ID A0A0C9MJN6_9FUNG Unreviewed; 628 AA.
AC A0A0C9MJN6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Vacuolar protein sorting-associated protein 27 {ECO:0000256|ARBA:ARBA00017753, ECO:0000256|PIRNR:PIRNR036956};
GN ORFNames=MAM1_0016c01528 {ECO:0000313|EMBL:GAN02088.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN02088.1};
RN [1] {ECO:0000313|EMBL:GAN02088.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN02088.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) 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.
CC {ECO:0000256|PIRNR:PIRNR036956}.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC {ECO:0000256|PIRNR:PIRNR036956}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000256|ARBA:ARBA00004125,
CC ECO:0000256|PIRNR:PIRNR036956}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125, ECO:0000256|PIRNR:PIRNR036956};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004125,
CC ECO:0000256|PIRNR:PIRNR036956}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the VPS27 family.
CC {ECO:0000256|ARBA:ARBA00008597, ECO:0000256|PIRNR:PIRNR036956}.
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DR EMBL; DF836305; GAN02088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9MJN6; -.
DR STRING; 91626.A0A0C9MJN6; -.
DR OrthoDB; 922060at2759; -.
DR Proteomes; UP000053815; 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 CDD; cd16979; VHS_Vps27; 1.
DR Gene3D; 1.20.5.1940; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 6.10.140.100; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR017073; HGS/VPS27.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
DR InterPro; IPR049425; Vps27_GAT-like.
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; HEPATOCYTE GROWTH FACTOR-REGULATED TYROSINE KINASE SUBSTRATE; 1.
DR PANTHER; PTHR46275:SF1; HEPATOCYTE GROWTH FACTOR-REGULATED TYROSINE KINASE SUBSTRATE; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF02809; UIM; 2.
DR Pfam; PF00790; VHS; 1.
DR Pfam; PF21356; Vps27_GAT-like; 1.
DR PIRSF; PIRSF036956; Hrs_Vps27; 2.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00726; UIM; 2.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50330; UIM; 2.
DR PROSITE; PS50179; VHS; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Endosome {ECO:0000256|ARBA:ARBA00022753, ECO:0000256|PIRNR:PIRNR036956};
KW Membrane {ECO:0000256|PIRNR:PIRNR036956};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 29..149
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 168..228
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 268..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 69676 MW; F31042A4F1CB2EDE CRC64;
MGSFWWGSNG LDELIEKATS ELLPAGQVDL ALHLEISDQI RSKKVNAKDA MRSLKQRLNH
KNPNVVMSTL ELVDTCVKNS GSTFVKEVAT REFMEELTHI IKMATGSSHV KSKTLSLIQV
WGIASKGNPA LSYISDTYTL LRAEGYTFPH VTDKIDSTLF ETAVAPEWTD SACCERCRTS
FTLTNRKHHC RQCGATFCQQ CSSKSMPLPH LGINDSVRVC DGCYIKVKLA KVADRDAVPH
LLGTPASISS SLTPTYTPSI KNKAQTTTTA TTASNTNNNN NSSAANDDQF EDDIKKAIEL
SLKESQQQQK LASFYSSEQK EEPAAANAKN KSAGEDEEEA NLAAAIAASL QDMKLSAAST
AKDDYPKYNS NDLSPIDMEN IQLFSTLMQR VQSAANDVSG DTQINQLYTQ IGTLQPKLVR
TLNDTSRKHE MFVHLHTKLN QAVKAYDKLI EDRLASATQR TRTPSYPTYY NHAQTAAAAT
PQVQHQYLST WQQPMNVYPH YSAQTPISLP LSQPAQPQPH SQTYPQPQPQ PQPVSTLDNM
RTHQAPPPLP PTSGQQQWYP SAERSPYEYQ PQSTMTPVPV QTPVMQPTPY PVVSHGSSYT
QPQPQQQQQQ QKQVYHQQPV EEAPLIEL
//
