MVP1_ASPOR
ID MVP1_ASPOR Reviewed; 724 AA.
AC Q2UB56;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Sorting nexin mvp1;
GN Name=mvp1; ORFNames=AO090102000101;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007162; BAE61209.1; -; Genomic_DNA.
DR RefSeq; XP_001822342.1; XM_001822290.2.
DR AlphaFoldDB; Q2UB56; -.
DR SMR; Q2UB56; -.
DR STRING; 510516.Q2UB56; -.
DR EnsemblFungi; BAE61209; BAE61209; AO090102000101.
DR GeneID; 5994387; -.
DR KEGG; aor:AO090102000101; -.
DR HOGENOM; CLU_009058_1_0_1; -.
DR OMA; MWHELRV; -.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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..724
FT /note="Sorting nexin mvp1"
FT /id="PRO_0000238595"
FT DOMAIN 351..459
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 387
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 389
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 413
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 426
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 724 AA; 79918 MW; 3130221F2E2D28B5 CRC64;
MSLFGTSPED SSAGNSAHRS KSSLFADEPS LGTGSNANLG SSSLFADDDD LSSGSPWNSN
VNKRTARHKL VKTLLSDSDA PESYIDAYDL VLSAGDRVGA GIGLTSVREI LSGSGISASD
QEKILNIVVS GDIDSANGLG RGEFNVLLAL VGLAQEGEDL TLDAVDDRRK KLPAPKSLYL
DALRANQESG TPAPSQERPI TPPRPASPQQ APNSAHSRRE SMTGLESDPW GSPELHRGHA
HAQLESDHPV LNGYGSVRSA TNAWSSRVGE DNNPNEISNS NRANSQTDSA PSHGSGFGWG
ESLGNTPSDG GLGGTARAGL GGFGPPSSVH SDSNPRRRSL GIGRVASPPV EEHVTVTLLP
EKEGMFMFQH RNYEVKSARR GSTVVRRYSD FVWLLDCLQK RYPFRQLPLL PPKRLSADSN
AFLEKRRRGL VRFTNALVRH PVLSQEQLVI MFLTVPTELS VWRKQATISV QDEFTGRDLP
PDLEDSLPST LPDTFETVRG GVKRSAEIYI NLCTLLERLA KRNEGLAADH LRFSLALQSL
TEVTRDTYAI DTNDVPLLNE GIRATANHLS VSQSLLEDEA RAWEEGVLED LKRQRDCLVS
VREMFDRRDR YARNNIPQLE RRIENNERKL QDLRSRPQGT VKPGEIEKVE DAIIKDKESI
VQQHARGVFI KECIRDEIVY FQQSQYHISR LHQEWSQERV KYAELQADNW RSLSDQVESM
PLSG
