SNX4_GIBZE
ID SNX4_GIBZE Reviewed; 460 AA.
AC I1RXT2;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Sorting nexin-4 {ECO:0000250|UniProtKB:P47057};
DE AltName: Full=Autophagy-related protein 24 {ECO:0000303|PubMed:28894236};
GN Name=ATG24 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG091571, FGRAMPH1_01T27793;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28894236; DOI=10.1038/s41598-017-11640-z;
RA Lv W., Wang C., Yang N., Que Y., Talbot N.J., Wang Z.;
RT "Genome-wide functional analysis reveals that autophagy is necessary for
RT growth, sporulation, deoxynivalenol production and virulence in Fusarium
RT graminearum.";
RL Sci. Rep. 7:11062-11062(2017).
CC -!- FUNCTION: Sorting nexin involved in the separation or division of
CC vacuoles throughout the entire life cycle of the cells (By similarity).
CC Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to
CC the trans-Golgi network, for cytoplasm to vacuole transport (Cvt),
CC mitophagy, and pexophagy (By similarity). Autophagy is required for
CC proper vegetative growth, asexual/sexual reproduction, and full
CC virulence (PubMed:28894236). Autophagy is particularly involved in the
CC biosynthesis of deoxynivalenol (DON), an important virulence
CC determinant (PubMed:28894236). {ECO:0000250|UniProtKB:P47057,
CC ECO:0000269|PubMed:28894236}.
CC -!- SUBUNIT: Forms a complex with ATG20 and ATG17 (By similarity).
CC {ECO:0000250|UniProtKB:P47057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47057}.
CC Membrane {ECO:0000250|UniProtKB:P47057}; Peripheral membrane protein.
CC Endosome membrane; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P47057}. Note=Endosome and other perivacuolar
CC punctate structures (By similarity). Associates to phosphatidylinositol
CC 3-phosphate, necessary for peripheral membrane localization to the
CC perivacuolar punctate structures (By similarity).
CC {ECO:0000250|UniProtKB:P47057}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization to the perivacuolar
CC punctate structures. {ECO:0000250|UniProtKB:P47057}.
CC -!- DISRUPTION PHENOTYPE: Significantly decreases the radial growth of
CC colonies under nutrient-rich conditions (PubMed:28894236). Strongly
CC reduces conidiation (PubMed:28894236). Causes only mild infection in
CC point-inoculated spikelets of flowering wheat heads and impairs the
CC spreading to nearby spikelets (PubMed:28894236).
CC {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; HG970335; CEF84195.1; -; Genomic_DNA.
DR RefSeq; XP_011328628.1; XM_011330326.1.
DR AlphaFoldDB; I1RXT2; -.
DR SMR; I1RXT2; -.
DR STRING; 5518.FGSG_09157P0; -.
DR GeneID; 23556120; -.
DR KEGG; fgr:FGSG_09157; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G27793; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_027221_2_0_1; -.
DR InParanoid; I1RXT2; -.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Cytoplasm; Endosome; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..460
FT /note="Sorting nexin-4"
FT /id="PRO_0000443923"
FT DOMAIN 56..178
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 238..266
FT /evidence="ECO:0000255"
FT COILED 306..337
FT /evidence="ECO:0000255"
FT COILED 374..403
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 52478 MW; 43D2E5D147601DC7 CRC64;
MTATEQQQDD FSNVSWSEHV HDQQTRSVPD AEEPGHDMNA PGTGLERDAP SLGNEKLECT
VDTPIKENDG TKDAFVSYLI TTHSTFSSFQ RSTTTVRRRF TDFVFLYKQL TRDYPAAAVP
PLPDKQRMEY VRGDRFGSDF TTRRANSLQR FLSRLSLHPT LRRAPILHTF LESPDWNATM
RSRGSRVSSA SDPGSAGVFD NFADTFINAF TKLHRPDRRF LEVKEKSDKL DDDLGHIEKV
IARVARREAD LEVDLRDLAE QFQKLIPLEP HVEPAVHGFS ASIEDTASHL RKLKDMTDQD
YLGSLRDMQA YSIALKNLLK AREQKQLDYE QLTEYLNKST TERDTLQSGH GGGSGAGSFL
RAKIEDVRGV DHEQARRERT RKLELRVEEL THEVESARKT SDMFDDEVVK EVADFERIKR
IEMKAQLGSL ADSHIEFYGE VASIWEKYVE EMEKQGITSA
