P50542-4)

The sequence of this isoform differs from the canonical sequence as follows:
     45-45: P → PASEAVSVLEVESPGA

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 639

639

Peroxisomal targeting signal 1 receptor

PRO_0000106305

Regions

Repeat

335 – 368

34

TPR 1

Repeat

369 – 402

34

TPR 2

Repeat

403 – 436

34

TPR 3

Repeat

452 – 485

34

TPR 4

Repeat

488 – 521

34

TPR 5

Repeat

522 – 555

34

TPR 6

Repeat

556 – 589

34

TPR 7

Amino acid modifications

Cross-link

11

Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence

45

1

P → PASEAVSVLEVESPGA in isoform 4.

VSP_043639

Alternative sequence

215 – 251

37

Missing in isoform 2.

VSP_021880

Alternative sequence

283 – 290

8

Missing in isoform 3.

VSP_024106

Natural variant

526

1

N → K in PBD2B; neonatal adrenoleukodystrophy; strongly affects peroxisomal protein import. Ref.1 Ref.15

VAR_007543

Natural variant

600

1

S → W in PBD2B; infantile Refsum disease; mildly affects peroxisomal protein import. Ref.15

VAR_031328

Experimental info

Mutagenesis

118

1

W → A: Strongly reduced interaction with PEX14. Ref.9

Mutagenesis

122

1

F → A: Strongly reduced interaction with PEX14. Ref.9

Sequence conflict

425

1

T → I in AAC50103. Ref.1

Secondary structure

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639

Helix Strand Turn

Details...

