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Database: UniProt
Entry: B2AY80_PODAN
LinkDB: B2AY80_PODAN
Original site: B2AY80_PODAN 
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
//
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