ID PEX13_HUMAN Reviewed; 403 AA. AC Q92968; B2RCS1; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 02-SEP-2026, entry version 210. DE RecName: Full=Peroxisomal membrane protein PEX13 {ECO:0000305}; DE AltName: Full=Peroxin-13 {ECO:0000305}; GN Name=PEX13 {ECO:0000303|PubMed:9653144, ECO:0000312|HGNC:HGNC:8855}; 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], 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]. RX PubMed=10441330; DOI=10.1093/hmg/8.9.1673; RA Toyama R., Mukai S., Itagaki A., Tamura S., Shimozawa N., Suzuki Y., RA Kondo N., Wanders R.J., Fujiki Y.; RT "Isolation, characterization and mutation analysis of PEX13-defective RT Chinese hamster ovary cell mutants."; RL Hum. Mol. Genet. 8:1673-1681(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Trachea; 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 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 40-403, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=8858165; DOI=10.1083/jcb.135.1.85; RA Gould S.J., Kalish J.E., Morrell J.C., Bjoerkman J., Urquhart A.J., RA Crane D.I.; RT "Pex13p is an SH3 protein of the peroxisome membrane and a docking factor RT for the predominantly cytoplasmic PTs1 receptor."; RL J. Cell Biol. 135:85-95(1996). RN [7] 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 [8] RP INTERACTION WITH PEX19, AND SUBCELLULAR LOCATION. RX PubMed=11390669; DOI=10.1128/mcb.21.13.4413-4424.2001; RA Fransen M., Wylin T., Brees C., Mannaerts G.P., Van Veldhoven P.P.; RT "Human pex19p binds peroxisomal integral membrane proteins at regions RT distinct from their sorting sequences."; RL Mol. Cell. Biol. 21:4413-4424(2001). RN [9] RP INVOLVEMENT IN PBD11A. RX PubMed=19449432; DOI=10.1002/ajmg.a.32874; RA Al-Dirbashi O.Y., Shaheen R., Al-Sayed M., Al-Dosari M., Makhseed N., RA Abu Safieh L., Santa T., Meyer B.F., Shimozawa N., Alkuraya F.S.; RT "Zellweger syndrome caused by PEX13 deficiency: report of two novel RT mutations."; RL Am. J. Med. Genet. A 149:1219-1223(2009). RN [10] RP FUNCTION, AND INTERACTION WITH PEX14. 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 [11] RP FUNCTION, INTERACTION WITH PEX7, AND MUTAGENESIS OF 10-LYS--GLU-13. RX PubMed=40739340; DOI=10.1038/s41556-025-01711-z; RA Chen W.W., Rodrigues T.A., Wendscheck D., Pedrosa A.G., Yang C., RA Francisco T., Moecklinghoff T., Zografakis A., Nunes-Silva B., RA Avraham R.E., Silva A.R., Ferreira M.J., Das H., Koster J., Neuwirth S., RA Bender J., Oeljeklaus S., Sondhi V., Gatsogiannis C., Schuldiner M., RA Zalckvar E., Hofmann K., Waterham H.R., DeBerardinis R.J., Azevedo J.E., RA Warscheid B.; RT "PEX39 facilitates the peroxisomal import of PTS2-containing proteins."; RL Nat. Cell Biol. 27:1256-1271(2025). RN [12] RP VARIANT PBD11B THR-326. RX PubMed=10441568; DOI=10.1086/302534; RA Liu Y., Bjoerkman J., Urquhart A., Wanders R.J.A., Crane D.I., Gould S.J.; RT "PEX13 is mutated in complementation group 13 of the peroxisome-biogenesis RT disorders."; RL Am. J. Hum. Genet. 65:621-634(1999). RN [13] RP INVOLVEMENT IN PBD11A, AND VARIANT PBD11B THR-326. RX PubMed=10332040; DOI=10.1093/hmg/8.6.1077; RA Shimozawa N., Suzuki Y., Zhang Z., Imamura A., Toyama R., Mukai S., RA Fujiki Y., Tsukamoto T., Osumi T., Orii T., Wanders R.J.A., Kondo N.; RT "Nonsense and temperature-sensitive mutations in PEX13 are the cause of RT complementation group H of peroxisome biogenesis disorders."; RL Hum. Mol. Genet. 