ID B2NIZ2_BOVIN Unreviewed; 1079 AA.
AC B2NIZ2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=SLC4A4 {ECO:0000313|EMBL:BAG31939.1,
GN ECO:0000313|Ensembl:ENSBTAP00000060194.1,
GN ECO:0000313|VGNC:VGNC:34894};
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 {ECO:0000313|EMBL:BAG31939.1};
RN [1] {ECO:0000313|EMBL:BAG31939.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Parotid gland {ECO:0000313|EMBL:BAG31939.1};
RX PubMed=16037094; DOI=10.1113/jphysiol.2005.088633;
RA Yamaguchi S., Ishikawa T.;
RT "Electrophysiological characterization of native Na+-HCO3- cotransporter
RT current in bovine parotid acinar cells.";
RL J. Physiol. (Lond.) 568:181-197(2005).
RN [2] {ECO:0000313|EMBL:BAG31939.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Parotid gland {ECO:0000313|EMBL:BAG31939.1};
RA Yamaguchi S., Ishikawa T.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSBTAP00000060194.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000060194.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSBTAP00000060194.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000060194.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Electrogenic sodium/bicarbonate cotransporter with a
CC Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate
CC bicarbonate influx/efflux at the basolateral membrane of cells and
CC regulate intracellular pH. {ECO:0000256|ARBA:ARBA00037277}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 hydrogencarbonate(out) + Na(+)(out) = 2
CC hydrogencarbonate(in) + Na(+)(in); Xref=Rhea:RHEA:72215,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000256|ARBA:ARBA00036309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 hydrogencarbonate(out) + Na(+)(out) = 3
CC hydrogencarbonate(in) + Na(+)(in); Xref=Rhea:RHEA:72219,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000256|ARBA:ARBA00035820};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004554}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651}. Lateral cell membrane
CC {ECO:0000256|ARBA:ARBA00034693}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034693}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362035}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362035}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000256|ARBA:ARBA00010993, ECO:0000256|RuleBase:RU362035}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362035}.
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DR EMBL; AB436382; BAG31939.1; -; mRNA.
DR RefSeq; XP_005208126.1; XM_005208069.3.
DR Ensembl; ENSBTAT00000080169.1; ENSBTAP00000068265.1; ENSBTAG00000002348.5.
DR Ensembl; ENSBTAT00000084190.1; ENSBTAP00000060194.1; ENSBTAG00000002348.5.
DR CTD; 8671; -.
DR VEuPathDB; HostDB:ENSBTAG00000002348; -.
DR VGNC; VGNC:34894; SLC4A4.
DR GeneTree; ENSGT00940000156290; -.
DR HOGENOM; CLU_002289_5_0_1; -.
DR OMA; LCMAPAN; -.
DR TreeFam; TF313630; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000002348; Expressed in spiral colon and 83 other cell types or tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008510; F:sodium:bicarbonate symporter activity; IEA:UniProt.
DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
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:SF10; ELECTROGENIC SODIUM BICARBONATE COTRANSPORTER 1; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU362035};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362035};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW Symport {ECO:0000256|ARBA:ARBA00022847};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362035};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362035};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362035}.
FT TRANSMEM 469..492
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 504..533
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 553..571
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 730..748
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 778..797
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 818..842
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 878..897
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 904..923
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 955..986
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 138..387
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 441..956
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 40..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 121375 MW; 8745DFEFFD51A6B5 CRC64;
MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKTG HREKKEKERI
SENYSDKSDV ENADESSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT ELDELLAVDG
QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCMEKGSI MLDREASSLP
QLVEMIVDHQ IETGLLKPDL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASRMFTN
PDNGSPAMTH RNLTSSSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG EVDFLDSPFI
AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD EVFHDIAYKA
KDRQDLIAGI DEFLDEVIVL PPGEWDPAIR IEPPKSLPSS DKRKNMYSGG ENVQMNGDTP
HDGGHGGGGH ADCEELQRTG RFCGGLIKDI KRKAPFFASD FYDALNIQAL SAILFIYLAT
VTNAITFGGL LGDATDNMQG VLESFLGTAV SGAIFCLFAG QPLTILSSTG PVLVFERLLF
NFSKDHNFDY LEFRLWIGLW SAFLCLILVA TDASFLVQYF TRFTEEGFSS LISFIFIYDA
FKKMIKLADY YPINSNFKVG YNTQFSCVCM PPDPVNISVS NDTTLAPEDL PTISSSNMYH
NATFDWAFLT TKECLKYGGK LVGNNCGFVP DITLMSFILF LGTYTSSMAL KKFKTSPYFP
TTARKLISDF AIILSILIFC VIDALVGVDT PKLIVPSEFK PTSPNRGWFV APFGGNPWWV
YLAAAIPALL VTILIFMDQQ ITAVIVNRKE HKLKKGAGYH LDLFWVAILM VVCSFMALPW
YVAATVISIA HIDSLKMETE TSAPGEQPKF LGVREQRVTG TLVFILTGLS VFMAPILKFI
PMPVLYGVFL YMGVASLNGV QFMDRLKLLL MPLKHQPDFI YLRHVPLRRV HLFTFLQVLC
LALLWILKST VAAIIFPVMI LALVAVRKGM DYLFSQHDLS FLDDVIPEKD KKKKEDEKKK
KKKKGSLDSD NDDSDCPYSE KVPSIKIPMD IMEQQPFLSD SKPSDRERSP TFLERHTSC
//
