ID A0A2K5ZXB9_MANLE Unreviewed; 696 AA.
AC A0A2K5ZXB9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Solute carrier family 53 member 1 {ECO:0000256|ARBA:ARBA00035271};
DE AltName: Full=Phosphate exporter SLC53A1 {ECO:0000256|ARBA:ARBA00035512};
GN Name=XPR1 {ECO:0000313|Ensembl:ENSMLEP00000032432.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000032432.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000032432.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823,
CC ChEBI:CHEBI:43474; Evidence={ECO:0000256|ARBA:ARBA00035090};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32824;
CC Evidence={ECO:0000256|ARBA:ARBA00035090};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family.
CC {ECO:0000256|ARBA:ARBA00009665}.
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DR RefSeq; XP_011858015.1; XM_012002625.1.
DR AlphaFoldDB; A0A2K5ZXB9; -.
DR SMR; A0A2K5ZXB9; -.
DR STRING; 9568.ENSMLEP00000032432; -.
DR Ensembl; ENSMLET00000056009.1; ENSMLEP00000032432.1; ENSMLEG00000040363.1.
DR GeneID; 105555608; -.
DR KEGG; mleu:105555608; -.
DR CTD; 9213; -.
DR GeneTree; ENSGT00500000044895; -.
DR OMA; KKRGDNC; -.
DR OrthoDB; 7162at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IEA:Ensembl.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0001618; F:virus receptor activity; IEA:Ensembl.
DR GO; GO:0030643; P:intracellular phosphate ion homeostasis; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR CDD; cd14477; SPX_XPR1_like; 1.
DR InterPro; IPR004342; EXS_C.
DR InterPro; IPR004331; SPX_dom.
DR PANTHER; PTHR10783:SF103; XENOTROPIC AND POLYTROPIC RETROVIRUS RECEPTOR 1; 1.
DR PANTHER; PTHR10783; XENOTROPIC AND POLYTROPIC RETROVIRUS RECEPTOR 1-RELATED; 1.
DR Pfam; PF03124; EXS; 1.
DR Pfam; PF03105; SPX; 3.
DR PROSITE; PS51380; EXS; 1.
DR PROSITE; PS51382; SPX; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 237..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 509..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..177
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT DOMAIN 439..643
FT /note="EXS"
FT /evidence="ECO:0000259|PROSITE:PS51380"
FT REGION 673..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..97
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 675..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 81536 MW; B5B05AF15CA106D4 CRC64;
MKFAEHLSAH ITPEWRKQYI QYEAFKDMLY SAQDQAPSVE VTDEDTVKRY FAKFEEKFFQ
TCEKELAKIN TFYSEKLAEA QRRFATLQNE LQSSLDAQKE STGVTTLRQR RKPVFHLSHE
ERVQHRNIKD LKLAFSEFYL SLILLQNYQN LNFTGFRKIL KKHDKILETS RGADWRVAHV
EVAPFYTCKK INQLISETEA VVTNELEDGD RQKAMKRLRV PPLGAAQPAP AWTTFRVGLF
CGIFIVLNIT LVLAAVFKLE TDRSIWPLIR IYRGGFLLIE FLFLLGINTY GWRQAGVNHV
LIFELNPRSN LSHQHLFEIA GFLGILWCLS LLACFFAPIS VIPTYVYPLA LYGFMVFFLI
NPTKTFYYKS RFWLLKLLFR VFTAPFHKVG FADFWLADQL NSLSVILMDL EYMICFYSLE
LKWDESEGLL PNNSEESGIC HKYTYGVRAI VQCIPAWLRF IQCLRRYRDT KRAFPHLVNA
GKYSTTFFMV TFAALYSTHK ERGHSDTMVF FYLWIVFYII SSCYTLIWDL KMDWGLFDKN
AGENTFLREE IVYPQKAYYY CAIIEDVILR FAWTIQISIT STTLLPHSGD IIATVFAPLE
VFRRFVWNFF RLENEHLNNC GEFRAVRDIS VAPLNADDQT LLEQMMDQDD GVRNRQKNRS
WKYNQSISLR RPRLASQSKA RDTKVLIEDT DDEANT
//