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Database: UniProt
Entry: H0YTR5_TAEGU
LinkDB: H0YTR5_TAEGU
Original site: H0YTR5_TAEGU 
ID   H0YTR5_TAEGU            Unreviewed;      1078 AA.
AC   H0YTR5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   Name=SLC4A4 {ECO:0000313|Ensembl:ENSTGUP00000001680.2};
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000001680.2, ECO:0000313|Proteomes:UP000007754};
RN   [1] {ECO:0000313|Ensembl:ENSTGUP00000001680.2, ECO:0000313|Proteomes:UP000007754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20360741; DOI=10.1038/nature08819;
RA   Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA   Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA   Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA   Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA   Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA   Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA   Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA   McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA   Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA   Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA   Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA   Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA   Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA   Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT   "The genome of a songbird.";
RL   Nature 464:757-762(2010).
RN   [2] {ECO:0000313|Ensembl:ENSTGUP00000001680.2}
RP   IDENTIFICATION.
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; H0YTR5; -.
DR   STRING; 59729.ENSTGUP00000021670; -.
DR   Ensembl; ENSTGUT00000001696.2; ENSTGUP00000001680.2; ENSTGUG00000001611.2.
DR   GeneTree; ENSGT00940000156290; -.
DR   HOGENOM; CLU_002289_5_2_1; -.
DR   TreeFam; TF313630; -.
DR   Proteomes; UP000007754; Chromosome 4.
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   3: Inferred from homology;
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:UP000007754};
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        729..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        777..796
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        817..841
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        877..896
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        903..922
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        954..985
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..955
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          39..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1011..1078
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        236..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1011..1038
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1078
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1078 AA;  121304 MW;  E590170BFFA445BC CRC64;
     MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHRRRPG HKEKKEKEKI
     SENYSDKSDV ENADETSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT ELDELLAVDG
     QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCIEKGSI MLDMEASSLP
     QVVEMIVDNQ IETGLLKSEL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASRMFSN
     PDNGSPAMAH RNLTSTSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG EVDFLESPFI
     AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD EVFHDIAYKA
     KDRQDLIAGI DEFLDEVIVL PPGEWDPAIR IEPPKSLPSS DKRKNMYSGG ENLQMNGDTP
     HDGGHGGGGH GDCEELQRTG RFCGGLIKDI KRKAPFFASD FYDALNIQAL SAILFIYLAT
     VTNAITFGGL LGDATENMQG VLESFLGTAV TGAIFCLLAG QPLTILSSTG PVLVFERLLF
     NFSKDNDFDY LEFRLWIGLW SAFQCLILVA TDASFLVKYF TRFTEEGFSS LISFIFIYDA
     FKKMIKLADH YPINSEFKVD YITHYSCACK PLDTVNSSLL NRTMVLSDYE LVSPSSELAN
     TTIDWAALTA KDCLKYGGQL VGNNCDYVPD ITLMSFILFF GTYTCSMALK KFKTSRYFPT
     TARKLISDFA IILSILIFCG IDALVGVDTP KLIVPSEFKP TSPERGWFIP PFGGNPWWVY
     LAAAIPALLV TILIFMDQQI TAVIVNRKEH KLKKGAGYHL DLFWVAILMI VCSFMGLPWY
     VAATVISIAH IDSLKMETET SAPGEQPKFL GVREQRVTGV IVFILTGVSV FMAPILKFIP
     MPVLYGVFLY MGVASLNGVQ FMDRLKLLLM PLKHQPDFIY LRHVPLRRVH LFTFLQVLCL
     ALLWILKSTV AAIIFPVMIL ALVAVRKAMD YLFSQHDLSF LDDVIPEKDK KKKEDEKKKK
     KKKGSMDSDN DDSDCPYSEK VPSIKIPMDI MEQEPFLSDS KPADREKSPT FLERHTSC
//
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