8:1077-1083(1999). RN [14] RP VARIANT PBD11B GLY-313. RX PubMed=17041890; DOI=10.1002/humu.9462; RA Krause C., Rosewich H., Thanos M., Gaertner J.; RT "Identification of novel mutations in PEX2, PEX6, PEX10, PEX12, and PEX13 RT in Zellweger spectrum patients."; RL Hum. Mutat. 27:1157-1157(2006). 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:28765278, PubMed:8858165, CC PubMed:9653144). 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:28765278, PubMed:8858165, PubMed:9653144). CC Involved in the import of PTS1- and PTS2-type containing proteins CC (PubMed:8858165, PubMed:9653144). {ECO:0000250|UniProtKB:P80667, CC ECO:0000269|PubMed:28765278, ECO:0000269|PubMed:8858165, CC ECO:0000269|PubMed:9653144}. CC -!- SUBUNIT: Component of the PEX13-PEX14 docking complex, composed of CC PEX13 and PEX14 (PubMed:28765278). Interacts (via SH3 domain) with CC PEX14 (via SH3-binding motif); forming the PEX13-PEX14 docking complex CC (PubMed:28765278). Interacts with PEX19 (PubMed:10704444, CC PubMed:11390669). Interacts (via KPWE motif) with PEX7; this CC interaction is essential for the import of PTS2-containing proteins CC (PubMed:40739340). {ECO:0000269|PubMed:10704444, CC ECO:0000269|PubMed:11390669, ECO:0000269|PubMed:28765278, CC ECO:0000269|PubMed:40739340}. CC -!- INTERACTION: CC Q92968; Q96LK0: CEP19; NbExp=3; IntAct=EBI-594849, EBI-741885; CC Q92968; P40855: PEX19; NbExp=12; IntAct=EBI-594849, EBI-594747; CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:11390669, CC ECO:0000269|PubMed:8858165}; Multi-pass membrane protein {ECO:0000255}. CC -!- DISEASE: Peroxisome biogenesis disorder complementation group 13 (PBD- CC CG13) [MIM:614883]: 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:10332040, ECO:0000269|PubMed:19449432}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Peroxisome biogenesis disorder 11A (PBD11A) [MIM:614883]: 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:10332040, ECO:0000269|PubMed:19449432}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Peroxisome biogenesis disorder 11B (PBD11B) [MIM:614885]: A CC peroxisome biogenesis disorder that includes neonatal CC adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two CC milder manifestations of the Zellweger disease spectrum. The clinical CC course of patients with the NALD and IRD presentation is variable and CC may include developmental delay, hypotonia, liver dysfunction, CC sensorineural hearing loss, retinal dystrophy and vision impairment. CC Children with the NALD presentation may reach their teens, while CC patients with the IRD presentation may reach adulthood. The clinical CC conditions are often slowly progressive in particular with respect to CC loss of hearing and vision. The biochemical abnormalities include CC accumulation of phytanic acid, very long chain fatty acids (VLCFA), CC di- and trihydroxycholestanoic acid and pipecolic acid. CC {ECO:0000269|PubMed:10332040, ECO:0000269|PubMed:10441568, CC ECO:0000269|PubMed:17041890}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the peroxin-13 family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-40 is the initiator. CC {ECO:0000305}. CC -!- CAUTION: There are conflicting reports regarding PEX13 topology, with CC one report placing the C-terminus in the cytosol. CC {ECO:0000269|PubMed:8858165}. 