SNX41_NEUCR
ID SNX41_NEUCR Reviewed; 619 AA.
AC Q7SB54;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 3.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Sorting nexin-41;
DE AltName: Full=Vacuolar sorting protein 6;
GN Name=vsp-6; Synonyms=snx41; ORFNames=NCU06259;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002238; EAA33627.3; -; Genomic_DNA.
DR RefSeq; XP_962863.3; XM_957770.3.
DR AlphaFoldDB; Q7SB54; -.
DR STRING; 5141.EFNCRP00000005976; -.
DR EnsemblFungi; EAA33627; EAA33627; NCU06259.
DR GeneID; 3879016; -.
DR KEGG; ncr:NCU06259; -.
DR VEuPathDB; FungiDB:NCU06259; -.
DR HOGENOM; CLU_014456_0_0_1; -.
DR InParanoid; Q7SB54; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
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; -; 2.
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 InterPro; IPR015404; Vps5_C.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF09325; Vps5; 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;
KW Reference proteome; Transport.
FT CHAIN 1..619
FT /note="Sorting nexin-41"
FT /id="PRO_0000213831"
FT DOMAIN 108..224
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142
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"
FT BINDING 191
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 619 AA; 68856 MW; B79FDF20CDE34055 CRC64;
MWNDEDNNPY GSFERRDSFA SSTNPASPTA RDYSIDARFP TPQDVRYDAP LTPSDAGDDE
VPGPTYPREA SDAATDDETD DQAHGELVPR RKPGGYDSRI EQMLYENPEL PILITEAGKS
QESGGRFIVY TIKTGDLTVR RRYSEFASLR DALTRLHPTL VIPPIPEKHT MADYAANPTN
AKQDQQIIDL RKRMLAVFLN RCRRMEQVRT DGVWWRFLDP NSSWTEVLHS HPVSSIPKQI
MKAPPLDPAN PTAGHSFLPV PSSSAKLKTL PTQALDSAAA ASLARFPPDA NSLSEQDLDA
YFIAFETSIK DLESLLTGPM EKVNRRTLNH LSSLASDLSE LGARYNAFAL SETAPTVSAA
IERVGQAADS SYIATEELST SLSASFAEPM RESAQFAGVV RNVLRYRILK RVQQEMTTDE
LNKKKALLES LERSEAEARR IDQYLSSSQQ IQPPRREPPA QHRRDGSGED TASIDSDFPP
THSDFSQAPS AKIGAPERTG GSPSHKKAAS TSITNKIFGP IRHAVQGVVD VDPERTRRDT
IGKTRESIVQ LEQAQIASAK DVKDASASVL KDLKRFQREK EDDLKRYMLA YAKSQIEWAK
KNQETWEEAK AEVNKINES
