ID A0A2U9B007_SCOMX Unreviewed; 1003 AA.
AC A0A2U9B007;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Putative solute carrier family 12 member 3-like {ECO:0000313|EMBL:AWO97197.1};
GN ORFNames=SMAX5B_021773 {ECO:0000313|EMBL:AWO97197.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWO97197.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWO97197.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CP026244; AWO97197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9B007; -.
DR STRING; 52904.ENSSMAP00000022927; -.
DR Proteomes; UP000246464; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015377; F:chloride:monoatomic cation 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; IPR018491; SLC12_C.
DR InterPro; IPR002948; SLC12A3.
DR InterPro; IPR004842; SLC12A_fam.
DR NCBIfam; TIGR00930; 2a30; 1.
DR PANTHER; PTHR11827:SF97; SLC12A10.3 SOLUTE CARRIER FAMILY 12 (SODIUM_POTASSIUM_CHLORIDE TRANSPORTERS), MEMBER 10, TANDEM DUPLICATE 3 ISOFORM X1-RELATED; 1.
DR PANTHER; PTHR11827; SOLUTE CARRIER FAMILY 12, CATION COTRANSPORTERS; 1.
DR Pfam; PF00324; AA_permease; 1.
DR Pfam; PF03522; SLC12; 2.
DR PRINTS; PR01230; NACLTRNSPORT.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 112..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 484..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 547..580
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 117..624
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 633..763
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT DOMAIN 797..1002
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 111571 MW; 3726F83BC3C492C3 CRC64;
MGQFTSRPDK LSSDARPRVR FSSDEEAPRS DLQRRDSQVE LRRASIYSVL DLVPQQELYS
CTLPRHKGAT ARPTLDELRR EAGVMEAANS HSLSVTEQHE GTHGRHKAPG RFGWMTGVMF
RCMLNMWGVI LLLRLSWITS QAGILLTWFI ILLSAAVTSV TALSISAIAT NGRASSGGAY
FMISRSLGPE IGGPVGMIFS FANTLACVLS VVGFAEVVRD LMQEFGAVMV DSINDIRIVG
VVTVTVLLLF SLAGMKWASK AHILLFVCVY SISFANYFVG SFIPPSPEKQ AQGIFGYRSD
VFVSNLKPDW RGAEGTFVQM FALFFPSTIG ILCGVNICGD LKDPATAIPK GSLMAIFWTT
ITFLAISGSI GSCVIRDASG NISDILTGNI TEGCVGLGCG LGWNFTQCIE SQSCGFGLAN
DLKVPGQVVG FSYLNTAGVF VASLSSAFGF LTSAPKIFQC LCRDNLYPYI GFFAKGYGKN
DEPLRAYILC YLIAVAFILI GELNSIAALI SNFFLCSFCL INFSCFHASI TNSPGWRPSF
HYYSKWTALF GAVISVFLMF LFTWWAALVT CCMILFLFGY VNYNKPKVNW GSSVQAGIYN
MALSYSISLS AVEDHVKNFR PQCLVLTGPP NQRPALVDFV GSFTKNISLM ICGDIIMEQE
KQTMPQEAAE RSMRWMNERK VCSFYTAFSA DSLRAGARHL MQAAGLGKLR PNTLVLGFKS
NWTDSSAESI DDYINTIYDT FDCNHCLCIL RMMDGLDVYD QFDFEVNQGF EPDEPVGNKD
QQSPVGESID DISTRVDHDQ MKTAFQNEQG TKTIDVYWIA DDGGLTLLVP YLLTRRRRWR
HSKVRVFIVG EEHNMEDGRN QMIALLKRFR LDFSDVIVIT DGEKRPQAKS LSRFEDSVAP
FRLHDEQQDG VSVQEFRQRS PWEISDKEFE AFKLKSERKV RLNEIIRRNS HHAALVLVSL
PVPQSDCPSA LYMSWLDTLT CGLHCPAVLI RGNQQSVLTF YCQ
//
