ID A7E1Z5_MOUSE Unreviewed; 1070 AA.
AC A7E1Z5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=Slc4a4 {ECO:0000313|EMBL:AAI48293.2,
GN ECO:0000313|Ensembl:ENSMUSP00000108844.4,
GN ECO:0000313|MGI:MGI:1927555};
GN Synonyms=slc4a4 {ECO:0000313|EMBL:ADN95183.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAI48293.2};
RN [1] {ECO:0000313|EMBL:AAI48293.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=PCR rescued clones {ECO:0000313|EMBL:AAI48293.2};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2] {ECO:0007829|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3] {ECO:0007829|PubMed:18034455}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [4] {ECO:0007829|PubMed:18630941}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5] {ECO:0000313|Ensembl:ENSMUSP00000108844.4, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000108844.4,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7] {ECO:0000313|EMBL:ADN95183.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6 {ECO:0000313|EMBL:ADN95183.1};
RC TISSUE=Epididymis {ECO:0000313|EMBL:ADN95183.1};
RX PubMed=21600280; DOI=10.1016/j.ygeno.2011.04.010;
RA Liu Y., Xu J.Y., Wang D.K., Wang L., Chen L.M.;
RT "Cloning and identification of two novel NBCe1 splice variants from mouse
RT reproductive tract tissues: A comparative study of NCBT genes.";
RL Genomics 98:112-119(2011).
RN [8] {ECO:0000313|Ensembl:ENSMUSP00000108844.4}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000108844.4};
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 EMBL; BC148292; AAI48293.2; -; mRNA.
DR EMBL; HQ204220; ADN95183.1; -; mRNA.
DR RefSeq; NP_001184076.1; NM_001197147.1.
DR ProteomicsDB; 331120; -.
DR Antibodypedia; 24400; 237 antibodies from 28 providers.
DR DNASU; 54403; -.
DR Ensembl; ENSMUST00000113218.10; ENSMUSP00000108844.4; ENSMUSG00000060961.17.
DR GeneID; 54403; -.
DR UCSC; uc012dyc.1; mouse.
DR AGR; MGI:1927555; -.
DR CTD; 8671; -.
DR MGI; MGI:1927555; Slc4a4.
DR VEuPathDB; HostDB:ENSMUSG00000060961; -.
DR GeneTree; ENSGT00940000156290; -.
DR HOGENOM; CLU_002289_5_0_1; -.
DR OrthoDB; 1013180at2759; -.
DR BioGRID-ORCS; 54403; 4 hits in 79 CRISPR screens.
DR ChiTaRS; Slc4a4; mouse.
DR Proteomes; UP000000589; Chromosome 5.
DR Bgee; ENSMUSG00000060961; Expressed in ciliary body and 246 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 GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
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|MaxQB:A7E1Z5,
KW ECO:0007829|PeptideAtlas:A7E1Z5};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
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 460..483
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 495..524
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 544..562
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 717..739
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 809..833
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 869..888
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 895..914
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 946..977
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 138..378
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 432..947
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 39..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Basic residues"
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 232..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1070
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1070 AA; 120465 MW; A17124475438F69A CRC64;
MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKAG HKEKKEKERI
SENYSDKSDV ENADESSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT ELDELLAVDG
QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCMEKGSI MLDREASSLP
QLVEMIADHQ IETGLLKPDL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASSPAMT
HRNLTSSSLN DISDKPEKDQ LKNKFMKKLP RDAEASNVLV GEVDFLDTPF IAFVRLQQAV
MLGALTEVPV PTRFLFILLG PKGKAKSYHE IGRAIATLMS DEVFHDIAYK AKDRHDLIAG
IDEFLDEVIV LPPGEWDPTI RIEPPKSLPS SDKRKNMYSG GENVQMNGDT PHDGGHGGGG
HGDCEELQRT GRFCGGLIKD IKRKAPFFAS DFYDALNIQA LSAILFIYLA TVTNAITFGG
LLGDATDNMQ GVLESFLGTA VSGAIFCLFA GQPLTILSST GPVLVFERLL FNFSKDHNFD
YLEFRLWIGL WSAFMCLVLV ATDASFLVQY FTRFTEEGFS SLISFIFIYD AFKKMIKLAD
YYPINSDFKV GYNTHFSCAC LPPDPVNLSV SNDTTLAPED LPTISSTDMY HNVTFDWAYL
SKKECVKYGG KLVGNNCDFV PDITLMSFIL FLGTYTSSMA MKKFKTSRYF PTTARKLISD
FAIILSILIF CVIDALVGVD TPKLIVPSEF KPTSPNRGWF VPPFGGNPWW VCLAAAIPAL
LVTILIFMDQ QITAVIVNRK EHKLKKGAGY HLDLFWVAIL MVVCSFMALP WYVAATVISI
AHIDSLKMET ETSAPGEQPK FLGVREQRVT GTLVFILTGL SVFMAPILKF IPMPVLYGVF
LYMGVASLNG VQFMDRLKLL LMPLKHQPDF IYLRHVPLRR VHLFTFLQVL CLALLWILKS
TVAAIIFPVM ILALVAVRKG MDYLFSQHDL SFLDDVIPEK DKKKKEDEKK KKKKKGSLDS
DNDDSDCPYS EKVPSIKIPM DIMEQQPFLS DNKPLDRERS STFLERHTSC
//
