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Database: UniProt
Entry: S7RW77_GLOTA
LinkDB: S7RW77_GLOTA
Original site: S7RW77_GLOTA 
ID   S7RW77_GLOTA            Unreviewed;       392 AA.
AC   S7RW77;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=GLOTRDRAFT_136081 {ECO:0000313|EMBL:EPQ59120.1};
OS   Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS   rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ59120.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ59120.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ59120.1,
RC   ECO:0000313|Proteomes:UP000030669};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; KB469297; EPQ59120.1; -; Genomic_DNA.
DR   RefSeq; XP_007862191.1; XM_007864000.1.
DR   AlphaFoldDB; S7RW77; -.
DR   STRING; 670483.S7RW77; -.
DR   GeneID; 19303466; -.
DR   KEGG; gtr:GLOTRDRAFT_136081; -.
DR   eggNOG; ENOG502SM68; Eukaryota.
DR   HOGENOM; CLU_058471_0_0_1; -.
DR   OMA; IYYRFLL; -.
DR   OrthoDB; 1647563at2759; -.
DR   Proteomes; UP000030669; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000030669};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367032}.
FT   DOMAIN          33..78
FT                   /note="Peroxisome membrane anchor protein Pex14p N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04695"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   392 AA;  43544 MW;  9CBFF02AD411C9A1 CRC64;
     MSGEDTQPPP SSKIESSSGV PASPSGPAQS GLERNELLAR ARTFLLSPQI KNEDILAKRR
     FLTEKGLTEP EIDGLLRELP SQVQVPQVPP RTYPQPPPSR LPDLLAGILR ISTWVAGGSA
     VLLLVFYRFI LPRLALTYQA RHALRRQQKD LVLRLNKSLE TLKDTQKESY ADIPRSDPFK
     EPPEYRVCRT IDDILTVCED RLDDVPRYTL LRCALAEFTA EGKEPTAQTL FERLRGKIPW
     LDTPEGVTYQ EKIWQMLISS SPFVPSDPSH PESCTWSFNP PPPPQPSSLV SGLSTLQSSL
     PSPPQFPRYQ HTHQALVDFT GYLTTQTYAS STFLRGSGYG VGGAEGNTEE EEVKREIRAL
     KGLVLNRRSF MGSLHRPPSV SAVPPAAPFP TP
//
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