VPS27_ASPTN
ID VPS27_ASPTN Reviewed; 556 AA.
AC Q0CJV3;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Vacuolar protein sorting-associated protein 27;
GN Name=vps27; ORFNames=ATEG_06031;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476601; EAU33792.1; -; Genomic_DNA.
DR RefSeq; XP_001215209.1; XM_001215209.1.
DR AlphaFoldDB; Q0CJV3; -.
DR SMR; Q0CJV3; -.
DR STRING; 341663.Q0CJV3; -.
DR EnsemblFungi; EAU33792; EAU33792; ATEG_06031.
DR GeneID; 4321630; -.
DR VEuPathDB; FungiDB:ATEG_06031; -.
DR eggNOG; KOG1818; Eukaryota.
DR HOGENOM; CLU_011862_2_1_1; -.
DR OMA; SDMVRSK; -.
DR OrthoDB; 828765at2759; -.
DR Proteomes; UP000007963; 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..556
FT /note="Vacuolar protein sorting-associated protein 27"
FT /id="PRO_0000292510"
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 232..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 556 AA; 61726 MW; 08E814CC4BA00CBF CRC64;
MAGWFSSASP LDEQVERATS SSLEDIALNL EISDLIRSKS VQPKEAMRSL KRRLENKNPN
VQLATLKLTD TCVKNGGTHF LAEIASREFM DNLVSLLKTE GLQLNTEVKE KMLELIQDWA
MAAQGRMDLS YVGQTYQRLQ EEGFRFPPKT QISGSMLESS APPEWIDSDV CMRCRTAFSF
MNRKHHCRNC GNVFDAQCSS KTLPLPHLGI LQPVRVDDGC YAKLTSKAAQ SSGLSDRTSF
KNNSITKSSA MEPRTARAEG GFDDDLRRAL QMSLEEAQNK GSSGYVPQPK VAQEPPKPSG
QPTAEEEEDA DLKAAIEASL RDMEEHKQKH AAALKNTTSE TPSHQPQNTT TLPKNPYELS
PVEVENIHLF AALVDRLQHQ PPGTILREPQ IQELYESIGT LRPKLARSYG ETMSKHDTLL
DLHSKLSTVV RYYDRMLEER LSSAYSQHSL GYGSIPSGPG YPNVYPSMPP TAEGKAGAEN
FYYGNSVVEN PLTASNPQYP QAAPDMMSRE KDTHARRPYE PQYVYTALHS LSTTILQWNG
APATDLHSPP PSANVP
