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Database: UniProt
Entry: A0A0E9NAM3_SAICN
LinkDB: A0A0E9NAM3_SAICN
Original site: A0A0E9NAM3_SAICN 
ID   A0A0E9NAM3_SAICN        Unreviewed;       713 AA.
AC   A0A0E9NAM3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Vacuolar protein sorting-associated protein 27 {ECO:0000256|ARBA:ARBA00017753, ECO:0000256|PIRNR:PIRNR036956};
GN   ORFNames=G7K_1135-t1 {ECO:0000313|EMBL:GAO46917.1};
OS   Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS   / NRRL Y-17804).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Taphrinomycotina incertae sedis; Saitoella.
OX   NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO46917.1, ECO:0000313|Proteomes:UP000033140};
RN   [1] {ECO:0000313|EMBL:GAO46917.1, ECO:0000313|Proteomes:UP000033140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO46917.1,
RC   ECO:0000313|Proteomes:UP000033140};
RX   PubMed=21914972; DOI=10.2323/jgam.57.243;
RA   Nishida H., Hamamoto M., Sugiyama J.;
RT   "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL   J. Gen. Appl. Microbiol. 57:243-246(2011).
RN   [2] {ECO:0000313|EMBL:GAO46917.1, ECO:0000313|Proteomes:UP000033140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO46917.1,
RC   ECO:0000313|Proteomes:UP000033140};
RX   PubMed=24646756; DOI=10.2323/jgam.60.7;
RA   Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT   "The early diverging ascomycetous budding yeast Saitoella complicata has
RT   three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT   lineages.";
RL   J. Gen. Appl. Microbiol. 60:7-12(2014).
CC   -!- FUNCTION: Component of the ESCRT-0 complex which is the sorting
CC       receptor for ubiquitinated cargo proteins at the multivesicular body
CC       (MVB) and recruits ESCRT-I to the MVB outer membrane.
CC       {ECO:0000256|PIRNR:PIRNR036956}.
CC   -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC       {ECO:0000256|PIRNR:PIRNR036956}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000256|ARBA:ARBA00004125,
CC       ECO:0000256|PIRNR:PIRNR036956}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004125, ECO:0000256|PIRNR:PIRNR036956};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004125,
CC       ECO:0000256|PIRNR:PIRNR036956}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the VPS27 family.
CC       {ECO:0000256|ARBA:ARBA00008597, ECO:0000256|PIRNR:PIRNR036956}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAO46917.1}.
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DR   EMBL; BACD03000006; GAO46917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E9NAM3; -.
DR   STRING; 698492.A0A0E9NAM3; -.
DR   OMA; RTAFSFM; -.
DR   Proteomes; UP000033140; Unassembled WGS sequence.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProt.
DR   GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProt.
DR   CDD; cd15735; FYVE_spVPS27p_like; 1.
DR   CDD; cd21385; GAT_Vps27; 1.
DR   CDD; cd16979; VHS_Vps27; 1.
DR   Gene3D; 1.20.5.1940; -; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 6.10.140.100; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR017073; HGS/VPS27.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR002014; VHS_dom.
DR   InterPro; IPR049425; Vps27_GAT-like.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR47794; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR   PANTHER; PTHR47794:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00790; VHS; 1.
DR   Pfam; PF21356; Vps27_GAT-like; 1.
DR   PIRSF; PIRSF036956; Hrs_Vps27; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00726; UIM; 2.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50330; UIM; 2.
DR   PROSITE; PS50179; VHS; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   3: Inferred from homology;
KW   Endosome {ECO:0000256|ARBA:ARBA00022753, ECO:0000256|PIRNR:PIRNR036956};
KW   Membrane {ECO:0000256|PIRNR:PIRNR036956};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033140};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          19..149
FT                   /note="VHS"
FT                   /evidence="ECO:0000259|PROSITE:PS50179"
FT   DOMAIN          167..227
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          229..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   713 AA;  76436 MW;  6634D00B68640830 CRC64;
     MASWFGSNPL DEQVERATSE SLPAGAEDLA LSLEICDQIR SKTVDSKTAM RSLKKRINHR
     NPNVQIAALK LTDVCVKNGG NHFLTEIASR EFMDNLVSLL NASGGLNPDV MSKVLECIQT
     WAIAFRGKSH LDYVQHTQSS LASTGFQFPS VTEITSSFVD TAAPPDWTDS DVCMRCRTTF
     TFTNRKHHCR NCGNVFCGAC SSKTMALPHL GVMQAVRVCD GCYQKKQETI KATPPKAQPT
     PSGPPRSLRS GGGHMQPRSA RVVNDDDDAD FQTALKMSLE ESRRGNGVSS GYVPNIGNSS
     NPFVPATNNP PASSASSVRS GYELPAPRKS LLQVAEADEE DPDLKAAIEA SLREAQAQSA
     RAAHVHQASA AQSAPAPQPQ SQPPAHELTP TEAENITLFA TLIDRLAASP NPAAILSDPQ
     ISSLHDSISL LRPKLARAMG ESVRKYETLV DMHAKLGTVV RLYDRTLEEQ LRRAYERHSV
     SGYAQPAFGA APTMSPQATG GYYGQSQAPP QAYPGMPDRQ YSTGPAGYTS PPPMDGQHDP
     YATQGYGPPQ VARPGPFGQA AYPPPMPPMY TGGSQHAAPS GQAPLQAAHT GGSQREFYSS
     PDPRPVENGG YHPQMPAAPP LDGMAPQHSG YGNAPPVEDA QRAWQDQQLQ RSGSYYAAEQ
     APSAPQGALG ELNALNTYQT PPAGLEVVEH GGHQAWQQTK PTPQPQEGSL IDL
//
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