ID   S4A10_BOVIN             Reviewed;        1117 AA.
AC   Q32LP4;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Sodium-driven chloride bicarbonate exchanger {ECO:0000250|UniProtKB:Q6U841};
DE   AltName: Full=Solute carrier family 4 member 10 {ECO:0000250|UniProtKB:Q6U841};
GN   Name=SLC4A10 {ECO:0000250|UniProtKB:Q6U841};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Sodium/bicarbonate cotransporter which plays an important
CC       role in regulating intracellular pH (By similarity). Has been shown to
CC       act as a sodium/bicarbonate cotransporter in exchange for intracellular
CC       chloride (By similarity). Has also been shown to act as a
CC       sodium/biocarbonate cotransporter which does not couple net influx of
CC       bicarbonate to net efflux of chloride, with the observed chloride
CC       efflux being due to chloride self-exchange (By similarity). Controls
CC       neuronal pH and may contribute to the secretion of cerebrospinal fluid
CC       (By similarity). Reduces the excitability of CA1 pyramidal neurons and
CC       modulates short-term synaptic plasticity (By similarity). Required in
CC       retinal cells to maintain normal pH which is necessary for normal
CC       vision (By similarity). In the kidney, likely to mediate bicarbonate
CC       reclamation in the apical membrane of the proximal tubules (By
CC       similarity). {ECO:0000250|UniProtKB:Q5DTL9,
CC       ECO:0000250|UniProtKB:Q6U841, ECO:0000250|UniProtKB:Q80ZA5}.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q5DTL9}; Multi-pass membrane protein
CC       {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q80ZA5};
CC       Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:Q5DTL9}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q5DTL9}. Perikaryon
CC       {ECO:0000250|UniProtKB:Q5DTL9}. Presynapse
CC       {ECO:0000250|UniProtKB:Q5DTL9}. Postsynapse
CC       {ECO:0000250|UniProtKB:Q5DTL9}. Note=Detected in dendrites and axon
CC       terminals of retinal OFF bipolar cells and in axon terminals of ON
CC       bipolar cells. In amacrine cells, located in the perikaryon. Also
CC       detected in basal and apical dendrites of hippocampal pyramidal cells.
CC       {ECO:0000250|UniProtKB:Q5DTL9}.
CC   -!- DOMAIN: The N-terminal cytoplasmic domain is likely to have a high
CC       level of intrinsic disorder. {ECO:0000250|UniProtKB:Q80ZA5}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q5DTL9}.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Has been shown to act as a sodium/bicarbonate cotransporter in
CC       exchange for intracellular chloride (By similarity). Has also been
CC       shown to act as a sodium/biocarbonate cotransporter which is not
CC       responsible for net efflux of chloride, with the observed chloride
CC       efflux being due to chloride self-exchange (By similarity).
CC       {ECO:0000250|UniProtKB:Q5DTL9, ECO:0000250|UniProtKB:Q6U841}.
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DR   EMBL; BC109483; AAI09484.1; -; mRNA.
DR   RefSeq; NP_001033217.1; NM_001038128.1.
DR   AlphaFoldDB; Q32LP4; -.
DR   SMR; Q32LP4; -.
DR   STRING; 9913.ENSBTAP00000064195; -.
DR   GlyCosmos; Q32LP4; 4 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000020366; -.
DR   Ensembl; ENSBTAT00000069330.1; ENSBTAP00000064195.1; ENSBTAG00000015317.6.
DR   GeneID; 517077; -.
DR   KEGG; bta:517077; -.
DR   CTD; 57282; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015317; -.
DR   VGNC; VGNC:34890; SLC4A10.
DR   eggNOG; KOG1172; Eukaryota.
DR   GeneTree; ENSGT00940000156972; -.
DR   InParanoid; Q32LP4; -.
DR   OMA; EDAEKEX; -.
DR   OrthoDB; 1013180at2759; -.
DR   Reactome; R-BTA-425381; Bicarbonate transporters.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000015317; Expressed in occipital lobe and 27 other cell types or tissues.
DR   ExpressionAtlas; Q32LP4; baseline.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098794; C:postsynapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0036477; C:somatodendritic compartment; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0008510; F:sodium:bicarbonate symporter activity; ISS:UniProtKB.
