S26A4_RAT
ID S26A4_RAT Reviewed; 780 AA.
AC Q9R154;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Pendrin;
DE AltName: Full=Sodium-independent chloride/iodide transporter;
DE AltName: Full=Solute carrier family 26 member 4;
GN Name=Slc26a4; Synonyms=Pds;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=10449762; DOI=10.1073/pnas.96.17.9727;
RA Everett L.A., Morsli H., Wu D.K., Green E.D.;
RT "Expression pattern of the mouse ortholog of the Pendred's syndrome gene
RT (Pds) suggests a key role for pendrin in the inner ear.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9727-9732(1999).
CC -!- FUNCTION: Sodium-independent transporter of chloride and iodide.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cell membrane; Multi-pass membrane protein.
CC Note=Localizes to the apical brush border of cells in the cortical
CC collecting ducts of the kidney. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000305}.
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DR EMBL; AF167412; AAD51618.1; -; mRNA.
DR RefSeq; NP_062087.1; NM_019214.1.
DR RefSeq; XP_008762798.1; XM_008764576.2.
DR RefSeq; XP_017449543.1; XM_017594054.1.
DR AlphaFoldDB; Q9R154; -.
DR SMR; Q9R154; -.
DR STRING; 10116.ENSRNOP00000010350; -.
DR PaxDb; Q9R154; -.
DR Ensembl; ENSRNOT00000087300; ENSRNOP00000070261; ENSRNOG00000058692.
DR GeneID; 29440; -.
DR KEGG; rno:29440; -.
DR UCSC; RGD:3293; rat.
DR CTD; 5172; -.
DR RGD; 3293; Slc26a4.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244807; -.
DR HOGENOM; CLU_003182_9_4_1; -.
DR InParanoid; Q9R154; -.
DR OMA; KMEQCGF; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; Q9R154; -.
DR TreeFam; TF313784; -.
DR Reactome; R-RNO-427601; Multifunctional anion exchangers.
DR PRO; PR:Q9R154; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000058692; Expressed in kidney and 8 other tissues.
DR Genevisible; Q9R154; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015111; F:iodide transmembrane transporter activity; IDA:RGD.
DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015698; P:inorganic anion transport; IDA:RGD.
DR GO; GO:0006885; P:regulation of pH; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR030285; Pendrin.
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; PTHR11814; 1.
DR PANTHER; PTHR11814:SF33; PTHR11814:SF33; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR TIGRFAMs; TIGR00815; sulP; 1.
DR PROSITE; PS01130; SLC26A; 1.
DR PROSITE; PS50801; STAS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Chloride; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..780
FT /note="Pendrin"
FT /id="PRO_0000080166"
FT TOPO_DOM 1..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..263
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..344
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..421
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..486
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..780
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 535..729
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
SQ SEQUENCE 780 AA; 85715 MW; DA0CDB7496B8D535 CRC64;
MAARDRRSEP PQLAEYSCSY AVSRPVYSEL AFQQQRERRL PERRTLRDSL ARSCSCSRKR
AFGALKALLP ILDWLPKYRV KEWLLSDIIS GVSTGLVGTL QGMAYALLAA VPVQYGLYSA
FFPILTYFVF GTSRHISVGP FPVVSLMVGS VVLSMAPDDH FLVPSGNGST LNTTTLDTGT
RDAARVLLAS TLTLLVGIIQ LVFGGLQIGF IVRYLADPLV GGFTTAAAFQ VLVSQLKIVL
NVSTKNYNGV LSIIYTLIEI FQNIGDTNIA DFIAGLLTII VCMAVKELND RFKHKIPVPI
PIEVIVTIIA TAISYGANLE ANYNAGIVKS IPSGFLPPVL PSVGLFSDML AASFSIAVVA
YAIAVSVGKV YATKHDYIID GNQEFIAFGI SNVFSGFFSC FVATTALSRT AVQESTGGKT
QVAGLISAVI VMVAIVALGK LLEPLQKSVL AAVVIANLKG MFMQVCDVPR LWKQNKTDAV
IWVFTCIMSI ILGLDLGLLA GLLFGLLTVV LRVQFPSWNG LGSVPSTDIY KSITHYKNLE
EPEGVKILRF SSPIFYGNVD GFKKCVKSTV GFDAIRVYNK RLKALRRIQK LIKKGQLRAT
KNGIISDVGS SNNAFEPDED VEEPEELDIP TKEIEIQVDW NSELPVKVNV PKVPIHSLVL
DCGAVSFLDV VGVRSLRMIV KEFQRIDVNV YFALLQDDVL EKMEQCGFFD DNIRKDRFFL
TVHDAILYLQ NQAKSREGQD SLLETITLIQ DCKDPLELME AEINEEELDV QDEAMRRLAS
