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Database: UniProt
Entry: A0A670KGP1_PODMU
LinkDB: A0A670KGP1_PODMU
Original site: A0A670KGP1_PODMU 
ID   A0A670KGP1_PODMU        Unreviewed;      1142 AA.
AC   A0A670KGP1;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Solute carrier family 12 member 1 {ECO:0000313|Ensembl:ENSPMRP00000036588.1};
GN   Name=SLC12A1 {ECO:0000313|Ensembl:ENSPMRP00000036588.1};
OS   Podarcis muralis (Wall lizard) (Lacerta muralis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC   Lacertibaenia; Lacertidae; Podarcis.
OX   NCBI_TaxID=64176 {ECO:0000313|Ensembl:ENSPMRP00000036588.1, ECO:0000313|Proteomes:UP000472272};
RN   [1] {ECO:0000313|Ensembl:ENSPMRP00000036588.1, ECO:0000313|Proteomes:UP000472272}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30819892; DOI=10.1073/pnas.1820320116;
RA   Andrade P., Pinho C., Perez I de Lanuza G., Afonso S., Brejcha J.,
RA   Rubin C.J., Wallerman O., Pereira P., Sabatino S.J., Bellati A.,
RA   Pellitteri-Rosa D., Bosakova Z., Bunikis I., Carretero M.A., Feiner N.,
RA   Marsik P., Pauperio F., Salvi D., Soler L., While G.M., Uller T., Font E.,
RA   Andersson L., Carneiro M.;
RT   "Regulatory changes in pterin and carotenoid genes underlie balanced color
RT   polymorphisms in the wall lizard.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:5633-5642(2019).
RN   [2] {ECO:0000313|Ensembl:ENSPMRP00000036588.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 chloride(out) + K(+)(out) + Na(+)(out) = 2 chloride(in) +
CC         K(+)(in) + Na(+)(in); Xref=Rhea:RHEA:72395, ChEBI:CHEBI:17996,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00034631};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72396;
CC         Evidence={ECO:0000256|ARBA:ARBA00034631};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SLC12A transporter family.
CC       {ECO:0000256|ARBA:ARBA00010593}.
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DR   AlphaFoldDB; A0A670KGP1; -.
DR   Ensembl; ENSPMRT00000038757.1; ENSPMRP00000036588.1; ENSPMRG00000023307.1.
DR   GeneTree; ENSGT00940000158030; -.
DR   OMA; FRIKFAE; -.
DR   Proteomes; UP000472272; Chromosome 14.
DR   GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
DR   GO; GO:0015377; F:chloride:monoatomic cation symporter activity; IEA:InterPro.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR004841; AA-permease/SLC12A_dom.
DR   InterPro; IPR013612; AA_permease_N.
DR   InterPro; IPR018491; SLC12_C.
DR   InterPro; IPR002445; Slc12a1.
DR   InterPro; IPR002443; SLC12A1/SLC12A2.
DR   InterPro; IPR004842; SLC12A_fam.
DR   NCBIfam; TIGR00930; 2a30; 1.
DR   PANTHER; PTHR11827:SF93; SOLUTE CARRIER FAMILY 12 MEMBER 1; 1.
DR   PANTHER; PTHR11827; SOLUTE CARRIER FAMILY 12, CATION COTRANSPORTERS; 1.
DR   Pfam; PF00324; AA_permease; 2.
DR   Pfam; PF08403; AA_permease_N; 1.
DR   Pfam; PF03522; SLC12; 1.
DR   PRINTS; PR01207; NAKCLTRNSPRT.
DR   PRINTS; PR01209; NAKCLTRSPRT2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023201};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472272};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023201}.
FT   TRANSMEM        210..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        246..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        299..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        369..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        423..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        457..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        588..607
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        613..634
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        646..670
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          91..158
FT                   /note="Amino acid permease N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08403"
FT   DOMAIN          183..248
FT                   /note="Amino acid permease/ SLC12A"
FT                   /evidence="ECO:0000259|Pfam:PF00324"
FT   DOMAIN          255..728
FT                   /note="Amino acid permease/ SLC12A"
FT                   /evidence="ECO:0000259|Pfam:PF00324"
FT   DOMAIN          737..1142
FT                   /note="SLC12A transporter C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03522"
FT   REGION          31..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          867..894
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        31..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1142 AA;  126072 MW;  B4676DC32C0C2B9B CRC64;
     LPINMSMNNS PNVFLDPSPN RFQVNVINES HDNSVQSQGD PDSQRYEETS FADDVSNRLR
     VGYRPENREL YDNFFQNGDA SKTDGNFHPY DTHSNTYYLK TFGHNTMDAV PKIGYYRNTG
     SVSGVKINRP SLMDIHEQLA KNIAVTSGSV DKFAKADGNT EEAESNKEEE TKGGFVKFGW
     VKGVLVRCML NIWGVMLFIR LSWIVGQAGI GLGVIIILLA TMVTSITGLS TSAIATNGFV
     RGGSNIFSGI FSGLGVVVIC LSVVVTTLTG ISMSAICTNG VVRGGGAYYL ISRSLGPEFG
     GSIGLIFAFA NAVAVAMYVV GFAETVVELL KNSNAIMVDA TNDIRIIGAI TVVILLGISV
     AGMEWEAKAQ VILLFILLAA IVNFFIGTVI PSNNEKRARG FFNYQASIFA ENFGPDFRGD
     EGFFSVFAIF FPAATGILAG ANISGDLEDP QAAIPKGTML AILVTTIAYV GVAICAAACV
     VRDATGNVND TVVSGMNCNG SSACALGYDF SSCKTQTCDY GLMNNFQVMS MVSGFGPLIT
     AGIFSATLSS ALTSLVSAPK VFQALCKDNI YRALHFFAKG YGKNNEPIRG YVLTFIIAMA
     FILIAELNTI APIISNFFLA SYALINFSCF HASYAKSPGW RPAFKYYNMW VSLFGAILCC
     GVMFVINWWA AVITYAVELF LYIYVTYKKP DVNWGSSSQA VYYINAIDSA LELTTVDDHV
     KNFRPQCIVL TGEPMARPAL LDIAHSFTKN NGLCICCEVY TGPRKLCVTE MNSGMATKQA
     WLTKNKRKAF YAAVAADSFR DGVKSLLQAS GLGRMRPNTL VLGFKKDWKE ATAVEVENYM
     GVVHDAFDFD FGVVVARISQ GFDISQVLLV QEELKKLEQE RQVLEATIKD SKFEEGNGGI
     QRYFRRAAKL NITKTIPKKE SSISTISSMH VGEFNQRLLE ASSQFKKKQG KGTIDVWWLF
     DDGGLILLIP YMLTLRKKWK DCKLRIFTGG KVTRLEEEKL MMASLLSKFR IKFADIHIIG
     DINMKPNKES WKFFEEMIEP YRLHESCKDL TTAEKLKREA PWKITDAELE AVKEKSYRQV
     RLNELLQEHS RAANLIVLTL PVARKGIISD YLYMAWLEIL SRNLPPVLLI RGNHKNVLTF
     YS
//
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