GenomeNet

Database: UniProt
Entry: A0A401KZI7_ASPAW
LinkDB: A0A401KZI7_ASPAW
Original site: A0A401KZI7_ASPAW 
ID   A0A401KZI7_ASPAW        Unreviewed;       606 AA.
AC   A0A401KZI7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Vacuolar protein sorting-associated protein 17 {ECO:0000256|PIRNR:PIRNR011791};
GN   ORFNames=AAWM_07507 {ECO:0000313|EMBL:GCB24622.1};
OS   Aspergillus awamori (Black koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB24622.1, ECO:0000313|Proteomes:UP000286921};
RN   [1] {ECO:0000313|EMBL:GCB24622.1, ECO:0000313|Proteomes:UP000286921}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB24622.1,
RC   ECO:0000313|Proteomes:UP000286921};
RA   Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT   "Aspergillus awamori IFM 58123T.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the membrane-associated retromer complex which
CC       is essential in endosome-to-Golgi retrograde transport.
CC       {ECO:0000256|PIRNR:PIRNR011791}.
CC   -!- SUBUNIT: Component of the retromer complex.
CC       {ECO:0000256|PIRNR:PIRNR011791}.
CC   -!- SIMILARITY: Belongs to the VPS17 family.
CC       {ECO:0000256|PIRNR:PIRNR011791}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GCB24622.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BDHI01000021; GCB24622.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401KZI7; -.
DR   STRING; 105351.A0A401KZI7; -.
DR   Proteomes; UP000286921; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0030904; C:retromer complex; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR   CDD; cd07625; BAR_Vps17p; 1.
DR   CDD; cd06891; PX_Vps17p; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR014461; Retromer_complex_Vps17.
DR   InterPro; IPR037907; Vps17_PX.
DR   InterPro; IPR015404; Vps5_C.
DR   PANTHER; PTHR47433; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 17; 1.
DR   PANTHER; PTHR47433:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 17; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF09325; Vps5; 1.
DR   PIRSF; PIRSF011791; Vps17; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
PE   3: Inferred from homology;
KW   Protein transport {ECO:0000256|PIRNR:PIRNR011791};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286921};
KW   Transport {ECO:0000256|PIRNR:PIRNR011791}.
FT   DOMAIN          172..252
FT                   /note="PX"
FT                   /evidence="ECO:0000259|Pfam:PF00787"
FT   DOMAIN          306..490
FT                   /note="Sorting nexin/Vps5-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09325"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   606 AA;  66953 MW;  515C68FF55C4C05E CRC64;
     MDYSAISNDP DHPAGTSPWA SPRPTQTTFP ASVTSDIPPA PLPPQDPYNA ESQPTETPGF
     QENEIGSPDL SARLQGAQLG EPGYVDEHSQ HTQQQHGQQP RSQLPARYQT GPRQNPRQPA
     PVYRIQAKVT GLERTGKKDP ILRFDVHVSD ILFLPRPAPT DYRLQTNIPK FRTTQYRDVR
     RTHAEFVKLA DHLISANPEA LVPAVPPPLT PAGAGTEEDE IRVKSSLQRW LNVVLSNEVL
     IHDDEVVLFV ESDFGYSPVV RMKQPATGVR RKVLKQFAPP PDDTPELQNA RPIVKMFYLG
     TMDTSHKVDR VVKARRGLGL AESDFGVKLG QMHVQETHPG LSNAYRKLGK IIQTVGDFHA
     VQATAEATTL GDPLSYHSSD AFIVKETLTN RHILLRDLIQ AQQATRSKRA AADRLKVSSS
     VRPDKVDEAI NALDEAQGHE DYLTKRTQRV TSNLLAEKQR WFDRTTNDML ASLREYTLRQ
     IESERRTLAT LESVRPDIRA IDASGGLSRL GRESHPTARR PNLGSSQGPK GDAWSGIPRR
     SDSLGRSLSG SFVAPTPTED DEEVNGHGTG KGRLRSASGV SSIVEEDDDD RLDARNAASR
     LATSTF
//
DBGET integrated database retrieval system