ID J5SSX0_TRIAS Unreviewed; 773 AA.
AC J5SSX0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=PX domain-containing protein {ECO:0000259|PROSITE:PS50195};
GN ORFNames=A1Q1_03837 {ECO:0000313|EMBL:EJT47366.1};
OS Trichosporon asahii var. asahii (strain ATCC 90039 / CBS 2479 / JCM 2466 /
OS KCTC 7840 / NBRC 103889/ NCYC 2677 / UAMH 7654) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1186058 {ECO:0000313|EMBL:EJT47366.1, ECO:0000313|Proteomes:UP000002748};
RN [1] {ECO:0000313|EMBL:EJT47366.1, ECO:0000313|Proteomes:UP000002748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 90039 / CBS 2479 / JCM 2466 / KCTC 7840 / NCYC 2677 / UAMH
RC 7654 {ECO:0000313|Proteomes:UP000002748};
RX PubMed=23104369; DOI=10.1128/EC.00237-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Draft genome sequence of CBS 2479, the standard type strain of
RT Trichosporon asahii.";
RL Eukaryot. Cell 11:1415-1416(2012).
CC -!- SUBCELLULAR LOCATION: Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004481}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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:EJT47366.1}.
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DR EMBL; ALBS01000256; EJT47366.1; -; Genomic_DNA.
DR RefSeq; XP_014177737.1; XM_014322262.1.
DR AlphaFoldDB; J5SSX0; -.
DR GeneID; 25987350; -.
DR KEGG; tasa:A1Q1_03837; -.
DR VEuPathDB; FungiDB:A1Q1_03837; -.
DR HOGENOM; CLU_014456_1_1_1; -.
DR OrthoDB; 5475877at2759; -.
DR Proteomes; UP000002748; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR CDD; cd06867; PX_SNX41_42; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
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; IPR044106; PX_Snx41/Atg20.
DR PANTHER; PTHR46979; SORTING NEXIN-41; 1.
DR PANTHER; PTHR46979:SF2; SORTING NEXIN-41; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT DOMAIN 1..194
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 84024 MW; B8B5665CCECBD3C6 CRC64;
MEDVTNPFST SPSRSPSATP TRSPVLSRTT SHSSTNQRPS APGSVAGASS PPPTQRASFP
DPSKEPRRGT GVLPGPKPKE GFCCERDRQI AQGEEISIID AFKTTEGGKS SYITYVIRIG
ALQGLYPVLI IPPIPSKQSI TDYAVKGQSK TKEDVATIAT RKRLLEDFLR RVCRHPILGG
EHVFHRFLED GSEVLHSPPI SLLPKNPLHA PSHNPTFEDV NGNDDPDSTS STSYIAHHLL
PNPSPTHPLH RPDLRFQESE AFTDKFHQHF AHNMEKVNRR ATKRWSEHAS DMSELGAQWN
GFSLMESGPL GTAIEKVGQA VDADFLATTK MVSYNGLLLT NPQLQDWEQN ASEPLHTYTQ
FAQLIKSRLS FRHQKHVQYE LVQEALENQR DKLEILEAAE REARRLEQAL ERGGVAAGAS
ASAPSSPPAR EDSSIPELAR PSVRRSGQSF GLLSAVKHSL SGMMDVDPEA TRRANIAKTR
DNISQLEDSL QASAQDLKYA STTLQADLDR FQRQKVADLR ELTIQLSTIH RDWCKANLEA
WKAAQAAIDE IPDHPNKVPA DAAARVASID RDRDLPPVPQ QESRRSSVAH GSPAKRDSLS
MGGARSPSKP LSPGMGARSP SNASNPLPKM GQLNLDSPFS ETPFSSHPLG EPSAPANGLD
PLGGSMISPR HTPKPAEDAD TPKWPSSPVK SSPPEQKSVD VPPSPKSTQA VKSLNEEARD
EDEPVESSKG TLVDRKDSAG SVGSKLSTTN IKPADITKDT KPKTEDVGPL GPL
//