ID PEX14_HUMAN Reviewed; 377 AA. AC O75381; B2R7N1; B3KML6; B7Z1N2; Q8WX51; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 194. DE RecName: Full=Peroxisomal membrane protein PEX14 {ECO:0000305}; DE AltName: Full=PTS1 receptor-docking protein; DE AltName: Full=Peroxin-14 {ECO:0000305}; DE AltName: Full=Peroxisomal membrane anchor protein PEX14; GN Name=PEX14 {ECO:0000303|PubMed:9653144, ECO:0000312|HGNC:HGNC:8856}; 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), INTERACTION WITH PEX5 AND PEX13, RP AND FUNCTION. RX PubMed=9653144; DOI=10.1073/pnas.95.14.8087; RA Fransen M., Terlecky S.R., Subramani S.; RT "Identification of a human PTS1 receptor docking protein directly required RT for peroxisomal protein import."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8087-8092(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10212238; DOI=10.1074/jbc.274.18.12593; RA Shimizu N., Itoh R., Hirono Y., Otera H., Ghaedi K., Tateishi K., RA Tamura S., Okumoto K., Harano T., Mukai S., Fujiki Y.; RT "The peroxin Pex14p. cDNA cloning by functional complementation on a RT Chinese hamster ovary cell mutant, characterization, and functional RT analysis."; RL J. Biol. Chem. 274:12593-12604(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, Cerebellum, and Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle; 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 [8] RP PROTEIN SEQUENCE OF 2-34; 184-195 AND 352-363, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lempens A., Norman J.C.; RL Submitted (OCT-2009) to UniProtKB. RN [9] RP INTERACTION WITH PEX19. RX PubMed=10704444; DOI=10.1083/jcb.148.5.931; RA Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.; RT "PEX19 binds multiple peroxisomal membrane proteins, is predominantly RT cytoplasmic, and is required for peroxisome membrane synthesis."; RL J. Cell Biol. 148:931-944(2000). RN [10] RP INTERACTION WITH PEX5. RX PubMed=11438541; DOI=10.1074/jbc.m104647200; RA Saidowsky J., Dodt G., Kirchberg K., Wegner A., Nastainczyk W., RA Kunau W.-H., Schliebs W.; RT "The di-aromatic pentapeptide repeats of the human peroxisome import RT receptor PEX5 are separate high affinity binding sites for the peroxisomal RT membrane protein PEX14."; RL J. Biol. Chem. 276:34524-34529(2001). RN [11] RP INTERACTION WITH PEX5 AND PEX19. RX PubMed=12488033; DOI=10.1016/s0005-2736(02)00635-1; RA Oliveira M.E., Reguenga C., Gouveia A.M., Guimaraes C.P., Schliebs W., RA Kunau W.H., Silva M.T., Sa-Miranda C., Azevedo J.E.; RT "Mammalian Pex14p: membrane topology and characterisation of the Pex14p- RT Pex14p interaction."; RL Biochim. Biophys. Acta 1567:13-22(2002). RN [12] RP INVOLVEMENT IN PBD-CGK AND PBD13A. RX PubMed=15146459; DOI=10.1002/humu.20032; RA Shimozawa N., Tsukamoto T., Nagase T., Takemoto Y., Koyama N., Suzuki Y., RA Komori M., Osumi T., Jeannette G., Wanders R.J., Kondo N.; RT "Identification of a new complementation group of the peroxisome biogenesis RT disorders and PEX14 as the mutated gene."; RL Hum. Mutat. 23:552-558(2004). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP INTERACTION WITH PEX5. RX PubMed=21976670; DOI=10.1074/jbc.m111.287201; RA Freitas M.O., Francisco T., Rodrigues T.A., Alencastre I.S., Pinto M.P., RA Grou C.P., Carvalho A.F., Fransen M., Sa-Miranda C., Azevedo J.E.; RT "PEX5 protein binds monomeric catalase blocking its tetramerization and RT releases it upon binding the N-terminal domain of PEX14."; RL J. Biol. Chem. 286:40509-40519(2011). