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Database: UniProt
Entry: G3Y5Y7_ASPNA
LinkDB: G3Y5Y7_ASPNA
Original site: G3Y5Y7_ASPNA 
ID   G3Y5Y7_ASPNA            Unreviewed;       357 AA.
AC   G3Y5Y7;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
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};
DE   Flags: Fragment;
GN   ORFNames=ASPNIDRAFT_183268 {ECO:0000313|EMBL:EHA22002.1};
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA22002.1, ECO:0000313|Proteomes:UP000009038};
RN   [1] {ECO:0000313|EMBL:EHA22002.1, ECO:0000313|Proteomes:UP000009038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC   NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(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. 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHA22002.1}.
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DR   EMBL; ACJE01000013; EHA22002.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3Y5Y7; -.
DR   STRING; 380704.G3Y5Y7; -.
DR   HOGENOM; CLU_045718_0_0_1; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
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:SF0; PEROXISOMAL MEMBRANE PROTEIN PEX14; 1.
DR   Pfam; PF04695; Pex14_N; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367032};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140, ECO:0000256|RuleBase:RU367032};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU367032};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367032}.
FT   DOMAIN          1..34
FT                   /note="Peroxisome membrane anchor protein Pex14p N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04695"
FT   REGION          237..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          166..193
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        239..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EHA22002.1"
SQ   SEQUENCE   357 AA;  37767 MW;  5CC3005D48A9F47D CRC64;
     LQDPSVAASP IEKRVAFLQS KNLTKEEIDV ALARAGEDPS TAAAAVAASS GYQSAPQQVV
     YRPPPPPAAG YGYPPYGQWQ APPEPPKRDW RDWFIMATVM GGVGYGLYTI TKRYISPLIA
     PPTPPQLEQD KEHIDEQFNR AFALIEQLST DTAALKSAEE TRTERLDTAL REVENLVSDM
     KNASRRRDDE TRRISDEVKS LKDAIPKALE GAREGNETRL KELGAELKSL KVLLGNRLGG
     SGNNATSPAP GRFSGMNIPT ASRPAEESTP AAAAPVNGTP AAPASTEQPS QSAQPTPSPS
     TPSMSNSPLS QLGRSASIPA WQMAAANRSK TASPSTPSTS TPDNTTGAAP ESSAPAS
//
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