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Database: UniProt
Entry: A0A2K5ZXB9_MANLE
LinkDB: A0A2K5ZXB9_MANLE
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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
//
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