ID B2AY80_PODAN Unreviewed; 635 AA.
AC B2AY80;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Vacuolar fusion protein MON1 {ECO:0000256|ARBA:ARBA00018132, ECO:0000256|RuleBase:RU367048};
GN ORFNames=PODANS_1_10180 {ECO:0000313|EMBL:CAP69354.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP69354.1};
RN [1] {ECO:0000313|EMBL:CAP69354.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP69354.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP69354.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP69354.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP23374.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for multiple vacuole delivery pathways including the
CC cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and
CC endocytosis. {ECO:0000256|ARBA:ARBA00003063,
CC ECO:0000256|RuleBase:RU367048}.
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC {ECO:0000256|RuleBase:RU367048}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU367048}. Prevacuolar compartment membrane
CC {ECO:0000256|ARBA:ARBA00004380, ECO:0000256|RuleBase:RU367048};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004380,
CC ECO:0000256|RuleBase:RU367048}. Vacuole membrane
CC {ECO:0000256|RuleBase:RU367048}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU367048}.
CC -!- SIMILARITY: Belongs to the MON1/SAND family.
CC {ECO:0000256|RuleBase:RU367048}.
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DR EMBL; CU633901; CAP69354.1; -; Genomic_DNA.
DR EMBL; FO904936; CDP23374.1; -; Genomic_DNA.
DR RefSeq; XP_001908681.1; XM_001908646.1.
DR AlphaFoldDB; B2AY80; -.
DR STRING; 515849.B2AY80; -.
DR GeneID; 6193080; -.
DR KEGG; pan:PODANSg5716; -.
DR VEuPathDB; FungiDB:PODANS_1_10180; -.
DR eggNOG; KOG0997; Eukaryota.
DR HOGENOM; CLU_014574_5_0_1; -.
DR OrthoDB; 73361at2759; -.
DR Proteomes; UP000001197; Chromosome 1.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-UniRule.
DR GO; GO:0006623; P:protein targeting to vacuole; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR InterPro; IPR043972; FUZ/MON1/HPS1_longin_1.
DR InterPro; IPR043971; FUZ/MON1/HPS1_longin_2.
DR InterPro; IPR043970; FUZ/MON1/HPS1_longin_3.
DR InterPro; IPR004353; Mon1.
DR PANTHER; PTHR13027; SAND PROTEIN-RELATED; 1.
DR PANTHER; PTHR13027:SF7; VACUOLAR FUSION PROTEIN MON1 HOMOLOG; 1.
DR Pfam; PF19036; Fuz_longin_1; 1.
DR Pfam; PF19037; Fuz_longin_2; 1.
DR Pfam; PF19038; Fuz_longin_3; 1.
DR PRINTS; PR01546; YEAST73DUF.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|RuleBase:RU367048};
KW Endosome {ECO:0000256|ARBA:ARBA00022753, ECO:0000256|RuleBase:RU367048};
KW Membrane {ECO:0000256|RuleBase:RU367048};
KW Protein transport {ECO:0000256|RuleBase:RU367048};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Transport {ECO:0000256|RuleBase:RU367048};
KW Vacuole {ECO:0000256|RuleBase:RU367048}.
FT DOMAIN 186..308
FT /note="FUZ/MON1/HPS1 first Longin"
FT /evidence="ECO:0000259|Pfam:PF19036"
FT DOMAIN 348..487
FT /note="FUZ/MON1/HPS1 second Longin"
FT /evidence="ECO:0000259|Pfam:PF19037"
FT DOMAIN 525..624
FT /note="FUZ/MON1/HPS1 third Longin"
FT /evidence="ECO:0000259|Pfam:PF19038"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 68747 MW; E2436200E93CF915 CRC64;
MAQETEEGNA VSSPSPPSPS PSPPPPPLPP RRKVSGEAPL QVGGQLQSKP TTAVSSIDIS
TLSFPDGTRG TFPTPSVGSG PSPLNSGYGT PSRDSSGDNL TDSMSVMSLA PTVRAPGDLA
SLVAGEFNRK SRAWNLLRSQ SETVQPFEAI ESGDSSELSG FEKEFDNIPE NLTDDVRLSM
WQSKMKHYLI LSSAGKPIWS RHGDLSLINS SMGVIQTIIS FYEGAKDPLM GFTAGKARFV
VLTAGPLYFV AISKLGESDS QLRGQLEALY MQILSTLTLP TLKNIFVHRP STDLRKPLEG
TETLLSSLAD SFTKGSPTAL LGALECLKLR KSQRHAINNI FLKNRAEKLL YGLIVAGGKL
VSVIRPRKHS LHPSDLQLIF NMLFESGSIK SGGGESWIPI CLPAFNNSGY LYMYVSFFDE
DGNETQPKPS STTKPTSSST PTIPEEGSPP PQPPPPPPPQ PESPQEIALI LISPDRESFF
PFSSLRTSLY NSLTKSTHLS LIRSSLASPR PSISSILPGS NPPPISHFIY KSRPNVQFVM
SSLHPLFTSP MARRKLMSQY QTLHAAMHAK HSHLKVIYSV GGDCASLGWV TPLFEFYCVA
GPNVSRQAMT EAANRVVKWV GREEARVFII GGGVF
//