SPXS3_DICDI
ID SPXS3_DICDI Reviewed; 919 AA.
AC Q54MJ9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=SPX and EXS domain-containing protein 3;
DE AltName: Full=Protein XPR1 homolog;
GN Name=xpr1; ORFNames=DDB_G0285957;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: May play a role in phosphate homeostasis. Binds inositol
CC hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as
CC 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important
CC intracellular signaling molecules. {ECO:0000250|UniProtKB:Q9UBH6,
CC ECO:0000250|UniProtKB:Q9Z0U0}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The SPX domain has high affinity for inositol polyphosphates,
CC such as myo-inositol hexakisphosphate and 5-diphospho-myo-inositol
CC pentakisphosphate (5-InsP7). Its affinity for inorganic phosphate is
CC tow to three orders of magnitude lower. {ECO:0000250|UniProtKB:Q9UBH6}.
CC -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family. {ECO:0000305}.
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DR EMBL; AAFI02000082; EAL64513.1; -; Genomic_DNA.
DR RefSeq; XP_637991.1; XM_632899.1.
DR AlphaFoldDB; Q54MJ9; -.
DR STRING; 44689.DDB0233081; -.
DR PaxDb; Q54MJ9; -.
DR PRIDE; Q54MJ9; -.
DR EnsemblProtists; EAL64513; EAL64513; DDB_G0285957.
DR GeneID; 8625342; -.
DR KEGG; ddi:DDB_G0285957; -.
DR dictyBase; DDB_G0285957; xpr1.
DR eggNOG; KOG1162; Eukaryota.
DR HOGENOM; CLU_006116_1_1_1; -.
DR InParanoid; Q54MJ9; -.
DR OMA; HEMRNRR; -.
DR PhylomeDB; Q54MJ9; -.
DR PRO; PR:Q54MJ9; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; ISS:UniProtKB.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; ISS:UniProtKB.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IBA:GO_Central.
DR GO; GO:0006817; P:phosphate ion transport; IBA:GO_Central.
DR InterPro; IPR004342; EXS_C.
DR InterPro; IPR004331; SPX_dom.
DR InterPro; IPR033507; Syg1.
DR PANTHER; PTHR10783:SF4; PTHR10783:SF4; 1.
DR Pfam; PF03124; EXS; 1.
DR Pfam; PF03105; SPX; 1.
DR PROSITE; PS51380; EXS; 1.
DR PROSITE; PS51382; SPX; 1.
PE 3: Inferred from homology;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..919
FT /note="SPX and EXS domain-containing protein 3"
FT /id="PRO_0000330822"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 676..696
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..350
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT DOMAIN 605..806
FT /note="EXS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00712"
FT REGION 62..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..338
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P43585"
FT REGION 891..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 22
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P43585"
FT SITE 26
FT /note="Important for inositol polyphosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P43585"
SQ SEQUENCE 919 AA; 105312 MW; FE2A08CC474B3C6F CRC64;
MKFGKYLQRR QVSAWKKKYV FYKSFKKQIK SIKRAKTEEE LYIGNESQIQ IELTAIPINK
SISKIPPPSQ SSSSPSQSQS QIEIPLQSIE PTTTTTTTAA TSSSSSSTTT TNVNSKTIIN
SSGGSIKSNN SNPLSQSSII QRGPVIIREN NIEREEKKFD SMLQEEFDKV NTFFKQQEDE
FIHQFNDIKQ KVVAMSEICK NSSSKSLKDA ISEDSPRLGK FSHLFYNPSI IKKRNSSNLT
SSAIKDDGVG GASSNSQRYA QSSPSSSSSS SPSAMAVKAI AHAANAETYW NPGSLKLGKI
RRSLKRAMEE NYREIQALKE YTSLNMIAFR KIFKKYDKVL QSDSSVDGMK LVQQQYFVKS
KKLVVIEREI ESLYTNTFKH GNRRNAMAKL RVPKEYNAPP KVVFLTGGLS GMSLILFIFC
IRYMINNVAI IYFDSPTPLH FLSMFMLHRM IGIPILLLWY FGILLYVTSG KNINLFLILG
WDARTNITHY HILFLASGLT FLWTLSLFLY TYLAIHIDGK LPILFPFLLI AIVLFIVFCP
FNIIFRPSRY WLIHTFARIF SAPFLPVKFK DFFFGDQFTS LSIVLSDLEY VICFFVSDLW
TDGDICWRIN PYIKPCLVCV PPLLRALQSL RRFKDTKQNI HMMNFGKYSL TMLSTVTSSI
ANSKLLTDSS HKKGTLALWI IISIVSTIYS LGWDFLMDWG VLRTHSRNFL LRDHLFYRHK
WVYYFAMITN TLMRGSWTIN VSFEALSSRT KELIVLATAV IEVTRRFQWN FFRLENEHLS
NVGKFRAFDL KIPDILNTQS QQQQQQQQQQ QQQQQQQQQQ QQQQQEEIGA NELLGNNGEP
IVGDSKTVIT SDDFINGTSK QEGTIDLDRA QFQYSKNDLE DKIEESIINN KNNNNNECTP
FSENSFYNND HSGDENSNE