Helix

109 – 124

16

Helix

318 – 321

4

Turn

331 – 334

4

Helix

338 – 347

10

Helix

351 – 363

13

Helix

369 – 381

13

Helix

385 – 398

14

Helix

403 – 415

13

Helix

419 – 431

13

Turn

434 – 436

3

Helix

437 – 439

3

Helix

460 – 481

22

Helix

488 – 500

13

Helix

504 – 517

14

Helix

522 – 534

13

Helix

538 – 551

14

Helix

556 – 569

14

Helix

572 – 587

16

Beta strand

593 – 595

3

Helix

601 – 614

14

Helix

617 – 619

3

Helix

620 – 624

5

Helix

628 – 634

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 12, 2006. Version 3. Checksum: 9D6951F58AED31AC	FASTA	639	70,865
	10 20 30 40 50 60 MAMRELVEAE CGGANPLMKL AGHFTQDKAL RQEGLRPGPW PPGAPASEAA SKPLGVASED 70 80 90 100 110 120 ELVAEFLQDQ NAPLVSRAPQ TFKMDDLLAE MQQIEQSNFR QAPQRAPGVA DLALSENWAQ 130 140 150 160 170 180 EFLAAGDAVD VTQDYNETDW SQEFISEVTD PLSVSPARWA EEYLEQSEEK LWLGEPEGTA 190 200 210 220 230 240 TDRWYDEYHP EEDLQHTASD FVAKVDDPKL ANSEFLKFVR QIGEGQVSLE SGAGSGRAQA 250 260 270 280 290 300 EQWAAEFIQQ QGTSDAWVDQ FTRPVNTSAL DMEFERAKSA IESDVDFWDK LQAELEEMAK 310 320 330 340 350 360 RDAEAHPWLS DYDDLTSATY DKGYQFEEEN PLRDHPQPFE EGLRRLQEGD LPNAVLLFEA 370 380 390 400 410 420 AVQQDPKHME AWQYLGTTQA ENEQELLAIS ALRRCLELKP DNQTALMALA VSFTNESLQR 430 440 450 460 470 480 QACETLRDWL RYTPAYAHLV TPAEEGAGGA GLGPSKRILG SLLSDSLFLE VKELFLAAVR 490 500 510 520 530 540 LDPTSIDPDV QCGLGVLFNL SGEYDKAVDC FTAALSVRPN DYLLWNKLGA TLANGNQSEE 550 560 570 580 590 600 AVAAYRRALE LQPGYIRSRY NLGISCINLG AHREAVEHFL EALNMQRKSR GPRGEGGAMS 610 620 630 ENIWSTLRLA LSMLGQSDAY GAADARDLST LLTMFGLPQ
	Isoform 2 [UniParc]. Checksum: EA4E6FAAF5E11C55	FASTA	602	66,830
	10 20 30 40 50 60 MAMRELVEAE CGGANPLMKL AGHFTQDKAL RQEGLRPGPW PPGAPASEAA SKPLGVASED 70 80 90 100 110 120 ELVAEFLQDQ NAPLVSRAPQ TFKMDDLLAE MQQIEQSNFR QAPQRAPGVA DLALSENWAQ 130 140 150 160 170 180 EFLAAGDAVD VTQDYNETDW SQEFISEVTD PLSVSPARWA EEYLEQSEEK LWLGEPEGTA 190 200 210 220 230 240 TDRWYDEYHP EEDLQHTASD FVAKVDDPKL ANSEGTSDAW VDQFTRPVNT SALDMEFERA 250 260 270 280 290 300 KSAIESDVDF WDKLQAELEE MAKRDAEAHP WLSDYDDLTS ATYDKGYQFE EENPLRDHPQ 310 320 330 340 350 360 PFEEGLRRLQ EGDLPNAVLL FEAAVQQDPK HMEAWQYLGT TQAENEQELL AISALRRCLE 370 380 390 400 410 420 LKPDNQTALM ALAVSFTNES LQRQACETLR DWLRYTPAYA HLVTPAEEGA GGAGLGPSKR 430 440 450 460 470 480 ILGSLLSDSL FLEVKELFLA AVRLDPTSID PDVQCGLGVL FNLSGEYDKA VDCFTAALSV 490 500 510 520 530 540 RPNDYLLWNK LGATLANGNQ SEEAVAAYRR ALELQPGYIR SRYNLGISCI NLGAHREAVE 550 560 570 580 590 600 HFLEALNMQR KSRGPRGEGG AMSENIWSTL RLALSMLGQS DAYGAADARD LSTLLTMFGL PQ
	Isoform 3 [UniParc]. Checksum: 9F3B705D888C484B	FASTA	631	69,872
	10 20 30 40 50 60 MAMRELVEAE CGGANPLMKL AGHFTQDKAL RQEGLRPGPW PPGAPASEAA SKPLGVASED 70 80 90 100 110 120 ELVAEFLQDQ NAPLVSRAPQ TFKMDDLLAE MQQIEQSNFR QAPQRAPGVA DLALSENWAQ 130 140 150 160 170 180 EFLAAGDAVD VTQDYNETDW SQEFISEVTD PLSVSPARWA EEYLEQSEEK LWLGEPEGTA 190 200 210 220 230 240 TDRWYDEYHP EEDLQHTASD FVAKVDDPKL ANSEFLKFVR QIGEGQVSLE SGAGSGRAQA 250 260 270 280 290 300 EQWAAEFIQQ QGTSDAWVDQ FTRPVNTSAL DMEFERAKSA IELQAELEEM AKRDAEAHPW 310 320 330 340 350 360 LSDYDDLTSA TYDKGYQFEE ENPLRDHPQP FEEGLRRLQE GDLPNAVLLF EAAVQQDPKH 370 380 390 400 410 420 MEAWQYLGTT QAENEQELLA ISALRRCLEL KPDNQTALMA LAVSFTNESL QRQACETLRD 430 440 450 460 470 480 WLRYTPAYAH LVTPAEEGAG GAGLGPSKRI LGSLLSDSLF LEVKELFLAA VRLDPTSIDP 490 500 510 520 530 540 DVQCGLGVLF NLSGEYDKAV DCFTAALSVR PNDYLLWNKL GATLANGNQS EEAVAAYRRA 550 560 570 580 590 600 LELQPGYIRS RYNLGISCIN LGAHREAVEH FLEALNMQRK SRGPRGEGGA MSENIWSTLR 610 620 630 LALSMLGQSD AYGAADARDL STLLTMFGLP Q
	Isoform 4 [UniParc]. Checksum: CF2055CBD6902BFE	FASTA	654	72,291
	10 20 30 40 50 60 MAMRELVEAE CGGANPLMKL AGHFTQDKAL RQEGLRPGPW PPGAPASEAV SVLEVESPGA 70 80 90 100 110 120 ASEAASKPLG VASEDELVAE FLQDQNAPLV SRAPQTFKMD DLLAEMQQIE QSNFRQAPQR 130 140 150 160 170 180 APGVADLALS ENWAQEFLAA GDAVDVTQDY NETDWSQEFI SEVTDPLSVS PARWAEEYLE 190 200 210 220 230 240 QSEEKLWLGE PEGTATDRWY DEYHPEEDLQ HTASDFVAKV DDPKLANSEF LKFVRQIGEG 250 260 270 280 290 300 QVSLESGAGS GRAQAEQWAA EFIQQQGTSD AWVDQFTRPV NTSALDMEFE RAKSAIESDV 310 320 330 340 350 360 DFWDKLQAEL EEMAKRDAEA HPWLSDYDDL TSATYDKGYQ FEEENPLRDH PQPFEEGLRR 370 380 390 400 410 420 LQEGDLPNAV LLFEAAVQQD PKHMEAWQYL GTTQAENEQE LLAISALRRC LELKPDNQTA 430 440 450 460 470 480 LMALAVSFTN ESLQRQACET LRDWLRYTPA YAHLVTPAEE GAGGAGLGPS KRILGSLLSD 490 500 510 520 530 540 SLFLEVKELF LAAVRLDPTS IDPDVQCGLG VLFNLSGEYD KAVDCFTAAL SVRPNDYLLW 550 560 570 580 590 600 NKLGATLANG NQSEEAVAAY RRALELQPGY IRSRYNLGIS CINLGAHREA VEHFLEALNM 610 620 630 640 650 QRKSRGPRGE GGAMSENIWS TLRLALSMLG QSDAYGAADA RDLSTLLTMF GLPQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 of the peroxisome biogenesis disorders." Dodt G., Braverman N., Wong C., Moser A., Moser H.W., Watkins P., Valle D., Gould S.J. Nat. Genet. 