DR   GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
DR   GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR   GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR   GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; ISS:UniProtKB.
DR   Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR   InterPro; IPR013769; Band3_cytoplasmic_dom.
DR   InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR003024; Na/HCO3_transpt.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   NCBIfam; TIGR00834; ae; 1.
DR   PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR   PANTHER; PTHR11453:SF32; SODIUM-DRIVEN CHLORIDE BICARBONATE EXCHANGER; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
PE   2: Evidence at transcript level;
KW   Antiport; Cell membrane; Cell projection; Glycoprotein; Ion transport;
KW   Membrane; Phosphoprotein; Reference proteome; Sodium; Sodium transport;
KW   Symport; Synapse; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1117
FT                   /note="Sodium-driven chloride bicarbonate exchanger"
FT                   /id="PRO_0000245239"
FT   TOPO_DOM        1..508
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        509..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        530..537
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        538..558
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        559..561
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        562..582
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        583..595
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        596..616
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        617..625
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        626..646
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        647..719
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        720..740
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        741..761
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        762..782
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        783..808
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        809..829
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        830..854
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        855..875
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        876..911
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        912..932
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        933..934
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        935..955
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        956..997
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        998..1018
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1019..1117
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..74
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         88
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT   MOD_RES         93
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT   MOD_RES         1056
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT   MOD_RES         1084
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT   CARBOHYD        673
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        676
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        686
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        696
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1117 AA;  125776 MW;  5C53EE5C535DC58F CRC64;
     MQSGTCESFQ SLSHQRNDEE AVVDRGGTRS ILKTHFEKED LEGHRTLFIG VHVPLGGRKS
     HRRHRHRGHK HRKRDRERDS GLEDGRESPS FDTPSQRVQF ILGTEDDDEE HIPHDLFTEL
     DEICWREGED AEWRETARWL KFEEDVEDGG ERWSKPYVAT LSLHSLFELR SCILNGTVLL
     DMHANTLEEI ADMVLDQQVS SGQLNEDVRH RVHEALMKQH HHQNQKKLTN RIPIVRSFAD
     IGKKQSEPNS MDKNAGQVVS PQSAPACVEN KNDVSRENST VDFSKGLGGQ QKGHTSPCGM
     KQRHEKGPPH QQDREVDLHF MKKIPPGAEA SNILVGELEF LDRTVVAFVR LSPAVLLQGL
     AEVPIPTRFL FILLGPLGKG QQYHEIGRSI ATLMTDEVFH DVAYKAKDRN DLVSGIDEFL
     DQVTVLPPGE WDPSIRIEPP KNVPSQEKRK IPAVPNGTAA HGEAEPHGGH SGPELQRTGR
     LFGGLILDIK RKAPYFWSDF TDALSLQCLA SFLFLYCACM SPVITFGGLL GEATEGRISA
     IESLFGASMT GIAYSLFGGQ PLTILGSTGP VLVFEKILFK FCKEYGLSYL SLRASIGLWT
     ATLCIILVAT DASSLVCYIT RFTEEAFASL ICIIFIYEAL EKLFELSEAY PINMHNDLEL
     LTQYSCNCVE PHNPSNNTLK EWRESNISAS DIIWENLTVS ECTSLHGEYV GRACGHEHPY
     VPDVLFWSVI LFFSTVTLSA TLKQFKTSRY FPTKVRSIVS DFAVFLTILC MVLIDYAIGI
     PSPKLQVPSV FKPTRDDRGW FVTPLGPNPW WTVIAAIIPA LLCTILIFMD QQITAVIINR
     KEHKLKKGCG YHLDLLMVAV MLGVCSIMGL PWFVAATVLS ITHVNSLKLE SECSAPGEQP
     KFLGIREQRV TGLMIFILMG SSVFMTSILK FIPMPVLYGV FLYMGASSLK GIQFFDRIKL
     FWMPAKHQPD FIYLRHVPLR KVHLFTVIQM SCLGLLWIIK VSRAAIVFPM MVLALVFVRK
     LMDFLFTKRE LSWLDDLMPE SKKKKLEDAE KEEEQSMLAM EDEGTVQLPL EGHYRDDPSV
     INISDEMSKT ALWRNLLITA DNSKDKESSF PSKSSPS
//