PEX14_DICDI
ID PEX14_DICDI Reviewed; 748 AA.
AC Q54C55;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Peroxisomal membrane protein PEX14;
DE AltName: Full=PTS1 receptor-docking protein;
DE AltName: Full=Peroxin-14;
GN Name=pex14; ORFNames=DDB_G0293264;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: May be a component of the peroxisomal translocation
CC machinery. {ECO:0000250|UniProtKB:O75381}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:O75381}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O75381}.
CC -!- SIMILARITY: Belongs to the peroxin-14 family. {ECO:0000305}.
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DR EMBL; AAFI02000200; EAL60831.1; -; Genomic_DNA.
DR RefSeq; XP_629211.1; XM_629209.1.
DR AlphaFoldDB; Q54C55; -.
DR SMR; Q54C55; -.
DR STRING; 44689.DDB0238078; -.
DR PaxDb; Q54C55; -.
DR PRIDE; Q54C55; -.
DR EnsemblProtists; EAL60831; EAL60831; DDB_G0293264.
DR GeneID; 8629090; -.
DR KEGG; ddi:DDB_G0293264; -.
DR dictyBase; DDB_G0293264; pex14.
DR eggNOG; ENOG502R97S; Eukaryota.
DR HOGENOM; CLU_371912_0_0_1; -.
DR InParanoid; Q54C55; -.
DR OMA; LTSNYIM; -.
DR Reactome; R-DDI-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-DDI-9033241; Peroxisomal protein import.
DR Reactome; R-DDI-9603798; Class I peroxisomal membrane protein import.
DR PRO; PR:Q54C55; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990429; C:peroxisomal importomer complex; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; ISS:dictyBase.
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 GO; GO:0006625; P:protein targeting to peroxisome; ISS:dictyBase.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR025655; PEX14.
DR InterPro; IPR006785; Pex14_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR23058; PTHR23058; 1.
DR Pfam; PF04695; Pex14_N; 1.
PE 3: Inferred from homology;
KW Coiled coil; Membrane; Peroxisome; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..748
FT /note="Peroxisomal membrane protein PEX14"
FT /id="PRO_0000371417"
FT TRANSMEM 278..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 8..60
FT /evidence="ECO:0000255"
FT COILED 241..277
FT /evidence="ECO:0000255"
FT COILED 316..413
FT /evidence="ECO:0000255"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 83361 MW; B7FBBE7B477B5237 CRC64;
MDNDDINNNN NNNNNNNNNN NSQELDQQEQ TQEEITKQRI QKRKEEAKRI MEERKKREQQ
PPSQRQYEDV EDDQQQQPIR PIKQLPQRQQ QYDDNDEPPQ QQQYEPKISQ RKVPLPPMKQ
PTTSSTASAA TGSILSPSSN FREDMVKKAV LFLNNPNVKN TALARKVAYL EKKGLTSDEV
KEALKRVETG NINGSSTNNS NITQSNSISR TRNDNYGNNN NNSSNNNNNI QQQQYYQQQQ
QQHQQQQQMA LTQIQSYQKR LEADDQRIAQ LMMNNNRFSW NSFLFSVTAI VGAASGLAYL
TSNYIIPFLN GGKTNKDASA NMDKKITSLQ EEIIKLQSTI IQQGNDFRES TKSLKTLIEQ
QQQQILQQQQ INSVSTTTNS ATSASNSSEI VEIKKELKNL INLIGNKENS NNSNNNSNNS
NNNNGYSKYN GFNGVYNKSS YDDVSTNNNN KTNSPPSPNK PTTTTTTTAT STPGSNISNT
NKTLPPIIKT NPYSHLSWKL PTDQPPVIPS WQQKSSNPPS DLSNANDKSS PSNSNPSTPT
KPYQSSFNYG DVNSFVGGSN TLNFDEKPTT TTTTSTTPSN ERPSSPSVNN NNNNNNNNNN
NNNNNNNNNN NTTIASTSNE SNNSKVETTS NDSDKSTSPS SSSNNTTSTT ATTTTITSAS
TEDNKQQSDE TPYSSDFLDV INQLKQGKTP PGIRTDIDDK PLENSTVTKS AKERPKKPWE
RDTLTSVTNN LSVEETQTIN NTDSSVEK