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [23] RP FUNCTION, AND INTERACTION WITH PEX13 AND PEX5. RX PubMed=28765278; DOI=10.1074/jbc.m117.805044; RA Dias A.F., Rodrigues T.A., Pedrosa A.G., Barros-Barbosa A., Francisco T., RA Azevedo J.E.; RT "The peroxisomal matrix protein translocon is a large cavity-forming RT protein assembly into which PEX5 protein enters to release its cargo."; RL J. Biol. Chem. 292:15287-15300(2017). RN [24] RP STRUCTURE BY NMR OF 16-80 IN COMPLEXES WITH PEX5 AND PEX19, MUTAGENESIS OF RP PHE-52 AND LYS-56, SUBCELLULAR LOCATION, AND INTERACTION WITH PEX5 AND RP PEX19. RX PubMed=19197237; DOI=10.1038/emboj.2009.7; RA Neufeld C., Filipp F.V., Simon B., Neuhaus A., Schueller N., David C., RA Kooshapur H., Madl T., Erdmann R., Schliebs W., Wilmanns M., Sattler M.; RT "Structural basis for competitive interactions of Pex14 with the import RT receptors Pex5 and Pex19."; RL EMBO J. 28:745-754(2009). RN [25] {ECO:0007744|PDB:4BXU} RP STRUCTURE BY NMR OF 16-80 IN COMPLEX WITH PEX5, AND INTERACTION WITH PEX5. RX PubMed=24235149; DOI=10.1074/jbc.m113.499707; RA Neuhaus A., Kooshapur H., Wolf J., Meyer N.H., Madl T., Saidowsky J., RA Hambruch E., Lazam A., Jung M., Sattler M., Schliebs W., Erdmann R.; RT "A novel Pex14 protein-interacting site of human Pex5 is critical for RT matrix protein import into peroxisomes."; RL J. Biol. Chem. 289:437-448(2014). RN [26] RP FUNCTION, AND INTERACTION WITH TUBULIN. RX PubMed=21525035; DOI=10.1242/jcs.079368; RA Bharti P., Schliebs W., Schievelbusch T., Neuhaus A., David C., Kock K., RA Herrmann C., Meyer H.E., Wiese S., Warscheid B., Theiss C., Erdmann R.; RT "PEX14 is required for microtubule-based peroxisome motility in human RT cells."; RL J. Cell Sci. 124:1759-1768(2011). CC -!- FUNCTION: Component of the PEX13-PEX14 docking complex, a translocon CC channel that specifically mediates the import of peroxisomal cargo CC proteins bound to PEX5 receptor (PubMed:9653144, PubMed:24235149, CC PubMed:28765278). The PEX13-PEX14 docking complex forms a large import CC pore which can be opened to a diameter of about 9 nm (By similarity). CC Mechanistically, PEX5 receptor along with cargo proteins associates CC with the PEX14 subunit of the PEX13-PEX14 docking complex in the CC cytosol, leading to the insertion of the receptor into the organelle CC membrane with the concomitant translocation of the cargo into the CC peroxisome matrix (PubMed:24235149, PubMed:28765278). Plays a key role CC for peroxisome movement through a direct interaction with tubulin CC (PubMed:21525035). {ECO:0000250|UniProtKB:P53112, CC ECO:0000269|PubMed:21525035, ECO:0000269|PubMed:24235149, CC ECO:0000269|PubMed:28765278, ECO:0000269|PubMed:9653144}. CC -!- SUBUNIT: Interacts with PEX13; forming the PEX13-PEX14 docking complex CC (PubMed:9653144, PubMed:28765278). Interacts with PEX5 (via WxxxF/Y CC motifs) (PubMed:11438541, PubMed:19197237, PubMed:21976670, CC PubMed:9653144, PubMed:12488033, PubMed:28765278, PubMed:24235149). CC Interacts with PEX19 (PubMed:10704444, PubMed:12488033). Interacts with CC tubulin (PubMed:21525035). {ECO:0000269|PubMed:10704444, CC ECO:0000269|PubMed:11438541, ECO:0000269|PubMed:12488033, CC ECO:0000269|PubMed:19197237, ECO:0000269|PubMed:21525035, CC ECO:0000269|PubMed:21976670, ECO:0000269|PubMed:24235149, CC ECO:0000269|PubMed:28765278, ECO:0000269|PubMed:9653144}. CC -!- INTERACTION: CC O75381; Q9BS16: CENPK; NbExp=3; IntAct=EBI-594898, EBI-6871750; CC O75381; Q9BT78: COPS4; NbExp=3; IntAct=EBI-594898, EBI-742413; CC O75381; O43681: GET3; NbExp=3; IntAct=EBI-594898, EBI-2515857; CC O75381; Q9Y4F3: MARF1; NbExp=3; IntAct=EBI-594898, EBI-5235902; CC O75381; P40855: PEX19; NbExp=26; IntAct=EBI-594898, EBI-594747; CC O75381; P50542: PEX5; NbExp=13; IntAct=EBI-594898, EBI-597835; CC -!- SUBCELLULAR LOCATION: Peroxisome membrane CC {ECO:0000269|PubMed:19197237}; Single-pass membrane protein CC {ECO:0000250|UniProtKB:Q642G4}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75381-1; Sequence=Displayed; CC Name=2; CC IsoId=O75381-2; Sequence=VSP_037021; CC -!