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; AF048755; AAC39844.1; -; mRNA. DR EMBL; AB022192; BAA88907.1; -; mRNA. DR EMBL; AK315244; BAG37668.1; -; mRNA. DR EMBL; CH471053; EAX00018.1; -; Genomic_DNA. DR EMBL; BC067090; AAH67090.1; -; mRNA. DR EMBL; U71374; AAD05572.1; -; mRNA. DR CCDS; CCDS1866.1; -. DR RefSeq; NP_002609.1; NM_002618.4. DR PDB; 7Z0I; X-ray; 1.80 A; A=261-346. DR PDB; 7Z0J; X-ray; 2.30 A; A/B=261-346, A/B=371-383. DR PDB; 7Z0K; X-ray; 2.30 A; A/B=261-346. DR AlphaFoldDB; Q92968; -. DR SMR; Q92968; -. DR BioGRID; 111217; 40. DR ComplexPortal; CPX-10021; Peroxisomal PEX13-PEX14 docking complex. DR ELM; Q92968; -. DR FunCoup; Q92968; 1085. DR IntAct; Q92968; 23. DR MINT; Q92968; -. DR NDEx; MUSIC2-C5213-PEX13; Osteosarcoma (U2OS) cell map - Intracellular trafficking and peroxisomes (28 proteins). DR STRING; 9606.ENSP00000295030; -. DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family. DR iPTMnet; Q92968; -. DR PhosphoSitePlus; Q92968; -. DR BioMuta; PEX13; -. DR DMDM; 3914319; -. DR jPOST; Q92968; -. DR MassIVE; Q92968; -. DR PaxDb; 9606-ENSP00000295030; -. DR PeptideAtlas; Q92968; -. DR ProteomicsDB; 75634; -. DR Pumba; Q92968; -. DR Antibodypedia; 30577; 111 antibodies from 31 providers. DR DNASU; 5194; -. DR Ensembl; ENST00000295030.6; ENSP00000295030.4; ENSG00000162928.10. DR GeneID; 5194; -. DR KEGG; hsa:5194; -. DR MANE-Select; ENST00000295030.6; ENSP00000295030.4; NM_002618.4; NP_002609.1. DR UCSC; uc002sau.5; human. DR AGR; HGNC:8855; -. DR ClinPGx; PA33197; -. DR CTD; 5194; -. DR DisGeNET; 5194; -. DR GeneCards; PEX13; -. DR GeneReviews; PEX13; -. DR HGNC; HGNC:8855; PEX13. DR HPA; ENSG00000162928; Low tissue specificity. DR MalaCards; PEX13; -. DR MIM; 601789; gene. DR MIM; 614883; phenotype. DR MIM; 614885; phenotype. DR OpenTargets; ENSG00000162928; -. DR Orphanet; 772; Infantile Refsum disease. DR Orphanet; 44; Neonatal adrenoleukodystrophy. DR Orphanet; 912; Zellweger syndrome. DR VEuPathDB; HostDB:ENSG00000162928; -. DR eggNOG; KOG3875; Eukaryota. DR GeneTree; ENSGT00390000016883; -. DR HOGENOM; CLU_045457_0_0_1; -. DR InParanoid; Q92968; -. DR OMA; EGWFPKK; -. DR OrthoDB; 10037838at2759; -. DR PAN-GO; Q92968; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q92968; -. DR PathwayCommons; Q92968; -. 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; Q92968; -. DR SIGNOR; Q92968; -. DR Agora; ENSG00000162928; -. DR BioGRID-ORCS; 5194; 61 hits in 1166 CRISPR screens. DR ChiTaRS; PEX13; human. DR GeneWiki; PEX13; -. DR GenomeRNAi; 5194; -. DR Pharos; Q92968; Tbio. DR PRO; PR:Q92968; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q92968; protein. DR Bgee; ENSG00000162928; Expressed in secondary oocyte and 175 other cell types or tissues. DR ExpressionAtlas; Q92968; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:1990429; C:peroxisomal importomer complex; IPI:ComplexPortal. DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0008320; F:transmembrane protein transporter activity; IDA:UniProtKB. DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:UniProt. DR GO; GO:0021795; P:cerebral cortex cell migration; ISS:UniProtKB. DR GO; GO:0001561; P:fatty acid alpha-oxidation; ISS:UniProtKB. DR GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB. DR GO; GO:0060152; P:microtubule-based peroxisome localization; ISS:UniProtKB. DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB. DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IDA:UniProtKB. DR GO; GO:0016561; P:protein import into peroxisome matrix, translocation; IDA:UniProt. DR GO; GO:0001967; P:suckling behavior; ISS:UniProtKB. DR CDD; cd11864; SH3_PEX13_eumet; 1. DR FunFam; 2.30.30.40:FF:000109; Peroxisomal biogenesis factor 13; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR007223; Peroxin-13_N. DR InterPro; IPR035463; Pex13. