ID   A0A2R9CAF4_PANPA        Unreviewed;       606 AA.
AC   A0A2R9CAF4;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   10-JUN-2026, entry version 41.
DE   RecName: Full=Sodium-independent sulfate anion transporter {ECO:0000256|ARBA:ARBA00073161};
DE   AltName: Full=Solute carrier family 26 member 11 {ECO:0000256|ARBA:ARBA00083171};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000038839.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000038839.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000038839.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- FUNCTION: Sodium-independent anion exchanger mediating bicarbonate,
CC       chloride, sulfate and oxalate transport. Exhibits sodium-independent
CC       sulfate anion transporter activity that may cooperate with SLC26A2 to
CC       mediate DIDS-sensitive sulfate uptake into high endothelial venules
CC       endothelial cells (HEVEC). In the kidney, mediates chloride-bicarbonate
CC       exchange, facilitating V-ATPase-mediated acid secretion. May function
CC       as a chloride channel, playing an important role in moderating chloride
CC       homeostasis and neuronal activity in the cerebellum.
CC       {ECO:0000256|ARBA:ARBA00054369}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogencarbonate(in) + chloride(out) = hydrogencarbonate(out)
CC         + chloride(in); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:17996; Evidence={ECO:0000256|ARBA:ARBA00049347};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxalate(in) + chloride(out) = oxalate(out) + chloride(in);
CC         Xref=Rhea:RHEA:72263, ChEBI:CHEBI:17996, ChEBI:CHEBI:30623;
CC         Evidence={ECO:0000256|ARBA:ARBA00052349};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sulfate(in) + H(+)(in) = sulfate(out) + H(+)(out);
CC         Xref=Rhea:RHEA:28574, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189;
CC         Evidence={ECO:0000256|ARBA:ARBA00050316};
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004424}. Basolateral cell membrane
CC       {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004554}. Lysosome membrane
CC       {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004155}.
CC   -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC       {ECO:0000256|ARBA:ARBA00008692}.
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DR   EMBL; AJFE02110121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02110122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_063455516.1; XM_063599446.1.
DR   RefSeq; XP_063455517.1; XM_063599447.1.
DR   AlphaFoldDB; A0A2R9CAF4; -.
DR   STRING; 9597.ENSPPAP00000038839; -.
DR   Ensembl; ENSPPAT00000061748.1; ENSPPAP00000038839.1; ENSPPAG00000042136.1.
DR   GeneID; 100980279; -.
DR   CTD; 284129; -.
DR   GeneTree; ENSGT01150000286920; -.
DR   OMA; IPETAGF; -.
DR   Proteomes; UP000240080; Chromosome 17.
DR   Bgee; ENSPPAG00000042136; Expressed in adult mammalian kidney and 6 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:Ensembl.
DR   GO; GO:0140900; F:chloride:bicarbonate antiporter activity; IEA:Ensembl.
DR   GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR   FunFam; 3.30.750.24:FF:000013; Solute carrier family 26 member 11; 1.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
DR   InterPro; IPR018045; S04_transporter_CS.
DR   InterPro; IPR011547; SLC26A/SulP_dom.
DR   InterPro; IPR001902; SLC26A/SulP_fam.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR   Pfam; PF01740; STAS; 1.
DR   Pfam; PF00916; Sulfate_transp; 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 1.
DR   PROSITE; PS01130; SLC26A; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   3: Inferred from homology;
KW   Anion exchange {ECO:0000256|ARBA:ARBA00022681};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        52..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        156..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        199..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        308..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        341..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        398..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        440..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          480..564
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
SQ   SEQUENCE   606 AA;  65169 MW;  AD5D899DF7FF2177 CRC64;
     MPSSVTALGQ ARSSGPGMAP SACCCSPAAV QRRLPILAWL PSYSLQWLKM DFVAGLSVGL
     TAIPQALAYA EVAGLPPQYG LYSAFMGCFV YFFLGTSRDV TLGPTAIMSL LVSFYTFHEP
     AYAVLLAFLS GCIQLAMGLL RLGFLLDFIS YPVIKGFTSA AAVTIGFGQI KNLLGLQNIP
     RPFFLQVYHT FLRIAETSVG DAVLGLVCML LLLVLKLMRD HVPPVHPEMP PGVRLSRGLV
     WAATTARNAL VVSFAALVAY SFEVTGYQPF ILTGETAEGL PPVRIPPFSV TTANGTISFT
     KMVQDMGAGL AVVPLMGLLE SIAVAKAFAS QNNYRIDANQ ELLAIGLTNM LGSLVSSYPV
     TGSFGRTAVN AQSGVCTPAG GLVTGVLVLL SLDYLTSLFY YIPKSALAAV IIMAVAPLFD
     TKIFRTLWRV KRLDLLPLCV TFLLCFWEVQ YGILAGALVS LLMLLHSAAR PETKVSEGPV
     LVLQPASGLS FPAAEALREE ILSRALEVSP PRCLVLECTH VCSIDYTVVL GLGELLQDFQ
     KQGVALAFVG LQVPVLRVLL SADLKGFQYF STLEEAEKHL RQEPGTQPYN IREDSILDQK
     VALLKA
//