ID A0A1V4K0G3_PATFA Unreviewed; 1424 AA.
AC A0A1V4K0G3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Solute carrier family 12 member 4 isoform B {ECO:0000313|EMBL:OPJ77871.1};
GN Name=SLC12A4 {ECO:0000313|EMBL:OPJ77871.1};
GN ORFNames=AV530_014902 {ECO:0000313|EMBL:OPJ77871.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ77871.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ77871.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ77871.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ77871.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:ARBA00004589}; Lipid-
CC anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004589}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family.
CC {ECO:0000256|ARBA:ARBA00010593}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ77871.1}.
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DR EMBL; LSYS01005191; OPJ77871.1; -; Genomic_DNA.
DR STRING; 372326.A0A1V4K0G3; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd01301; rDP_like; 1.
DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR000180; Dipep_AS.
DR InterPro; IPR000076; KCL_cotranspt.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR008257; Pept_M19.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR004842; SLC12A_fam.
DR NCBIfam; TIGR00930; 2a30; 1.
DR PANTHER; PTHR11827:SF46; SOLUTE CARRIER FAMILY 12 MEMBER 4; 1.
DR PANTHER; PTHR11827; SOLUTE CARRIER FAMILY 12, CATION COTRANSPORTERS; 1.
DR Pfam; PF00324; AA_permease; 2.
DR Pfam; PF01244; Peptidase_M19; 1.
DR Pfam; PF03522; SLC12; 2.
DR PRINTS; PR01081; KCLTRNSPORT.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00869; RENAL_DIPEPTIDASE_1; 1.
DR PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
PE 3: Inferred from homology;
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
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:UP000190648};
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 461..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 539..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 590..609
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 615..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 749..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 790..816
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 895..913
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 919..940
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 952..969
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 463..638
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 744..1034
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
FT DOMAIN 1048..1165
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT DOMAIN 1178..1424
FT /note="SLC12A transporter C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03522"
FT REGION 361..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1424 AA; 158681 MW; 6A61BE390B51D4B7 CRC64;
MRERAIELMQ DTRLIDGHND FVLRLRIFYQ NRLSRVNLRE LNKTHTNLAK LQAGYVGAQF
WSVYVLCSAQ NKDAVRLTLE QIDVVKRMCN SYEELELVTT SQGISDSRRI ACLIGIEGGH
SIDSSLATLR MFYDLGVRYM TLTHSCNTPW SESSSKGTHS FYPGVIGLTA FGQEVVKEMN
RLGMLIDLSH ASYSTAKAAL NISKAPVIFS HSSAFSICNH SRNVPDDILQ QLKKNKGIIM
VTFNADVLAC GRKVVNVSTL ADHFDHIKKI AGSESIGVGG DYDGVERFPE GLEDVSKYPS
LIEELLRRGW NEAELKGVLR ENFLRVFREV ENVRNINGPV NVGESEIPQE EVQNSCRLDL
HNHGLPTARD SRGKPTGGHG NHKENSPFLN SAEAGKGGDY YDRNLALFEE ELDIRPKVSS
LLGKLVNYTN LTQGVKEHEE AESTDGSKKK VSKSPSMGTL MGVYLPCMQN IFGVILFLRL
TWMVGMAGVL QSFLIVLLCC CCTMLTTISM SAIATNGVVP AGGSYFMISR SLGPEFGGAV
GLCFYLGTTF AGAMYILGAI EILLTYIVPQ AAIFHPSGAH DVSSAMLNNM RVYGTVFLIL
MAVVVFVGVK YVNKFASLFL ACVVISILSI YAGAIKSIFD PPEFPICMLG NRTLSRDQFD
VCAKTIVKDN ITVASKLWEL FCHTKNLTTE NCDDYFLMNN VSEIAGIPGA ASGILKDNLW
SNYLEKGEIL EKAHHPSVDV AGQKNNLHLY VLSDIATSFM VLVGIFFPSV TGIMAGSNRS
GDLKDAQKSI PVGTILAIVT TSLVYFSCVL LFGACIEGVV LRDKYGDAVN KNLVVGTLSW
PSPWVIVVGS FFSTCGAGLQ SLTGAPRLLQ AIAKDNIIPF LWIFGHGKAN GEPTWALLLT
ALIAELGILI ASLDMVAPIL SMFFLMCYLF VNLACAVQTL LRTPNWRPRF KYYHWALSFL
GMSICLALMF ISSWYYALVA MLIAGMIYKY IEYQGAEKEW GDGIRGLSLS AARYALLRLE
EGPPHTKNWR PQLLVLLKLD EDLHVKYPRL LTFASQLKAG KGLTIIGSVI QGNFLETYGE
AQAAEQTIKN MMDIEKVKGF CQVVVANKVR EGIAHLIQSC GLGGMKHNTV VLGWPYGWRQ
SEDPRSWKTF IGTVRCTTAA HLALLVPKNV SFYPSNHERY NEGNIDVWWI VHDGGMLMLL
PFLLKQHKVW RKCKMRIFTV AQMDDNSIQM KKDLATFLYQ LRIEAEVEVV EMHNSDISAY
TYERTLMMEQ RSQMLRQMRL TKTEREREAQ LVKDRHSIAR LESLYSDEED ETDTVPENIQ
MTWTKEKCDA EKRNRGSAVG SFRDLISIKP NQSNVRRMHT AVKLNEVIVN RSHDARLVLL
NMPGPPKNTD GDENYMEFLE VLTEGLERVL LVRGGGREVI TIYS
//
