ID A0A452H6S9_9SAUR Unreviewed; 1112 AA.
AC A0A452H6S9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000010260.1};
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:ENSGAGP00000010260.1, 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:ENSGAGP00000010260.1}
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; A0A452H6S9; -.
DR Ensembl; ENSGAGT00000011784.1; ENSGAGP00000010260.1; 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 NCBIfam; TIGR00930; 2a30; 1.
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 185..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 499..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 631..648
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 660..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 190..347
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 466..742
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 756..873
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT DOMAIN 890..1095
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT REGION 23..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1112 AA; 123386 MW; 9B3D43B90F07AA37 CRC64;
MHQHQRSPAK MASVRFMVTP TKIDDIPGLS DTSPDLSSRS SSRVRFSSRE SVPETSRSEG
MSDFSGATTS VATLAGEQAS DRTSNPHDVA EDVSQTSITG EQCQLLDPGR 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 ENCILPALGW SS
//
