VPS27_ASPFU
ID VPS27_ASPFU Reviewed; 729 AA.
AC Q4WHN8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Vacuolar protein sorting-associated protein 27;
GN Name=vps27; ORFNames=AFUA_2G04740;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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. {ECO:0000250}.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- DOMAIN: The FYVE domain is involved in the binding to
CC phosphatidylinositol 3-phosphate (PtdIns(3)P) which is required for the
CC association to endosomal membranes.
CC -!- DOMAIN: Both IUM domains are necessary for efficient binding to
CC ubiquitin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VPS27 family. {ECO:0000305}.
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DR EMBL; AAHF01000008; EAL87567.1; -; Genomic_DNA.
DR RefSeq; XP_749605.1; XM_744512.1.
DR AlphaFoldDB; Q4WHN8; -.
DR SMR; Q4WHN8; -.
DR STRING; 746128.CADAFUBP00002125; -.
DR EnsemblFungi; EAL87567; EAL87567; AFUA_2G04740.
DR GeneID; 3506664; -.
DR KEGG; afm:AFUA_2G04740; -.
DR VEuPathDB; FungiDB:Afu2g04740; -.
DR eggNOG; KOG1818; Eukaryota.
DR HOGENOM; CLU_011862_1_0_1; -.
DR InParanoid; Q4WHN8; -.
DR OMA; SDMVRSK; -.
DR OrthoDB; 828765at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033565; C:ESCRT-0 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; 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; IBA:GO_Central.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR017073; HGS/VPS27.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
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 Pfam; PF01363; FYVE; 1.
DR Pfam; PF02809; UIM; 2.
DR Pfam; PF00790; VHS; 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; SSF48464; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50330; UIM; 2.
DR PROSITE; PS50179; VHS; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Endosome; Membrane; Metal-binding; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..729
FT /note="Vacuolar protein sorting-associated protein 27"
FT /id="PRO_0000292508"
FT DOMAIN 16..147
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 261..280
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 307..326
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT ZN_FING 165..225
FT /note="FYVE-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 276..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 79374 MW; 3F6DFD7B1CEB482D CRC64;
MAGWFSSTSP LDEQVERATS SSLEDMALNL EISDLIRSKS VQPKEAMRSL KRRLENRNPN
VQIATLKLTD TCVKNGGSHF LAEIASREFM DNLVSLLTTE GAPLNTDVKE KMLELIQDWA
MAAQGRMDLN YLGETYRKLQ NEGFRFPPKN EISGSMLESS APPEWIDSDV CMRCRTPFSF
MNRKHHCRNC GNVFDAQCSS KTLPLPHLGI LQPVRVDDGC YVKLTSKSSL PSNLSDRSAF
KNHSITKANA MEPRGARAEG GFDDDLRRAL QLSLEEAQSK GSSGYVPSTR INDEPAKTTT
QTNHEEEEDA DLKAAIEASL RDMEEHKKKH AAALKSNAAA TDSSTRDSAA ATPLPKNPYE
LSPVEVENIH LFAALVDRLQ HQPPGTILRE PQIQELYESI GALRPKLARS YGETMSKHDT
LLDLHAKLST VVRYYDRMLE ERLSSAYSQH SLGYATAPGG SPYPNIYPTM PSHIPEGKTG
AENFYYGNPV ADRAPPVGNT YGYPHSSRDI REPTAAPSGP ISSGVYNQPG QAVPQNPPWN
GNAPSVASPQ PSAPSTPFPN NSSGYPGPSA STQYYASAPH PEQDSNAYSG PRPGETDVSH
QSSPNMRRDS YYQSAGAPVT ARASAPEQSP PTDQGQSPAY MQYGDSHSAQ STGQPTHQHQ
PTAPPPQSYY FQHQPPQSAP LPTHSQTPGA PYGTYPGGDV SPIGAPAPAV HYQPAAQTKP
AVEESLIEL
