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Database: UniProt
Entry: W1PG66_AMBTC
LinkDB: W1PG66_AMBTC
Original site: W1PG66_AMBTC 
ID   W1PG66_AMBTC            Unreviewed;       552 AA.
AC   W1PG66;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=AMTR_s00058p00192040 {ECO:0000313|EMBL:ERN06664.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN06664.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
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; KI393888; ERN06664.1; -; Genomic_DNA.
DR   RefSeq; XP_006844989.1; XM_006844926.2.
DR   AlphaFoldDB; W1PG66; -.
DR   STRING; 13333.W1PG66; -.
DR   EnsemblPlants; ERN06664; ERN06664; AMTR_s00058p00192040.
DR   GeneID; 18434863; -.
DR   Gramene; ERN06664; ERN06664; AMTR_s00058p00192040.
DR   KEGG; atr:18434863; -.
DR   eggNOG; KOG2629; Eukaryota.
DR   HOGENOM; CLU_038637_1_0_1; -.
DR   OMA; FHWSHAI; -.
DR   OrthoDB; 358337at2759; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central.
DR   GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0016560; P:protein import into peroxisome matrix, docking; IBA:GO_Central.
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; PF17733; DUF5572; 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:UP000017836};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367032}.
FT   DOMAIN          54..98
FT                   /note="Peroxisome membrane anchor protein Pex14p N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04695"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..473
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  59488 MW;  424D40857C09DFD1 CRC64;
     MATDSSAPGL GNEKAGTPGV EPSKPTGDYE NGANVGATNE NGGKSVFVNS EPMREDQVQN
     AIKFLSHPKV QGSPVVFRRS FLERKGLTKE EIDEAFRRVP DPPSNASTTQ VATSTQEGQL
     QSALTVQPQP PVHTLQPAAV TTMTVPTPQK SGFQWSHIAL AVGLFAASGA CTGLLFKNAV
     VPRLKSWIRK VVSEEDELEK KDQLKPRPID EAAAAAKAAA AAAAEVARAS QEMLHAKNEE
     GKYFEAFTKL LEVQVEEMKT MRNTICNLEG IRENPRVLDQ QISKQFHSES GRPLSAPASI
     QPAGGAPHSQ QFMDVMAMVQ RGEKPPGIRE INDKVPNATQ PLTNSRLVPK SKPWEDTSRV
     QPSSIYISQT ETKVVDSPAS GQGAYYANGS ATQTQYRQPL RNGTPMAEQQ WWKQKPEPNP
     SYSFNPDRGA NVTITEAEPE NDGLQTQHSW APSKESLPRR AWVPPPPPPV AMPEAADAIR
     RPRSSGWVEG AGDERSTSSL GIGVEQDGPS ETGVLGSVKY DNSEVYGGTS AVDEDGSGKG
     LDTIVPLETE AQ
//
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