MVP1_CANAL
ID MVP1_CANAL Reviewed; 744 AA.
AC Q3MPQ4; A0A1D8PQP5; Q5AFM9; Q5AFN0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Sorting nexin MVP1;
GN Name=MVP1; OrderedLocusNames=CAALFM_C700790WA;
GN ORFNames=CaJ7.0093, CaO19.7038, CaO19.7039;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15937140; DOI=10.1534/genetics.104.034652;
RA Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T.,
RA Mikami Y.;
RT "Sequence finishing and gene mapping for Candida albicans chromosome 7 and
RT syntenic analysis against the Saccharomyces cerevisiae genome.";
RL Genetics 170:1525-1537(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; AP006852; BAE44606.1; -; Genomic_DNA.
DR EMBL; CP017629; AOW30455.1; -; Genomic_DNA.
DR RefSeq; XP_019331023.1; XM_019475478.1.
DR AlphaFoldDB; Q3MPQ4; -.
DR SMR; Q3MPQ4; -.
DR STRING; 237561.Q3MPQ4; -.
DR GeneID; 3637943; -.
DR KEGG; cal:CAALFM_C700790WA; -.
DR CGD; CAL0000175009; orf19.7039.
DR VEuPathDB; FungiDB:C7_00790W_A; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_009058_0_0_1; -.
DR InParanoid; Q3MPQ4; -.
DR OrthoDB; 793604at2759; -.
DR Proteomes; UP000000559; Chromosome 7.
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; 3.30.1520.10; -; 1.
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..744
FT /note="Sorting nexin MVP1"
FT /id="PRO_0000238596"
FT DOMAIN 326..444
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 369
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 371
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 395
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 410
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 CONFLICT 398
FT /note="T -> TV (in Ref. 1; BAE44606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 744 AA; 84897 MW; 6ADF78D267C27545 CRC64;
MNSNIEDDPW SSGWNDDNDN NNNNNTSIND PLTGATATTT PYQSSYLTSS QLFTSTGGGG
SGSGGGYNSG VNTYNTTIPP NLINVPSSYE TIYSHFITKY NNNNNNNNSN STFTLNDFEI
NIIDKLISLN YLTNYQKQKI LDIIYENNLL PINQSFKFYQ ILGLLALEID VPGTGDYVTL
QFRLNNNLPD LPEKFINEII NEENEQEEQT SGLLGNRNRS IQSHSHFGPN NQDDWNIDDS
TTISGGGGGG GGNFGDPLLV DHSYIHDDLI DESRSVGGTQ PQQGGGGGSG GGSGSGSGTI
APNVDSSYIE KYINDIKDQF KPLFSGIDLI KIKEVPEKEG IIFKHINYMI THDLKIGGTS
SGTKKVIRRY SDFVWLMEYL LEKYPFRVIP GLPPKKFTGA SPDSQFLQRR RRGLHRFLNQ
LIKHPILSQE PIVQSFLTVP TDLTTWKKQA KIDSSLEFKG QKIQTDFINV IWPIMGEPFL
KKWRQAEENI QFIIDKWVKI IILVERYERR QQQISFDNGK FAEMLNGFSK LNTKIYPDNE
DNNNSTRNDV NVNVVVVDNN ENYKQDFDFN SSGDIININQ CLNSIGEFFN KSSQVLIDES
YIINTKTLEK FKNYLDYLNS LQELFERTKQ LSINQIDLLD KRIKDQEIKF KKISEENPDI
KGGELIKLRQ SIINDKQEIF QQLNKDWLIK QCCLQEFIIF QETQFLITEL WVEWCKDRLK
CQEKLVGLYD NLNQEIIHDM PLER
