VPS27_CRYNJ
ID VPS27_CRYNJ Reviewed; 750 AA.
AC P0CS26; Q55S12; Q5KGG4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Vacuolar protein sorting-associated protein 27;
GN Name=VPS27; OrderedLocusNames=CNE03710;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(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; AE017345; AAW43634.1; -; Genomic_DNA.
DR RefSeq; XP_570941.1; XM_570941.1.
DR AlphaFoldDB; P0CS26; -.
DR SMR; P0CS26; -.
DR STRING; 5207.AAW43634; -.
DR PaxDb; P0CS26; -.
DR EnsemblFungi; AAW43634; AAW43634; CNE03710.
DR GeneID; 3257686; -.
DR KEGG; cne:CNE03710; -.
DR VEuPathDB; FungiDB:CNE03710; -.
DR eggNOG; KOG1818; Eukaryota.
DR HOGENOM; CLU_011862_1_0_1; -.
DR InParanoid; P0CS26; -.
DR OMA; VIMASWF; -.
DR OrthoDB; 227882at2759; -.
DR Proteomes; UP000002149; Chromosome 5.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProt.
DR GO; GO:0031623; P:receptor internalization; IBA:GO_Central.
DR GO; GO:0007034; P:vacuolar 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 PANTHER; PTHR46275; PTHR46275; 1.
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..750
FT /note="Vacuolar protein sorting-associated protein 27"
FT /id="PRO_0000292514"
FT DOMAIN 24..153
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 253..272
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 294..313
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT ZN_FING 172..232
FT /note="FYVE-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 268..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 750 AA; 82859 MW; 4BC5BA1A35946237 CRC64;
MSWLWGSTTN PQFEELAEKA CSPLNLPYPQ SEDIATALEV ADMIRSKAIQ PKMAMQSLKK
RIASKNGRVQ MYAIGLTDTC IKNGGDHFLL EVASKEFVDE LSNLIKATTT SPEVKQMLIK
YFQQWALAFK SKSELSFFVE VYNELRASGI TFPPPPAPVP SHLLTTTTAP AWVDSDACMR
CRSAFTFTNR KHHCRNCGLV FDQACSSHSM PLPKYGITEE VRVCDGCWAK AGRNKADAPA
PAVPGRTPRS RADLDADLQR AIELSLAESQ HSQNRHHSHF TPSEPPLAHG TVEDEDEQMR
LAIEASLRDM EARPSAPAGL GEAPEPEYRP LPTFDLSPRE NETILTFSNT MDQMAAYGER
DLRRFPHAHV LAEQANTVGG RLRRNVEEKS TKQQMLMEMQ DKLSQAVNLY GQILDGQQAY
AAKRAHEEQA RRYQQQQSYY TQQYQPQPQL YGQYPPNGYQ AFVPPQQAYQ PPQPQPEAQA
QHAPSLYPTM PYTTPNFTSP PQERVYPQQS HSSPYSQWSP APSHVQPGLA RQASVVVPPV
SSPVPAGVQR QASMTYGAPI PVAEQSQRQQ QQYASAPPFA SGAAPVDIPS APPPVNLSTH
PNSPQRHSYI PSHPQTQTQT QYESQPQEIP SQQDMQYGAS APPPDSLGSY VSEGTVGSAK
SGLEQEHAAS QIQPQPQPQA SAQTQTQSQS QLQAQPQQNQ YAAQTQLPAG MYNAASFPQP
LPPTIFPDAP VEAPKGLEKE EKEEALLIEL
