VPS27_PICST
ID VPS27_PICST Reviewed; 732 AA.
AC A3LX75;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Vacuolar protein sorting-associated protein 27;
GN Name=VPS27; ORFNames=PICST_36619;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; CP000500; ABN67754.2; -; Genomic_DNA.
DR RefSeq; XP_001385783.2; XM_001385746.1.
DR AlphaFoldDB; A3LX75; -.
DR SMR; A3LX75; -.
DR STRING; 4924.XP_001385783.2; -.
DR PRIDE; A3LX75; -.
DR EnsemblFungi; ABN67754; ABN67754; PICST_36619.
DR GeneID; 4839973; -.
DR KEGG; pic:PICST_36619; -.
DR eggNOG; KOG1818; Eukaryota.
DR HOGENOM; CLU_011862_2_0_1; -.
DR InParanoid; A3LX75; -.
DR OMA; PHSSCYS; -.
DR OrthoDB; 828765at2759; -.
DR Proteomes; UP000002258; Chromosome 6.
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; 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 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..732
FT /note="Vacuolar protein sorting-associated protein 27"
FT /id="PRO_0000292522"
FT DOMAIN 23..166
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 271..290
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 313..332
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT ZN_FING 187..247
FT /note="FYVE-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 245..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 732 AA; 83145 MW; 15151640367D4D98 CRC64;
MSWFGSSSDS TIELDNKIQE ATSESIPNGE LDLPLALEVT DLIRSKSLPP IQCMRSLKKR
LGMTYSNPNL LSSTLKLVDL CIKNCGSHFL NEIASKEFMD YLVDFIFKVH YDTKNYQVRN
SEAKMNVGEL ILSLIKEWSI LFSNSSDLSY VTRCFERLES EAYNFPDFAE TSALNSKFVD
TEVPPDWVDD DKCMICYDKF SMINRKHHCR ACGGVFCQTH SSNFIPLVSL GISKPVRACD
NCLAKQKSKN KPSQHNSSSH SRGTSRVQED DEDEMLRKAI ELSLQDTQIP VSAPVARDAP
TNSSQTKTIT DEDDDEDLKA AIAASMKDYQ DQERLREEQQ KQWQQEQEEK HHQEEQSDFY
NYSIPKPSNY SQQLPYVQSV ASLTEEEEAD INKFITLMYQ VKNDQNISYA RLHDEKLTDL
HTKVCPLRSK VTKNLIYTVE RQKAFTELNN KIAAITRLYE EHLDSKLKQT YGYQQSVPPV
QLPEINDYMR GPQSNYEQSI PAQGTGYQQQ AGYVHPETTG YPSYPGGQQP IPQQPIAQQP
SGSRPSAQQA QKAPEQKHEQ QQTSVPTFAY PPQESYPPEG EDDEEQSNFE LPPLPNQAQN
DFSYPPTQSY DSPSEPMYPN DSTDQQYNVY PPNGAGSEES KDEYSSGELQ PVQPTREHVL
RTRSSELPPH AVEQASARFP PIDTVEEEYQ NSNNSSVPYP DVSFPIAPTQ NLQPQQEPPK
KFVPEPEPLI DI
