ID F0UIZ3_AJEC8 Unreviewed; 414 AA.
AC F0UIZ3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peroxisomal membrane protein PEX14 {ECO:0000256|ARBA:ARBA00029502, ECO:0000256|RuleBase:RU367032};
DE AltName: Full=Peroxin-14 {ECO:0000256|ARBA:ARBA00029691, ECO:0000256|RuleBase:RU367032};
GN ORFNames=HCEG_05705 {ECO:0000313|EMBL:EGC46490.1}, I7I53_05517
GN {ECO:0000313|EMBL:QSS57116.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|EMBL:EGC46490.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|EMBL:EGC46490.1};
RG The Broad Institute Genome Sequencing Platform;
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QSS57116.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H88 {ECO:0000313|EMBL:QSS57116.1};
RA Voorhies M., Cohen S., Shea T.P., Petrus S., Munoz J.F., Poplawski S.,
RA Goldman W.E., Michael T., Cuomo C.A., Sil A., Beyhan S.;
RT "Chromosome-level genome assembly of a human fungal pathogen reveals
RT clustering of transcriptionally co-regulated genes.";
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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. The PEX13-PEX14 docking complex forms
CC a large import pore which can be opened to a diameter of about 9 nm.
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. {ECO:0000256|RuleBase:RU367032}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000256|RuleBase:RU367032}.
CC -!- SIMILARITY: Belongs to the peroxin-14 family.
CC {ECO:0000256|ARBA:ARBA00005443, ECO:0000256|RuleBase:RU367032}.
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DR EMBL; DS990639; EGC46490.1; -; Genomic_DNA.
DR EMBL; CP069106; QSS57116.1; -; Genomic_DNA.
DR AlphaFoldDB; F0UIZ3; -.
DR VEuPathDB; FungiDB:I7I53_05517; -.
DR HOGENOM; CLU_044743_0_0_1; -.
DR OMA; CDGLIYS; -.
DR Proteomes; UP000008142; Unassembled WGS sequence.
DR Proteomes; UP000663419; Chromosome 5.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IEA:UniProtKB-UniRule.
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:SF5; PEROXISOMAL MEMBRANE PROTEIN PEX14; 1.
DR Pfam; PF04695; Pex14_N; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|RuleBase:RU367032};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140, ECO:0000256|RuleBase:RU367032};
KW Protein transport {ECO:0000256|RuleBase:RU367032};
KW Reference proteome {ECO:0000313|Proteomes:UP000008142};
KW Translocation {ECO:0000256|ARBA:ARBA00023010};
KW Transport {ECO:0000256|RuleBase:RU367032}.
FT DOMAIN 46..89
FT /note="Peroxisome membrane anchor protein Pex14p N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04695"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..148
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 414 AA; 44372 MW; 57D1123AF32C276C CRC64;
MGENLKLKAP AIPSWQLSHS DNNTSNSATA VNAPKVELEK TDSPARETLI EQASVFLEDE
SIRDAPADKK IAFLESKGLE NADIQKLLHV PRSPEATNAG TKSPSISADS VKHIPSSAQL
AHVDASSATS PSPPSNNPSP PTTPTPPIIT YPEFLLHTQK PPPLVTLQGL MYTLYGAGGL
VATLYGASQF LINPMLAELS RARHELAETT QRNLSILNEK LENTVSSIPP PPIHQHSSRH
EQDLIDDDSA SIISDPTELF HRDIATQTSP ELSPNPTLPI DGLNAADLPS SEKTVDTHVK
RLQSISSQLA DYLSEEDNSG ITHSSTEKSL GELKNYLDGL IYNNPSPYLG SNLYRLYNDN
SGSISGNFSD VSEEADAIAA FKAEIRSVKG TLLSARNFPA GGGIRAPVPN TGAR
//
