ID A0A452HGR7_9SAUR Unreviewed; 1062 AA.
AC A0A452HGR7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000014066.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000014066.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000014066.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) + K(+)(in) = chloride(out) + K(+)(out);
CC Xref=Rhea:RHEA:72427, ChEBI:CHEBI:17996, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00034453};
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; A0A452HGR7; -.
DR Ensembl; ENSGAGT00000016105.1; ENSGAGP00000014066.1; ENSGAGG00000004450.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IEA:InterPro.
DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR000076; KCL_cotranspt.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827:SF66; SOLUTE CARRIER FAMILY 12 MEMBER 6; 1.
DR PANTHER; PTHR11827; SOLUTE CARRIER FAMILY 12, CATION COTRANSPORTERS; 1.
DR Pfam; PF00324; AA_permease; 2.
DR Pfam; PF03522; SLC12; 2.
DR PRINTS; PR01081; KCLTRNSPORT.
PE 3: Inferred from homology;
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Symport {ECO:0000256|ARBA:ARBA00022847};
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:ARBA00022847}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 472..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 561..578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 590..607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 120..277
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 396..672
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 686..803
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT DOMAIN 820..1062
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT REGION 90..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 118940 MW; AAD62241A4308A5A CRC64;
MYQWEEIYFI RVFFFVFSFL FFSFVIHFFP SSCQLLDPGR KKDIYLNNTS YEDGDEYFDK
NLALFEEEMD TRPKVSSLLN RMANYTNLTQ GAREHEEAEN IAEGKKKPTK TPQMGTFMGV
YLPCLQNIFG VILFLRLTWV VGTAGVLQAF AIVLICCCCV SVSGGSYFMI SRALGPEFGG
AVGLCFYLGT TFAAAMYILG AIEIFLMYIA PEAAIFRSTD ALKESAAMLN NMRVYGSAFL
VLMVLVVFVG VRYVNKFASL FLACVIVSIL AIYAGAIKSS FAPPRFPVCM LGNRTLSGRQ
IDICAKTQEL GNFTVPTQLW GLFCNSSKQL NATCDEYFAH NNVTSIQGIP GLASGIITEN
LWSSYLQKGE IIEKPSAHSV DVLGAMSQEY VLADITTSFT LLVGIFFPSV TGIMAGSNRS
GDLKDAQKSI PIGTILAILT TSFVCILPGL VWREGFGDAV HSNLVVGTLS WPSPWVIVIG
SFFSTCGAGL QSLTGAPRLL QAIAKDNIIP FLRVRARSAS LSFPQYPAAP PESWLHLHAG
RAALVWLCVA VLQLFPSAPE FFLMCYLFVN LACALQTLLR TPNWRPRFRY YHWALSFVGM
SICLALMFVS SWYYAIVAMV IAGMIYKYIE YQGSEKEWGD GIRGLSLSAA RFALLRLEEG
PPHTKNWRPQ LLVLLKLDED LHVKHPHLLT FASQLKAGKG LTIVGSVMVG NFLENYAEAL
AAEQTIKHLM EAERVKGFCQ LVVAAKVREG ISHLIQSCGL GGMKHNTVVM GWPNAWRQSE
DARAWKTFIS TVRVTTAARL ALLVAKNVAF YPGNAEPFLE GNIDVWWIVH DGGMLMLLPF
LLKQHKVWRK CNIRIFTVAQ LEDNSIQMKK DLATFLYHLR IEAEVEVVEM HDSDISAYTY
ERTLMMEQRS QMLRHMRLSK TERDREAQLV KDRNSMLRLT SIGSDEDEET ETYQEKVQMT
WTKDKYMAAR GQKARTLEGM QDLLNMKPDQ SNVRRMHTAV KLNEVIVNKS HEAKLVLLNM
PGPPRNPAGD ENYMEFLEVL TEGLERVLLV RGGGSEVITI YS
//
