ID A0A0C9LT44_9FUNG Unreviewed; 313 AA.
AC A0A0C9LT44;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=MAM1_0039d02828 {ECO:0000313|EMBL:GAN03375.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN03375.1};
RN [1] {ECO:0000313|EMBL:GAN03375.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN03375.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) 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; DF836328; GAN03375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9LT44; -.
DR STRING; 91626.A0A0C9LT44; -.
DR OrthoDB; 72231at2759; -.
DR Proteomes; UP000053815; 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:UP000053815};
KW Translocation {ECO:0000256|ARBA:ARBA00023010};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367032}.
FT TRANSMEM 94..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..46
FT /note="Peroxisome membrane anchor protein Pex14p N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04695"
FT REGION 285..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 313 AA; 35419 MW; AE682EFE9BC61AFB CRC64;
MKEDLITSAV SFLSSANVKT ADRDKKVEFL RKKGLDDQEI EEAFRRVEAA ITPQNQQVTA
ATHVPQLPPR IPYTTTQVVY YPPAPTPRMT NRDIVRHVLV LGMGSFALTA ALTLIIKKFM
SKVFSKIAVY QRDRYQQHAQ QWKRMESALT HHSASTTNDL QLAQEKLDNS LNRLLQSARE
LGQQKQQPYK PLRSTIERFT NSLSHNPLVT NTDTRHQFNY QSGFASSYAD RYQVDTNHNL
TVQSIKSEIR SVKGMLLSRR NFPIVNTAAP SPLISQGFVP PAPTIPSPST YHPRIGRSFR
NQTSTTVEDA SPR
//