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR19332; PEROXISOMAL MEMBRANE PROTEIN PEX13; 1. DR PANTHER; PTHR19332:SF1; PEROXISOMAL MEMBRANE PROTEIN PEX13; 1. DR Pfam; PF04088; Peroxin-13_N; 1. DR Pfam; PF14604; SH3_9; 1. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50002; SH3; 1. DR PDBsum; 7Z0I; -. DR PDBsum; 7Z0J; -. DR PDBsum; 7Z0K; -. PE 1: Evidence at protein level; KW 3D-structure; Disease variant; Membrane; Peroxisome; KW Peroxisome biogenesis disorder; Phosphoprotein; Protein transport; KW Proteomics identification; Reference proteome; SH3 domain; Translocation; KW Transmembrane; Transmembrane helix; Transport; Zellweger syndrome. FT CHAIN 1..403 FT /note="Peroxisomal membrane protein PEX13" FT /id="PRO_0000058323" FT TOPO_DOM 1..134 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:D4A2Y9" FT TRANSMEM 135..155 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 156..174 FT /note="Peroxisomal matrix" FT /evidence="ECO:0000305" FT TRANSMEM 175..192 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 193..233 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 234..254 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 255..403 FT /note="Peroxisomal matrix" FT /evidence="ECO:0000305" FT DOMAIN 272..336 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 1..68 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 145..233 FT /note="Targeting to peroxisomes" FT /evidence="ECO:0000269|PubMed:11390669" FT REGION 175..196 FT /note="Interaction with PEX19" FT /evidence="ECO:0000269|PubMed:11390669" FT MOTIF 10..13 FT /note="Required for binding to PEX7" FT /evidence="ECO:0000269|PubMed:40739340" FT COMPBIAS 1..11 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 59..68 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 354 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D0K1" FT VARIANT 313 FT /note="W -> G (in PBD11B; dbSNP:rs61752113)" FT /evidence="ECO:0000269|PubMed:17041890" FT /id="VAR_087140" FT VARIANT 326 FT /note="I -> T (in PBD11B; neonatal adrenoleukodystrophy; FT dbSNP:rs61752115)" FT /evidence="ECO:0000269|PubMed:10332040, FT ECO:0000269|PubMed:10441568" FT /id="VAR_009306" FT MUTAGEN 10..13 FT /note="KPWE->AAAA: Abolishes interaction with PEX7." FT /evidence="ECO:0000269|PubMed:40739340" FT TURN 267..270 FT /evidence="ECO:0007829|PDB:7Z0I" FT STRAND 274..281 FT /evidence="ECO:0007829|PDB:7Z0I" FT STRAND 298..301 FT /evidence="ECO:0007829|PDB:7Z0I" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:7Z0I" FT STRAND 313..321 FT /evidence="ECO:0007829|PDB:7Z0I" FT STRAND 323..327 FT /evidence="ECO:0007829|PDB:7Z0I" FT HELIX 328..330 FT /evidence="ECO:0007829|PDB:7Z0I" FT STRAND 331..337 FT /evidence="ECO:0007829|PDB:7Z0I" FT HELIX 372..378 FT /evidence="ECO:0007829|PDB:7Z0J" SQ SEQUENCE 403 AA; 44130 MW; 1E85BEE04366C01C CRC64; MASQPPPPPK PWETRRIPGA GPGPGPGPTF QSADLGPTLM TRPGQPALTR VPPPILPRPS QQTGSSSVNT FRPAYSSFSS GYGAYGNSFY GGYSPYSYGY NGLGYNRLRV DDLPPSRFVQ QAEESSRGAF QSIESIVHAF ASVSMMMDAT FSAVYNSFRA VLDVANHFSR LKIHFTKVFS AFALVRTIRY LYRRLQRMLG LRRGSENEDL WAESEGTVAC LGAEDRAATS AKSWPIFLFF AVILGGPYLI WKLLSTHSDE VTDSINWASG EDDHVVARAE YDFAAVSEEE ISFRAGDMLN LALKEQQPKV RGWLLASLDG QTTGLIPANY VKILGKRKGR KTVESSKVSK QQQSFTNPTL TKGATVADSL DEQEAAFESV FVETNKVPVA PDSIGKDGEK QDL //