ID A0A0H2UHB7_RAT Unreviewed; 1104 AA.
AC A0A0H2UHB7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=Slc4a4 {ECO:0000313|Ensembl:ENSRNOP00000004391.4,
GN ECO:0000313|RGD:68936};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000004391.4, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000004391.4, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000004391.4,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000004391.4}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000004391.4};
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 AlphaFoldDB; A0A0H2UHB7; -.
DR Ensembl; ENSRNOT00000004391.4; ENSRNOP00000004391.4; ENSRNOG00000003134.5.
DR RGD; 68936; Slc4a4.
DR GeneTree; ENSGT00940000156290; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000003134; Expressed in adult mammalian kidney and 19 other cell types or tissues.
DR ExpressionAtlas; A0A0H2UHB7; baseline and differential.
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 1: Evidence at protein 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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A0H2UHB7};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
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 479..502
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 514..543
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 563..581
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 736..758
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 828..852
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 888..907
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 914..933
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 966..996
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 148..397
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 451..965
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 50..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1053
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1104 AA; 124182 MW; C339E7A060E437D0 CRC64;
MYRCLLLNLV MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKAG
HKEKKEKERI SENYSDKSDV ENADESSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT
ELDELLAVDG QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCMEKGSI
MLDREASSLP QLVEMIADHQ IETGLLKPDL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT
VSSASRMFSN PDNGSPAMTH RNLTSSSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG
EVDFLDTPFI AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD
EVFHDIAYKA KDRHDLIAGI DEFLDEVIVL PPGEWDPAIR IEPPKSLPSS DKRKNMYSGG
ENVQMNGDTP HDGGHGGGGH GDCEELQRTG RFCGGLIKDI KRKAPFFASD FYDALNIQAL
SAILFIYLAT VTNAITFGGL LGDATDNMQG VLESFLGTAV SGAIFCLFAG QPLTILSSTG
PVLVFERLLF NFSKDHSFDY LEFRLWIGLW SAFMCLILVA TDASFLVQYF TRFTEEGFSS
LISFIFIYDA FKKMIKLADY YPINSDFRVG YNTHFSCACL PPDPVNLSVS NDTTLAPEDL
PTVSSTDMYH NATFDWAYLS KKECVKFGGK LVGNNCDFVP DITLMSFILF LGTYTSSMAM
KKFKTSRYFP TTARKLISDF AIILSILIFC VIDALVGVDT PKLIVPSEFK PTSPHRGWFV
PPFGGNPWWV CLAAAIPALL VTILIFMDQQ ITAVIVNRKE HKLKKGAGYH LDLFWVAILM
VVCSFMALPW YVAATVISIA HIDSLKMETE TSAPGEQPKF LGVREQRVTG TLVFILTGLS
VFMAPILKFI PMPVLYGVFL YMGVASLNGV QFMDRLKLLL MPLKHQPDFI YLRHVPLRRV
HLFTSLQVLC LALLWILKST VAAIIFPVMI LALVAVRKGM DYLFSQHDLS FLDDVIPEKD
KKKKEDEKKK KKKKGSLDSD NDDEKDPQHS LNATHHADKI PFLESLGLPS PPRSPVKVVP
QIRIELESED NDYLWRNKGT ETTL
//
