S12A4_RABIT
ID S12A4_RABIT Reviewed; 1085 AA.
AC Q28677;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Solute carrier family 12 member 4;
DE AltName: Full=Electroneutral potassium-chloride cotransporter 1;
DE AltName: Full=Erythroid K-Cl cotransporter 1;
DE AltName: Full=rbKCC1;
GN Name=SLC12A4; Synonyms=KCC1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=New Zealand white; TISSUE=Kidney;
RX PubMed=8663127; DOI=10.1074/jbc.271.27.16237;
RA Gillen C.M., Brill S., Payne J.A., Forbush B. III;
RT "Molecular cloning and functional expression of the K-Cl cotransporter from
RT rabbit, rat, and human. A new member of the cation-chloride cotransporter
RT family.";
RL J. Biol. Chem. 271:16237-16244(1996).
RN [2]
RP GLYCOSYLATION.
RX PubMed=10564083; DOI=10.1152/ajpcell.1999.277.5.c899;
RA Su W., Shmukler B.E., Chernova M.N., Stuart-Tilley A.K., de Franceschi L.,
RA Brugnara C., Alper S.L.;
RT "Mouse K-Cl cotransporter KCC1: cloning, mapping, pathological expression,
RT and functional regulation.";
RL Am. J. Physiol. 277:C899-C912(1999).
CC -!- FUNCTION: Mediates electroneutral potassium-chloride cotransport when
CC activated by cell swelling. May contribute to cell volume homeostasis
CC in single cells. May be involved in the regulation of basolateral Cl(-)
CC exit in NaCl absorbing epithelia.
CC -!- ACTIVITY REGULATION: Inhibited by WNK3. {ECO:0000250}.
CC -!- SUBUNIT: Homomultimer and heteromultimer with other K-Cl
CC cotransporters. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10564083}.
CC -!- MISCELLANEOUS: Activated by N-ethylmaleimide (NEM). Inhibited by
CC furosemide and bumetanide.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000305}.
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DR EMBL; U55053; AAC48593.1; -; mRNA.
DR PIR; T18369; T18369.
DR RefSeq; NP_001076172.1; NM_001082703.2.
DR AlphaFoldDB; Q28677; -.
DR SMR; Q28677; -.
DR STRING; 9986.ENSOCUP00000005495; -.
DR PRIDE; Q28677; -.
DR GeneID; 100009441; -.
DR KEGG; ocu:100009441; -.
DR CTD; 6560; -.
DR eggNOG; KOG2082; Eukaryota.
DR InParanoid; Q28677; -.
DR OrthoDB; 349744at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IEA:InterPro.
DR GO; GO:0140157; P:ammonium import across plasma membrane; IDA:ARUK-UCL.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR000622; KCC1.
DR InterPro; IPR000076; KCL_cotranspt.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827; PTHR11827; 1.
DR PANTHER; PTHR11827:SF46; PTHR11827:SF46; 1.
DR Pfam; PF00324; AA_permease; 2.
DR Pfam; PF03522; SLC12; 2.
DR PRINTS; PR01081; KCLTRNSPORT.
DR PRINTS; PR01082; KCLTRNSPORT1.
DR TIGRFAMs; TIGR00930; 2a30; 1.
PE 1: Evidence at protein level;
KW Chloride; Glycoprotein; Ion transport; Membrane; Phosphoprotein; Potassium;
KW Potassium transport; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1085
FT /note="Solute carrier family 12 member 4"
FT /id="PRO_0000178032"
FT TOPO_DOM 1..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 866..1085
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 28..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UP95"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIS8"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y666"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHW9"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UP95"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UP95"
FT MOD_RES 983
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UP95"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1085 AA; 120743 MW; 717408738E226B8E CRC64;
MPHFTVVPVD GPRRGDYDNL EGLSWVDYGE RAEREDPDGH GNHRESSPFL CPLEASRGSD
YYDRNLALFE EELDIRPKVS SLLGKLVSYT NLTQGAKEHE EAESGEGTRR RAAKAPSMGT
LMGVYLPCLQ NIFGVILFLR LTWMVGTAGV LQALLIVLIC CCCTLLTAIS MSAIATNGVV
PAGGSYFMIS RSLGPEFGGA VGLCFYLGTT FAAAMYILGA IEILLTYIAP PAAIFYPSGT
HDTSNATLNN MRVYGTVFLS FMTLVVFVGV KYVNKFASLF LACVIISILS IYAGGIKSMF
DPPVFPVCML GNRTLSRDQF DICAKTTMVD NETVATRLWS FFCHSPNLTT DSCDPYFLLN
NVTEIPGIPG AAAGVLQENL WSAYLEKGEV VEKRGLPSTD AVGLKENLPL YVVADIATSF
TVLVGIFFPS VTGIMAGSNR SGDLRDAQKS IPVGTILAIV TTSLVYFSSV VLFGACIEGV
VLRDKYGDGV SRNLVVGTLA WPSPWVIVVG SFFSTCGAGL QSLTGAPRLL QAIAKDNIIP
FLRVFGHGKA NGEPTWALLL TALIAELGIL IASLDMVAPI LSMFFLMCYL FVNLACAVQT
LLRTPNWRPR FKYYHWALSF LGMSLCLALM FVSSWYYALV AMLIAGMIYK YIEYQGAEKE
WGDGIRGLSL SAARYALLRL EEGPPHTKNW RPQLLVLLKL DEDLHVKYPR LLTFASQLKA
GKGLTIVGSV IQGSFLESYG EAQAAEQTIK NMMKIEKVKG FCQVVVASKV REGLAHLIQS
CGLGGMRHNS VVLGWPYGWR QSEDPRAWKT FIDTVRCTTA AHLALLVPKN IAFYPSNHER
YLEGHIDVWW IVHDGGMLML LPFLLRQHKV WRKCRMRIFT VAQMDDNSIQ MKKDLAVFLY
HLRLEAEVEV VEMHNSDISA YTYERTLMME QRSQMLRQMR LTKTEREREA QLVKDRHSAL
RLESLYSDEE DEAAAGADKI QMTWTRDKYM TEPWDPSHTP DNFRELVHIK PDQSNVRRMH
TAVKLNEVIV TRSHDARLVL LNMPGPPKNS EGDENYMEFL EVLTEGLERV LLVRGGGREV
ITIYS
