MVP1_NEUCR
ID MVP1_NEUCR Reviewed; 790 AA.
AC Q7SB97; U9WGC1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 3.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Sorting nexin mvp1;
DE AltName: Full=Vacuolar sorting protein 1;
GN Name=vsp-1; Synonyms=mvp1; ORFNames=NCU05715;
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: Required for vacuolar protein sorting. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; CM002238; ESA43133.1; -; Genomic_DNA.
DR RefSeq; XP_011393870.1; XM_011395568.1.
DR AlphaFoldDB; Q7SB97; -.
DR SMR; Q7SB97; -.
DR STRING; 5141.EFNCRP00000007649; -.
DR EnsemblFungi; ESA43133; ESA43133; NCU05715.
DR GeneID; 3879059; -.
DR KEGG; ncr:NCU05715; -.
DR VEuPathDB; FungiDB:NCU05715; -.
DR HOGENOM; CLU_009058_1_0_1; -.
DR InParanoid; Q7SB97; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR CDD; cd06866; PX_SNX8_Mvp1p_like; 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; IPR028662; SNX8/Mvp1.
DR InterPro; IPR035704; SNX8/Mvp1_PX.
DR InterPro; IPR045734; Snx8_BAR_dom.
DR PANTHER; PTHR47554; PTHR47554; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF19566; Snx8_BAR_dom; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..790
FT /note="Sorting nexin mvp1"
FT /id="PRO_0000238600"
FT DOMAIN 411..525
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 447
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 449
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 473
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 492
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 790 AA; 86091 MW; F5C895C6B3DE4A01 CRC64;
MSLFGSSPPN DGSAALNPAK TANSSRSTLF DNEAPTTRSG SALFADDDHD SPWDMPTPRK
QRSRADLIRN LLPSGDVPES YIETFDAVVR TENRSTNGRI TAGGVARTLA AAKLGADDQA
RIMGIIAPAS ASATGAGGGG DGAHGGEANS SAAAAAAAVG LGDLGRNEFN VLLALIGLVQ
EGEVASLDGV DERRRNLPQP KLQGLVNENV QPMLPNLSEL GAKPPQRPVT PPKAPTPSPP
KQQQQQQHQP PTLRKVSMEY PEDPWNAPDL HKGHNHGPLE HSTGHNGAAD VPRSVANDLN
GNDAVSYSTS PEVTTTSSAL PGRTTSTFTT SQPPSGPSSI HNVAESIQES NGAWNYFPGS
SSGGGFGEPA DNAITGPFGD SGGPGQSVSG SVGGSNPNRS IGHVRSGSNV EENILVTLMP
EKEGVFMFQH HNYEVSSIRR GSKVVRRYSD FVWLLDCLHK RYPFRVLPLL PPKRVAFNGN
HLSNDGAFIE KRRRGLARFL NALVRHPVLG QEQLVIMFLT VPTELSVWRK QATISVQDEF
TGRTLPPGLE DSLPPTLEEL FARTRVGVRR SAELYISTCT IMDRLIKRSE GVAADHARMA
VSLISLTETS ADTYATDHND VPLLNDGLQA MGRHLRTAQT LMEDEAKAWE EGVLEDLKRQ
RDALVSLRDM FDRRDRLDKD NIPFLQRRIE TNEAKLQALN AKPEGMVKPG EKERVVEAII
KDKESIVTQH NRSVFVKECI RDELRFFQNT QYNVSRLTQD WAQERVKYSE MLADNWRRLL
DDLEGMPLGD
