VPS27_ASPCL
ID VPS27_ASPCL Reviewed; 714 AA.
AC A1CEK1;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Vacuolar protein sorting-associated protein 27;
GN Name=vps27; ORFNames=ACLA_089930;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027052; EAW11300.1; -; Genomic_DNA.
DR RefSeq; XP_001272726.1; XM_001272725.1.
DR AlphaFoldDB; A1CEK1; -.
DR SMR; A1CEK1; -.
DR STRING; 5057.CADACLAP00008334; -.
DR EnsemblFungi; EAW11300; EAW11300; ACLA_089930.
DR GeneID; 4705079; -.
DR KEGG; act:ACLA_089930; -.
DR VEuPathDB; FungiDB:ACLA_089930; -.
DR eggNOG; KOG1818; Eukaryota.
DR HOGENOM; CLU_011862_1_0_1; -.
DR OMA; PHSSCYS; -.
DR OrthoDB; 828765at2759; -.
DR Proteomes; UP000006701; 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 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..714
FT /note="Vacuolar protein sorting-associated protein 27"
FT /id="PRO_0000292507"
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 306..325
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 277..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 78156 MW; 56D01CAF71B00D66 CRC64;
MAGWFSSSSP LDEQVERATS SSLEDIALNL EISDLIRSKS VQPKEAMRSL KRRLENRNPN
VQIATLKLTD TCVKNGGTHF LAEIASREYL DNMVSLLTAE GAPLNSDVKE KMLELIQDWA
MAAQGRMDLN YLGETYRKLQ SEGFRFPPKS EISGSMLESS APPEWIDHDV CMRCRTPFSF
MNRKHHCRNC GNVFDAQCSS KTLPLPHLGI LQPVRVDDGC YAKLTSKSFT PSTLSDRSAF
KNNSITKANA MEPRGARAEG GFDDDLRRAL QMSLEEAQNR GSGGYIPQPK VNEPSNATIQ
PHPQDEEDAD LKAAIEASLR DMEEHKKKHA AALKNNTVAT DSTAQDTGSA LPMPKNPYEL
SPVEVENIHL FAALVDRLQH QPPGTILRES QIQELYESIG TLRPKLARSY GETMSKHDTL
LDLHAKLSTV VRYYDRMLEE RLSSAYSQHS LGYGQAPGGS QYPNMYPSMP SQAVEGKSGA
ENFYYGNAVP ERSPPAHSTY AYQQGIAPSG PMSSGMYPQP GQALPSNPAW NGNAPPTTAS
PQLSTSSTPF PNHPVGYPAP SAPTQYYAPT APPEQDANTY STPRPGETEV SHQASPVMRR
DSYYQSAGAP PSAPEPSPPS EHGQSSGYMQ YADSRTMPPN SQYPPQQQPS AQPYYSQQPP
PQATPHTTYS QPPAAPYETH PVADVSPIGA PVPSAPYQQP APTRPAVEES LIEL
