SNX41_CRYNB
ID SNX41_CRYNB Reviewed; 638 AA.
AC P0CR65; Q55VX2; Q5KKB9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Sorting nexin-41;
GN Name=SNX41; OrderedLocusNames=CNBC3650;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
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: May be required for cytoplasm to vacuole transport (Cvt) and
CC pexophagy. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Endomembrane system {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=Endosome and other
CC perivacuolar punctate structures. {ECO:0000250}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization to the perivacuolar
CC punctate structures. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AAEY01000013; EAL22227.1; -; Genomic_DNA.
DR RefSeq; XP_776874.1; XM_771781.1.
DR AlphaFoldDB; P0CR65; -.
DR EnsemblFungi; EAL22227; EAL22227; CNBC3650.
DR GeneID; 4935030; -.
DR KEGG; cnb:CNBC3650; -.
DR VEuPathDB; FungiDB:CNBC3650; -.
DR HOGENOM; CLU_014456_1_1_1; -.
DR Proteomes; UP000001435; Chromosome 3.
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:0015031; P:protein transport; 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; -; 1.
DR Gene3D; 3.30.1520.10; -; 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 Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Autophagy; Endosome; Lipid-binding; Membrane; Protein transport; Transport.
FT CHAIN 1..638
FT /note="Sorting nexin-41"
FT /id="PRO_0000410294"
FT DOMAIN 84..201
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
SQ SEQUENCE 638 AA; 70743 MW; ADD7C7ED8DE4248A CRC64;
MDSDTSPNPF ASSPPSSPSP RPSLPPPVPR KPSSLVSAAS GSPPPTHRAS FPDPARHPKM
GATVPGPKPK TGYCCSIDKD ISAGEQVHIV DALKTTEGGT ASYITYVIRL GTHTVRRRYS
AFLSLHQSLT GLYPVLIIPP IPSKQSLTDY AVKGQSKARE DATIIARRKR LLEDFLQRLI
RHPILGGEHV LHRFLEEDVS WSEVLHSPPI SLLSKNPLHA PSHNPTFQPT TPTSPSEAPA
TTSYIAHHLL PTPSPSHPLR QPDQRFMDSE AFTEKFQSHF SGTMEKVNRR VTKRWGERAH
DMSELGGIWN GFSLVEQGKL GDAIEKVGRA VDAEYLATAA LLQSWEKTTT EPLHIYSQFA
TLIRARLSFR HQKHVQYELV QEALETQRDK LEILENAERE ARRLEEALER GGSVLASPQL
EPEAARDERE RAQRRARASQ GFGLLSAVKH SLSGMIDMDP EATRRANIAK TRDNISQLED
SYQAAAQDLK YASMTLQADL DRFQRQKVAD LREMAINLSQ VHRDWCKQNL EAWKAAQAAV
REIDPHPNRP AQTQTQVQSQ QSHAGPSTLH AQTEDDVSKL GVDAMKNEIE RVEIEIADKP
LPKPSLAETG GDGVVPSPQP RQENDTEERE GHGPLGPL