- DISEASE: Peroxisome biogenesis disorder complementation group K (PBD- CC CGK) [MIM:614887]: 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 {ECO:0000269|PubMed:15146459}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Peroxisome biogenesis disorder 13A (PBD13A) [MIM:614887]: A CC fatal peroxisome biogenesis disorder belonging to the Zellweger disease CC spectrum and clinically characterized by severe neurologic dysfunction CC with profound psychomotor retardation, severe hypotonia and neonatal CC seizures, craniofacial abnormalities, liver dysfunction, and CC biochemically by the absence of peroxisomes. Additional features CC include cardiovascular and skeletal defects, renal cysts, ocular CC abnormalities, and hearing impairment. Most severely affected CC individuals with the classic form of the disease (classic Zellweger CC syndrome) die within the first year of life. CC {ECO:0000269|PubMed:15146459}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the peroxin-14 family. {ECO:0000305}. 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; AF045186; AAC39843.1; -; mRNA. DR EMBL; AB017546; BAA36837.1; -; mRNA. DR EMBL; AK002194; BAG51028.1; -; mRNA. DR EMBL; AK293684; BAH11568.1; -; mRNA. DR EMBL; AK313046; BAG35878.1; -; mRNA. DR EMBL; CR450321; CAG29317.1; -; mRNA. DR EMBL; CR542083; CAG46880.1; -; mRNA. DR EMBL; AL139423; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL354956; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL591403; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471130; EAW71661.1; -; Genomic_DNA. DR EMBL; BC006327; AAH06327.1; -; mRNA. DR CCDS; CCDS30582.1; -. [O75381-1] DR RefSeq; NP_004556.1; NM_004565.2. [O75381-1] DR RefSeq; XP_011539882.1; XM_011541580.1. [O75381-2] DR PDB; 2W84; NMR; -; A=16-80. DR PDB; 2W85; NMR; -; A=16-80. DR PDB; 4BXU; NMR; -; A=16-80. DR PDBsum; 2W84; -. DR PDBsum; 2W85; -. DR PDBsum; 4BXU; -. DR AlphaFoldDB; O75381; -. DR BMRB; O75381; -. DR SASBDB; O75381; -. DR SMR; O75381; -. DR BioGRID; 111218; 237. DR CORUM; O75381; -. DR ELM; O75381; -. DR IntAct; O75381; 113. DR MINT; O75381; -. DR STRING; 9606.ENSP00000349016; -. DR BindingDB; O75381; -. DR ChEMBL; CHEMBL4523152; -. DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family. DR GlyGen; O75381; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; O75381; -. DR PhosphoSitePlus; O75381; -. DR BioMuta; PEX14; -. DR EPD; O75381; -. DR jPOST; O75381; -. DR MassIVE; O75381; -. DR MaxQB; O75381; -. DR PaxDb; 9606-ENSP00000349016; -. DR PeptideAtlas; O75381; -. DR ProteomicsDB; 49953; -. [O75381-1] DR ProteomicsDB; 49954; -. [O75381-2] DR Pumba; O75381; -. DR TopDownProteomics; O75381-2; -. [O75381-2] DR Antibodypedia; 27930; 355 antibodies from 33 providers. DR DNASU; 5195; -. DR Ensembl; ENST00000356607.9; ENSP00000349016.4; ENSG00000142655.13. [O75381-1] DR GeneID; 5195; -. DR KEGG; hsa:5195; -. DR MANE-Select; ENST00000356607.9; ENSP00000349016.4; NM_004565.3; NP_004556.1. DR UCSC; uc001arn.5; human. [O75381-1] DR AGR; HGNC:8856; -. DR CTD; 5195; -. DR DisGeNET; 5195; -. DR GeneCards; PEX14; -. DR GeneReviews; PEX14; -. DR HGNC; HGNC:8856; PEX14. DR HPA; ENSG00000142655; Low tissue specificity. DR MalaCards; PEX14; -. DR MIM; 601791; gene. DR MIM; 614887; phenotype. DR neXtProt; NX_O75381; -. DR OpenTargets; ENSG00000142655; -. DR Orphanet; 772; Infantile Refsum disease. DR Orphanet; 44; Neonatal adrenoleukodystrophy. DR Orphanet; 912; Zellweger syndrome. DR PharmGKB; PA33198; -. DR VEuPathDB; HostDB:ENSG00000142655; -. DR eggNOG; KOG2629; Eukaryota. DR GeneTree; ENSGT00390000015047; -. DR HOGENOM; CLU_065928_0_0_1; -. DR InParanoid; O75381; -. DR OMA; YNQWQPP; -. DR OrthoDB; 358337at2759; -. DR PhylomeDB; O75381; -. DR TreeFam; TF323535; -. DR PathwayCommons; O75381; -. DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins. DR Reactome; R-HSA-9033241; Peroxisomal protein import. DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import. DR SignaLink; O75381; -. DR SIGNOR; O75381; -. DR BioGRID-ORCS; 5195; 36 hits in 1163 CRISPR screens. DR ChiTaRS; PEX14; human. DR EvolutionaryTrace; O75381; -. DR GeneWiki; PEX14; -. DR GenomeRNAi; 5195; -. DR Pharos; O75381; Tbio. DR PRO; PR:O75381; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; O75381; Protein. DR Bgee; ENSG00000142655; Expressed in bronchial epithelial cell and 196 other cell types or tissues. DR ExpressionAtlas; O75381; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central. DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:HPA. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0048487; F:beta-tubulin binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB. DR GO; GO:0008320; F:protein transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB. DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:UniProt. DR GO; GO:0034453; P:microtubule anchoring; IDA:UniProtKB. DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB. DR GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB. DR GO; GO:0036250; P:peroxisome transport along microtubule; IDA:UniProtKB. DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:UniProtKB. DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IDA:UniProtKB. DR GO; GO:0044721; P:protein import into peroxisome matrix, substrate release; IDA:UniProtKB. DR GO; GO:0016561; P:protein import into peroxisome matrix, translocation; IDA:UniProtKB. DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR025655; PEX14. DR InterPro; IPR006785; Pex14_N. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR PANTHER; PTHR23058; PEROXISOMAL MEMBRANE PROTEIN PEX14; 1. DR PANTHER; PTHR23058:SF0; PEROXISOMAL MEMBRANE PROTEIN PEX14; 1. DR Pfam; PF04695; Pex14_N; 1. DR Genevisible; O75381; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW Membrane; Peroxisome; Peroxisome biogenesis disorder; Phosphoprotein; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport; Zellweger syndrome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712" FT CHAIN 2..377 FT /note="Peroxisomal membrane protein PEX14" FT /id="PRO_0000058325" FT TOPO_DOM 2..108 FT /note="Peroxisomal matrix" FT /evidence="ECO:0000250|UniProtKB:Q642G4" FT TRANSMEM 109..126 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 127..377 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q642G4" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 230..377 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..21 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 244..282 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 319..338 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 339..377 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712" FT MOD_RES 34 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 232 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 282 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q642G4" FT MOD_RES 335 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT VAR_SEQ 58..100 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037021" FT VARIANT 117 FT /note="A -> S (in dbSNP:rs12061667)" FT /id="VAR_051269" FT VARIANT 150 FT /note="A -> S (in dbSNP:rs11539793)" FT /id="VAR_051270" FT VARIANT 320 FT /note="R -> K (in dbSNP:rs12070353)" FT /id="VAR_051271" FT MUTAGEN 52 FT /note="F->A,W: Reduced interaction with PEX19, minor effect FT on interaction with PEX5." FT /evidence="ECO:0000269|PubMed:19197237" FT MUTAGEN 56 FT /note="K->A,E: Reduced interaction with PEX19, minor effect FT on interaction with PEX5." FT /evidence="ECO:0000269|PubMed:19197237" FT CONFLICT 319 FT /note="K -> E (in Ref. 3; BAG51028)" FT /evidence="ECO:0000305" FT STRAND 19..22 FT /evidence="ECO:0007829|PDB:4BXU" FT HELIX 26..36 FT /evidence="ECO:0007829|PDB:2W84" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:2W84" FT HELIX 46..55 FT /evidence="ECO:0007829|PDB:2W84" FT HELIX 60..70 FT /evidence="ECO:0007829|PDB:2W84" SQ SEQUENCE 377 AA; 41237 MW; FED28F62A0B94E7F CRC64; MASSEQAEQP SQPSSTPGSE NVLPREPLIA TAVKFLQNSR VRQSPLATRR AFLKKKGLTD EEIDMAFQQS GTAADEPSSL GPATQVVPVQ PPHLISQPYS PAGSRWRDYG ALAIIMAGIA FGFHQLYKKY LLPLILGGRE DRKQLERMEA GLSELSGSVA QTVTQLQTTL ASVQELLIQQ QQKIQELAHE LAAAKATTST NWILESQNIN ELKSEINSLK GLLLNRRQFP PSPSAPKIPS WQIPVKSPSP SSPAAVNHHS SSDISPVSNE STSSSPGKEG HSPEGSTVTY HLLGPQEEGE GVVDVKGQVR MEVQGEEEKR EDKEDEEDEE DDDVSHVDEE DCLGVQREDR RGGDGQINEQ VEKLRRPEGA SNESERD //