ATG37_GIBZE
ID ATG37_GIBZE Reviewed; 295 AA.
AC I1RMK9;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Autophagy-related protein 37 {ECO:0000303|PubMed:28894236};
GN Name=ATG37 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG05200, FGRAMPH1_01T17347;
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, 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: Acyl-CoA binding protein which acts as the peroxisome
CC receptor for pexophagy (By similarity). Required for both
CC micropexophagy and macropexophagy, but not for the cytoplasm to vacuole
CC transport (Cvt) or autophagy pathways (By similarity). Required for
CC functional micropexophagic apparatus (MIPA) and relocation of ATG11 to
CC the peroxisome-sequestering arms of the vacuole (By similarity). Binds
CC palmytoyl-CoA but not oleyl-CoA (By similarity).
CC {ECO:0000250|UniProtKB:C4R8D7}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:C4R8D7}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:C4R8D7}.
CC -!- DISRUPTION PHENOTYPE: Does not significantly decrease the growth rate
CC under nutrient-rich conditions (PubMed:28894236).
CC {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the ATG37 family. {ECO:0000305}.
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DR EMBL; HG970334; CEF87250.1; -; Genomic_DNA.
DR RefSeq; XP_011323708.1; XM_011325406.1.
DR AlphaFoldDB; I1RMK9; -.
DR SMR; I1RMK9; -.
DR STRING; 5518.FGSG_05200P0; -.
DR GeneID; 23552392; -.
DR KEGG; fgr:FGSG_05200; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G17347; -.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_043304_1_0_1; -.
DR InParanoid; I1RMK9; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.80.10; -; 1.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR Pfam; PF00887; ACBP; 1.
DR SUPFAM; SSF47027; SSF47027; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 3: Inferred from homology;
KW Autophagy; Glycoprotein; Lipid-binding; Membrane; Peroxisome;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..295
FT /note="Autophagy-related protein 37"
FT /id="PRO_0000443930"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 5..103
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REGION 124..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 295 AA; 33814 MW; 0A8FCB878A3A40AF CRC64;
MADSVDRVFV HALNTVKKIP KTGASRPPPT DRLRLYGLYK QAMEGDVDGV MERPTAASGL
ASDELQREKD KWDAWNLQKG LSRTESKRRY IEALIDTMHR YATTPDAEEL VSELEFVWNQ
IKDNSPSSSL SSPRPNQSTG AGAQQPQQEP EQASDGEGPL KELRPMSEYD EAELRSQRQV
DLEDDEVDVP TSDRSSGRWQ RKVERALTTM SAEVAALREQ IMTGREWRTK KERSVPAWVK
WFAWLLVKHI FADLVILSVV LLWLRKRKDQ RLEDIVRAGV RLMREYVRNV LPSRG