9:115-125(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INVOLVEMENT IN PBD2A, VARIANT PBD2B LYS-526, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	"Human peroxisomal targeting signal-1 receptor restores peroxisomal protein import in cells from patients with fatal peroxisomal disorders." Wiemer E.A.C., Nuttley W.M., Bertolaet B.L., Li X., Francke U., Wheelock M.J., Anne U.K., Johnson K.R., Subramani S. J. Cell Biol. 130:51-65(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY. Tissue: Liver.
[3]	"Identification and characterization of the putative human peroxisomal C-terminal targeting signal import receptor." Fransen M., Brees C., Baumgart E., Vanhooren J.C.T., Baes M., Mannaerts G.P., van Veldhoven P.P. J. Biol. Chem. 270:7731-7736(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: Liver.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4). Tissue: Testis.
[5]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Eye.
[8]	"PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor docking in peroxisomal matrix protein import." Chang C.C., Warren D.S., Sacksteder K.A., Gould S.J. J. Cell Biol. 147:761-774(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PEX12.
[9]	"The di-aromatic pentapeptide repeats of the human peroxisome import receptor PEX5 are separate high affinity binding sites for the peroxisomal membrane protein PEX14." Saidowsky J., Dodt G., Kirchberg K., Wegner A., Nastainczyk W., Kunau W.-H., Schliebs W. J. Biol. Chem. 276:34524-34529(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PEX14, MUTAGENESIS OF TRP-118 AND PHE-122.
[10]	"AWP1/ZFAND6 functions in Pex5 export by interacting with cys-monoubiquitinated Pex5 and Pex6 AAA ATPase." Miyata N., Okumoto K., Mukai S., Noguchi M., Fujiki Y. Traffic 13:168-183(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ZFAND6.
[11]	"Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5." Gatto G.J. Jr., Geisbrecht B.V., Gould S.J., Berg J.M. Nat. Struct. Biol. 7:1091-1095(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 272-639 IN COMPLEX WITH TARGETING PEPTIDE.
[12]	"Recognition of a functional peroxisome type 1 target by the dynamic import receptor Pex5p." Stanley W.A., Filipp F.V., Kursula P., Schueller N., Erdmann R., Schliebs W., Sattler M., Wilmanns M. Mol. Cell 24:653-663(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 321-639 IN COMPLEX WITH TARGETING PEPTIDE.
[13]	"A previously unobserved conformation for the human Pex5p receptor suggests roles for intrinsic flexibility and rigid domain motions in ligand binding." Stanley W.A., Pursiainen N.V., Garman E.F., Juffer A.H., Wilmanns M., Kursula P. BMC Struct. Biol. 7:24-24(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 315-639, BINDING TO C-TERMINAL TARGETING PEPTIDES.
[14]	"Structural basis for competitive interactions of Pex14 with the import receptors Pex5 and Pex19." Neufeld C., Filipp F.V., Simon B., Neuhaus A., Schueller N., David C., Kooshapur H., Madl T., Erdmann R., Schliebs W., Wilmanns M., Sattler M. EMBO J. 28:745-754(2009) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 108-127 IN COMPLEX WITH PEX14.
[15]	"Functional heterogeneity of C-terminal peroxisome targeting signal 1 in PEX5-defective patients." Shimozawa N., Zhang Z., Suzuki Y., Imamura A., Tsukamoto T., Osumi T., Fujiki Y., Orii T., Barth P.G., Wanders R.J., Kondo N. Biochem. Biophys. Res. Commun. 262:504-508(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PBD2B LYS-526 AND TRP-600, CHARACTERIZATION OF VARIANTS PBD2B LYS-526 AND TRP-600.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U19721 mRNA. Translation: AAC50103.1.
Z48054 mRNA. Translation: CAA88131.1.
X84899 mRNA. Translation: CAA59324.1.
AK292256 mRNA. Translation: BAF84945.1.
AK302742 mRNA. Translation: BAG63957.1.
AK316250 mRNA. Translation: BAH14621.1.
AC018653 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88671.1.
CH471116 Genomic DNA. Translation: EAW88674.1.
CH471116 Genomic DNA. Translation: EAW88672.1.
BC010621 mRNA. Translation: AAH10621.1.

