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Database: UniProt
Entry: C4Y6D2_CLAL4
LinkDB: C4Y6D2_CLAL4
Original site: C4Y6D2_CLAL4 
ID   C4Y6D2_CLAL4            Unreviewed;       650 AA.
AC   C4Y6D2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Vacuolar fusion protein MON1 {ECO:0000256|ARBA:ARBA00018132, ECO:0000256|RuleBase:RU367048};
GN   ORFNames=CLUG_03715 {ECO:0000313|EMBL:EEQ39587.1};
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ39587.1, ECO:0000313|Proteomes:UP000007703};
RN   [1] {ECO:0000313|EMBL:EEQ39587.1, ECO:0000313|Proteomes:UP000007703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ39587.1,
RC   ECO:0000313|Proteomes:UP000007703};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: Required for multiple vacuole delivery pathways including the
CC       cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and
CC       endocytosis. {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|ARBA:ARBA00008968, ECO:0000256|RuleBase:RU367048}.
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DR   EMBL; CH408079; EEQ39587.1; -; Genomic_DNA.
DR   RefSeq; XP_002616474.1; XM_002616428.1.
DR   AlphaFoldDB; C4Y6D2; -.
DR   STRING; 306902.C4Y6D2; -.
DR   GeneID; 8496674; -.
DR   KEGG; clu:CLUG_03715; -.
DR   VEuPathDB; FungiDB:CLUG_03715; -.
DR   HOGENOM; CLU_025637_0_0_1; -.
DR   InParanoid; C4Y6D2; -.
DR   OMA; AKWSANG; -.
DR   OrthoDB; 73361at2759; -.
DR   Proteomes; UP000007703; Unassembled WGS sequence.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
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|ARBA:ARBA00023006, ECO:0000256|RuleBase:RU367048};
KW   Endosome {ECO:0000256|RuleBase:RU367048};
KW   Membrane {ECO:0000256|RuleBase:RU367048};
KW   Protein transport {ECO:0000256|RuleBase:RU367048};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007703};
KW   Transport {ECO:0000256|RuleBase:RU367048};
KW   Vacuole {ECO:0000256|RuleBase:RU367048}.
FT   DOMAIN          171..304
FT                   /note="FUZ/MON1/HPS1 first Longin"
FT                   /evidence="ECO:0000259|Pfam:PF19036"
FT   DOMAIN          389..489
FT                   /note="FUZ/MON1/HPS1 second Longin"
FT                   /evidence="ECO:0000259|Pfam:PF19037"
FT   DOMAIN          528..637
FT                   /note="FUZ/MON1/HPS1 third Longin"
FT                   /evidence="ECO:0000259|Pfam:PF19038"
SQ   SEQUENCE   650 AA;  73072 MW;  24613F0B7A365034 CRC64;
     MDPYEGGAPT SNNSHRPRAL TSKLSFSFLQ QKVTASDSSS NLVTNPTTAV TLANANQADI
     AFPNEADDTS SLHPSYSNRY SLASGTSPYL SAVGSSDEEF EGENIENSEL TSLFQNLMAK
     DSRRGDENGI STPSMHNVFT DDEVPLDESF LMKRVALEKS DNLDTFKGKL KHFFILSTAG
     KPIYSMNGSD GLIMGYMGLI TTIVSTFHES LKSEFHHISQ DKFRLVVMDR NPLLLVAATN
     VSSELVPCSG DNSETSIIEE QLRTIYNYIL AVLSKPVICK NFDRRMNYDL RNILSHQDFN
     MLDSLCMKLT YGFTLSTTGE YEMDNSFYIG AMLNNAITCA KIRKSTRAKL DAILISCKRL
     KAKQHSSNGS LIISDKLLGS DKERFIASDL LFGFLTIEEK VLSYLRPKAH HLGNEDIRTL
     LSTVSSSLQV PEHDDAPELW IPLCMPNFND SGFLYLFVKQ LFLPTLASPI IIILLSGNKS
     SFYDMKEVAN YITYRIKRSS AFCRKLSDEL VHMSTSTPVL RELGISIIRH FIYKRKSYNQ
     FYMDNLQFDG NMSHVLRASS HVNHLYSNLA RSKTSIAIEG ISSAKKLTYT RWQLEGGWLT
     GFLLQDEKSE FYCICGGSGQ AQMIIEESLR IIRWCERYNK RLFVGDGVTF
//
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