ID G0UV37_TRYCI Unreviewed; 361 AA.
AC G0UV37;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=TCIL3000_10_100 {ECO:0000313|EMBL:CCC93251.1};
OS Trypanosoma congolense (strain IL3000).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCC93251.1};
RN [1] {ECO:0000313|EMBL:CCC93251.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IL3000 {ECO:0000313|EMBL:CCC93251.1};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(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; HE575323; CCC93251.1; -; Genomic_DNA.
DR AlphaFoldDB; G0UV37; -.
DR VEuPathDB; TriTrypDB:TcIL3000_10_100; -.
DR OrthoDB; 129678at2759; -.
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 Translocation {ECO:0000256|ARBA:ARBA00023010};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367032}.
FT DOMAIN 26..67
FT /note="Peroxisome membrane anchor protein Pex14p N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04695"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 361 AA; 39784 MW; 538871D0F17CC4E2 CRC64;
MSGLLSGSVH ELKPNSEMGH EPQKKAQRIA NAVEFLLDPR VKNASTANKV RFLKSKNLSA
EEICEAFVKC GQPKSLEEIK MLVNNQPYAS ALPTSQNTSL PVGEDVGTSE TSHSRHAGAP
LYVPQVPPLP EAQSLGRTMD WRDYVIAVGT ALAGSFAAFK AFQTYSPYEF RLKEEKEKPR
RRRSRNRRHI SSDSDTERAH ERRAASALPN PLPSVPTETK SVDKDAELER LKTELKETQE
ALEAEKKSKA ELSITLGKLR GQVNAYSRAN EKQEEKIKSL QEELTKLKTE AEKRDESSRV
VDGEINDKPP SLGGSFHAEN EKGLSGNLNE LSGEVAEETA QNLGTADPSN GEKEPLLGDE
V
//