IPI

IPI00032931.
IPI00165272.
IPI00384805.
IPI00940679.

PIR

A56126.

RefSeq

NP_000310.2. NM_000319.4.
NP_001124495.1. NM_001131023.1.
NP_001124496.1. NM_001131024.1.
NP_001124497.1. NM_001131025.1.
NP_001124498.1. NM_001131026.1.

UniGene

Hs.567327.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FCH	X-ray	2.20	A/B	272-639	[»]
2C0L	X-ray	2.30	A	335-639	[»]
2C0M	X-ray	2.50	A/B/C/F	321-639	[»]
2J9Q	X-ray	2.65	A/B	315-639	[»]
2W84	NMR	-	B	108-127	[»]
3R9A	X-ray	2.35	B/D	315-639	[»]

ProteinModelPortal

P50542.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34654N.

IntAct

P50542. 17 interactions.

MINT

MINT-241634.

STRING

9606.ENSP00000407401.

PTM databases

PhosphoSite

P50542.

Polymorphism databases

DMDM

119364633.

Proteomic databases

PaxDb

P50542.

PRIDE

P50542.

Protocols and materials databases

DNASU

5830.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000266563; ENSP00000266563; ENSG00000139197.
ENST00000266564; ENSP00000266564; ENSG00000139197.
ENST00000420616; ENSP00000410159; ENSG00000139197.
ENST00000434354; ENSP00000407401; ENSG00000139197.
ENST00000455147; ENSP00000400647; ENSG00000139197.

GeneID

5830.

KEGG

hsa:5830.

UCSC

uc001qsu.3. human.
uc001qsv.3. human.
uc001qsw.3. human.

Organism-specific databases

CTD

5830.

GeneCards

GC12P007341.

HGNC

HGNC:9719. PEX5.

HPA

HPA039259.

MIM

202370. phenotype.
214110. phenotype.
600414. gene.

neXtProt

NX_P50542.

Orphanet

772. Infantile Refsum disease.
44. Neonatal adrenoleukodystrophy.
912. Zellweger syndrome.

PharmGKB

PA34063.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0457.

HOGENOM

HOG000158146.

HOVERGEN

HBG053575.

InParanoid

P50542.

KO

K13342.

OrthoDB

EOG42V8FQ.

Gene expression databases

ArrayExpress

P50542.

Bgee

P50542.

CleanEx

HS_PEX5.

Genevestigator

P50542.

GermOnline

ENSG00000139197. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.10. 2 hits.

InterPro

IPR024111. PTS1R_family.
IPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

PANTHER

PTHR10130. PTHR10130. 1 hit.

Pfam

PF00515. TPR_1. 3 hits.
[Graphical view]

SMART

SM00028. TPR. 4 hits.
[Graphical view]

PROSITE

PS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PEX5. human.

EvolutionaryTrace

P50542.

GenomeRNAi

5830.

NextBio

22716.

SOURCE

Search...

Entry information

Entry name

PEX5_HUMAN

Accession

Primary (citable) accession number: P50542
Secondary accession number(s): A8K891 , B4DZ45, B7ZAD5, D3DUT8, Q15115, Q15266, Q96FN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 12, 2006
Last modified:	May 1, 2013
This is version 142 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.