S4A10_BOVIN
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 03-AUG-2022, entry version 105.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC109483; AAI09484.1; -; mRNA.
DR RefSeq; NP_001033217.1; NM_001038128.1.
DR AlphaFoldDB; Q32LP4; -.
DR SMR; Q32LP4; -.
DR STRING; 9913.ENSBTAP00000020366; -.
DR PaxDb; Q32LP4; -.
DR PRIDE; Q32LP4; -.
DR Ensembl; ENSBTAT00000069330; ENSBTAP00000064195; ENSBTAG00000015317.
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; KTHQFKD; -.
DR OrthoDB; 265068at2759; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000015317; Expressed in occipital lobe and 27 other tissues.
DR ExpressionAtlas; Q32LP4; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; IEA:Ensembl.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0097441; C:basal dendrite; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0097442; C:CA3 pyramidal cell dendrite; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0015301; F:anion:anion antiporter activity; IEA:Ensembl.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR GO; GO:0008510; F:sodium:bicarbonate symporter activity; ISS:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:Ensembl.
DR GO; GO:0021860; P:pyramidal neuron development; IEA:Ensembl.
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:0009416; P:response to light stimulus; IEA:Ensembl.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; ISS:UniProtKB.
DR Gene3D; 3.40.930.10; -; 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 PANTHER; PTHR11453; PTHR11453; 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; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 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
