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Database: UniProt
Entry: M2TS85_COCH5
LinkDB: M2TS85_COCH5
Original site: M2TS85_COCH5 
ID   M2TS85_COCH5            Unreviewed;       362 AA.
AC   M2TS85;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-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=COCHEDRAFT_1141504 {ECO:0000313|EMBL:EMD89359.1};
OS   Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD89359.1, ECO:0000313|Proteomes:UP000016936};
RN   [1] {ECO:0000313|EMBL:EMD89359.1, ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(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; KB445579; EMD89359.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2TS85; -.
DR   STRING; 701091.M2TS85; -.
DR   eggNOG; KOG2629; Eukaryota.
DR   HOGENOM; CLU_045718_0_0_1; -.
DR   OMA; YNQWQPP; -.
DR   Proteomes; UP000016936; 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:UP000016936};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367032}.
FT   DOMAIN          3..47
FT                   /note="Peroxisome membrane anchor protein Pex14p N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04695"
FT   REGION          42..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..95
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   362 AA;  38708 MW;  67B3FADC32AB371F CRC64;
     MVREDLITSA VSFLQDPSVA SAPLEKRIAF LQSKNLTQEE IDVSLARAAE DGGQPPPPPQ
     TSAVASNASY RPPPAAPYAS YPPQGYWQPP PPPPEPPKRD WRDYFIMATV MGGVGYGLYF
     TAKRYVLPLI QPPTQPQLEQ DKASVDESFK RAFDLLEQLN TDTTALKASE EARTARLDDA
     LGEVESVLST LKESSKRQGD DNRRIEDDVR GLRDLIPKAL ESHKEATDNR LKELSTELKS
     LKTLIGNRMG STAPRPQNVS GYYGAGQQPS VPQTPNVNGT SSVSTPTPQA PSTPAPAEQA
     NGTSGAGSQA NGLATPSASY SSRMPTGRAA IPAWQMAAAK KTEEAKKDTS ESGTAVEASA
     SS
//
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