SNF7_EMENI
ID SNF7_EMENI Reviewed; 242 AA.
AC Q5B5E0; C8V487;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Vacuolar-sorting protein snf7;
DE AltName: Full=Vacuolar protein-sorting-associated protein 32;
GN Name=snf7; Synonyms=vps32; ORFNames=AN4240;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP INTERACTION WITH PALA.
RX PubMed=12588984; DOI=10.1128/mcb.23.5.1647-1655.2003;
RA Vincent O., Rainbow L., Tilburn J., Arst H.N. Jr., Penalva M.A.;
RT "YPXL/I is a protein interaction motif recognized by Aspergillus PalA and
RT its human homologue, AIP1/Alix.";
RL Mol. Cell. Biol. 23:1647-1655(2003).
CC -!- FUNCTION: Required for the sorting and concentration of proteins
CC resulting in the entry of these proteins into the invaginating vesicles
CC of the multivesicular body (MVB). {ECO:0000250}.
CC -!- SUBUNIT: A component of the endosomal sorting required for transport
CC complex III (ESCRT-III) (By similarity). Interacts with palA.
CC {ECO:0000250, ECO:0000269|PubMed:12588984}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; AACD01000068; EAA59339.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF74412.1; -; Genomic_DNA.
DR RefSeq; XP_661844.1; XM_656752.1.
DR AlphaFoldDB; Q5B5E0; -.
DR SMR; Q5B5E0; -.
DR STRING; 162425.CADANIAP00004417; -.
DR EnsemblFungi; CBF74412; CBF74412; ANIA_04240.
DR EnsemblFungi; EAA59339; EAA59339; AN4240.2.
DR GeneID; 2873662; -.
DR KEGG; ani:AN4240.2; -.
DR eggNOG; KOG1656; Eukaryota.
DR HOGENOM; CLU_071097_1_0_1; -.
DR InParanoid; Q5B5E0; -.
DR OMA; WSWFGGA; -.
DR OrthoDB; 1490465at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0000815; C:ESCRT III complex; IBA:GO_Central.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:1904669; P:ATP export; IEA:EnsemblFungi.
DR GO; GO:0071454; P:cellular response to anoxia; IEA:EnsemblFungi.
DR GO; GO:1904902; P:ESCRT III complex assembly; IEA:EnsemblFungi.
DR GO; GO:0070676; P:intralumenal vesicle formation; IEA:EnsemblFungi.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:EnsemblFungi.
DR GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Endosome; Membrane; Reference proteome.
FT CHAIN 1..242
FT /note="Vacuolar-sorting protein snf7"
FT /id="PRO_0000211447"
FT REGION 187..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..95
FT /evidence="ECO:0000255"
FT COILED 152..179
FT /evidence="ECO:0000255"
FT COILED 216..242
FT /evidence="ECO:0000255"
FT COMPBIAS 219..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 242 AA; 27203 MW; 3A89B2AF06A8DA78 CRC64;
MWSWFGGAAA QKRKEAPKNA ILQLRSHLDM LQKREKHLEN QMNEQEAIAK KNVTTNKNAA
KAALRRKKVH EKNLEQTQAQ IVQLEQQIYS IEAANINHET LAAMKAAGAA MEKIHNGMTV
EQVDETILRD KLREQQAIND EIAIAITNPG FGEQVDEEDL EAELEGMEQE AMDERMLHTG
TVPVADQLNR LPAPANAERK ALPFPPQKRT PTDSLPAAKA KQKAEEEDEE AELEKLRAEM
AM
