PEX13_HUMAN
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 03-AUG-2022, entry version 191.
DE RecName: Full=Peroxisomal membrane protein PEX13;
DE AltName: Full=Peroxin-13;
GN Name=PEX13;
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].
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.
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 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 [11]
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).
CC -!- FUNCTION: Component of the peroxisomal translocation machinery with
CC PEX14 and PEX17. Functions as a docking factor for the predominantly
CC cytoplasmic PTS1 receptor (PAS10/PEX5). Involved in the import of PTS1
CC and PTS2 proteins.
CC -!- SUBUNIT: Interacts with PEX19. {ECO:0000269|PubMed:10704444,
CC ECO:0000269|PubMed:11390669}.
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
CC {ECO:0000269|PubMed:11390669}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11390669}.
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}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC 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 ---------------------------------------------------------------------------
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_002618.3.
DR AlphaFoldDB; Q92968; -.
DR SMR; Q92968; -.
DR BioGRID; 111217; 34.
DR ELM; Q92968; -.
DR IntAct; Q92968; 15.
DR MINT; Q92968; -.
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 EPD; Q92968; -.
DR jPOST; Q92968; -.
DR MassIVE; Q92968; -.
DR MaxQB; Q92968; -.
DR PaxDb; Q92968; -.
DR PeptideAtlas; Q92968; -.
DR PRIDE; Q92968; -.
DR ProteomicsDB; 75634; -.
DR Antibodypedia; 30577; 118 antibodies from 31 providers.
DR DNASU; 5194; -.
DR Ensembl; ENST00000295030.6; ENSP00000295030.4; ENSG00000162928.9.
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 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 neXtProt; NX_Q92968; -.
DR OpenTargets; ENSG00000162928; -.
DR Orphanet; 772; Infantile Refsum disease.
DR Orphanet; 44; Neonatal adrenoleukodystrophy.
DR Orphanet; 912; Zellweger syndrome.
DR PharmGKB; PA33197; -.
DR VEuPathDB; HostDB:ENSG00000162928; -.
DR eggNOG; KOG3875; Eukaryota.
DR GeneTree; ENSGT00390000016883; -.
DR HOGENOM; CLU_045457_0_0_1; -.
DR InParanoid; Q92968; -.
DR OMA; QPKIRGW; -.
DR OrthoDB; 1085263at2759; -.
DR PhylomeDB; Q92968; -.
DR TreeFam; TF327117; -.
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 BioGRID-ORCS; 5194; 59 hits in 1090 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 174 other tissues.
DR ExpressionAtlas; Q92968; baseline and differential.
DR Genevisible; Q92968; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA: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:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0001967; P:suckling behavior; ISS:UniProtKB.
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; PTHR19332; 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; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Disease variant; Membrane; Peroxisome; Peroxisome biogenesis disorder;
KW Phosphoprotein; Protein transport; Reference proteome; SH3 domain;
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..226
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 REGION 175..196
FT /note="Interaction with PEX19"
FT COMPBIAS 1..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0K1"
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"
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
