VPS27_PHANO
ID VPS27_PHANO Reviewed; 720 AA.
AC Q0U4Z8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Vacuolar protein sorting-associated protein 27;
GN Name=VPS27; ORFNames=SNOG_13166;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT79493.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH445349; EAT79493.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001803378.1; XM_001803326.1.
DR AlphaFoldDB; Q0U4Z8; -.
DR SMR; Q0U4Z8; -.
DR STRING; 321614.Q0U4Z8; -.
DR GeneID; 5980293; -.
DR KEGG; pno:SNOG_13166; -.
DR eggNOG; KOG1818; Eukaryota.
DR InParanoid; Q0U4Z8; -.
DR OMA; PHSSCYS; -.
DR OrthoDB; 828765at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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; 3.
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..720
FT /note="Vacuolar protein sorting-associated protein 27"
FT /id="PRO_0000292521"
FT DOMAIN 18..150
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 264..283
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 168..228
FT /note="FYVE-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 230..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..639
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..670
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 720 AA; 79467 MW; 61A3B0E51041BF85 CRC64;
MAGWFGSSTN SAFDEQIERA TSSSLEDMPL NLEISDVIRS KTVQPKDAMK SLKKRIGHKN
PNVQLATLNL TDTCVKNGGA HFIQEIASRE FMDNLTSLLK APSTIAPNND VKNKMLELIQ
SWATAAEGRM NLGYINEVYR SLQREGYHFP PKENIASSML DSSAPPEWTD SDVCMRCRTA
FTFTNRKHHC RNCGNVFCGA CSSKTIPLPH LGIMEPVRVD DGCHEKLTIR SRGAPVPRPF
DTPKPHKTLY QGAMEPRSAR VDDSFDADLK RALEMSLEDA KGTGSSGFVS QSQLQSKPKP
STNGSSRKEP QEEEDPDLAA AIAASLADME EQKKKYTTTF KQQTASSSAA APFVAPKNDY
ELTPVEAENI NLFSTLVDRL QHQPPGTILR EPQIQELYES IGKLRPKLAR TYGETMSKHD
TLLDLHAKLS SVVRYYDRML EERLSSTYNQ AGAMYGLPAP TQRPASNLYP SIQSGAPSGA
GENYYTGNAS QSDPYGRPQS HYAGGYQSTS QQPYRTPGQS QEQYPPAQQP SQPYPNLSQQ
APPSSNYQQS SPQLQRQEAP NQQYPPQQAY PSQAPPSTVS DAESANYYYG DNTQGQPSQP
PMQRSQSFAS QPAQQQPPSP QMYNHAPPQQ TPLSPPAYQN PSYPSQQQTA PPPQQQAPPQ
QAPPPPQQQQ WQQPAQTQTQ AWQPAPYAAG GYGPESFPSA PQNQLPPQQQ KVVDEPLIDL
