ID S26A8_BOVIN Reviewed; 960 AA.
AC A6QNW6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 08-NOV-2023, entry version 83.
DE RecName: Full=Testis anion transporter 1 {ECO:0000250|UniProtKB:Q96RN1};
DE AltName: Full=Anion exchange transporter;
DE AltName: Full=Solute carrier family 26 member 8;
GN Name=SLC26A8 {ECO:0000250|UniProtKB:Q96RN1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI49037.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI49037.1};
RC TISSUE=Hypothalamus {ECO:0000312|EMBL:AAI49037.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Antiporter that mediates the exchange of sulfate and oxalate
CC against chloride ions across a membrane. Stimulates anion transport
CC activity of CFTR (By similarity). May cooperate with CFTR in the
CC regulation of chloride and bicarbonate ions fluxes required for
CC activation of the ADCY10/PKA pathway during sperm motility and sperm
CC capacitation. May play a role in sperm tail differentiation and
CC motility and hence male fertility (By similarity).
CC {ECO:0000250|UniProtKB:Q8R0C3, ECO:0000250|UniProtKB:Q96RN1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) + sulfate(out) = chloride(out) + sulfate(in);
CC Xref=Rhea:RHEA:75295, ChEBI:CHEBI:16189, ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:Q96RN1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + oxalate(in) = chloride(in) + oxalate(out);
CC Xref=Rhea:RHEA:72263, ChEBI:CHEBI:17996, ChEBI:CHEBI:30623;
CC Evidence={ECO:0000250|UniProtKB:Q96RN1};
CC -!- SUBUNIT: Interacts with RACGAP1. Interacts with CFTR; stimulates anion
CC transport activity of CFTR. {ECO:0000250|UniProtKB:Q96RN1}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q96RN1}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Located at both the annulus
CC and the equatorial segment of the human sperm head.
CC {ECO:0000250|UniProtKB:Q96RN1}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q96RN1}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC149036; AAI49037.1; -; mRNA.
DR RefSeq; NP_001095600.1; NM_001102130.2.
DR AlphaFoldDB; A6QNW6; -.
DR SMR; A6QNW6; -.
DR STRING; 9913.ENSBTAP00000022931; -.
DR GlyCosmos; A6QNW6; 1 site, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000022931; -.
DR GeneID; 530509; -.
DR KEGG; bta:530509; -.
DR CTD; 116369; -.
DR eggNOG; KOG0236; Eukaryota.
DR InParanoid; A6QNW6; -.
DR OrthoDB; 1067648at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097227; C:sperm annulus; ISS:UniProtKB.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0160044; F:sulfate:chloride antiporter activity; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0008272; P:sulfate transport; ISS:UniProtKB.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
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 PANTHER; PTHR11814:SF11; TESTIS ANION TRANSPORTER 1; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS50801; STAS; 1.
PE 2: Evidence at transcript level;
KW Anion exchange; Developmental protein; Differentiation; Glycoprotein;
KW Ion transport; Meiosis; Membrane; Reference proteome; Spermatogenesis;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..960
FT /note="Testis anion transporter 1"
FT /id="PRO_0000322585"
FT TOPO_DOM 1..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..353
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..427
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..960
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 541..792
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 662..957
FT /note="Interaction with RACGAP1"
FT /evidence="ECO:0000250|UniProtKB:Q96RN1"
FT REGION 807..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..901
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 960 AA; 108744 MW; 2F661CE4C68D8E81 CRC64;
MQPDRSFQSF ASRYRQSSFT YDVKRDVYNE ENFQQEHRKK TASSGNVDID ISTVSHHVQC
RCSWHKFRRC LLTVFPFLEW MCFYRFKDWL LGDLLAGISV GLVQIPQVLM LGLLARHLIP
PLNVSYAAFC ASVIYGIFGS CHQMSIGTFF LVSALAINVL RTQPFNRGHL LLGTFIQADF
SNTSFYENYN RSLSSVASVT LLTGIIQLSM GMLGFGFIVA YIPEAAISAY LAATALHVML
SQLTCIFGIM ISYNSGPIAF FYNIINYCLG LPKANSTSIL LFLTAMVALR INKCIRISFN
EYPIEFPMEV FLVLGFAAFS NKVNMATENS LMLMEMIPYS FLFPVTPDMS NLTEVLIESF
SLALVSSSLL VFLGKKIASF HNYDVNSNQD LIAIGLCNVV SSFFRSYVFT GAVARTIIQD
KTGGRQQFAS LVGAGIMLLL MMKMARFFYR LPNAIVAGII LSNVLPYLEA VYTLPSLWRQ
NQYDCLIWMV TFMSAILLGL DIGLVVAVTF AFFIITVQSH RTKILLLGQI PNTNIYRSFQ
DYREVANIPG VKIFQCCNAI TFVNVHYLKR KVLEEIEMVK MPLTEEEIYT LFSQNEEGAQ
RGKICRCYCN CDEPEPSPRV IYTERYEVQR GRESSFINLV RCSRFESMNT AQTMSEDQVP
YITSSSSQRN PNYEEVEKVW LSDDPSRSMT ITLPEASDTQ VRATKLLPYS TSTILPSIHT
IILDFSMVHL VDARALVVLR QMFSAFQNAN ILVLIAGCHS FVVRSLEKND FFDAGITKAQ
LFLTLHDAVL FALSRKLPES SELSVDESET VIQETFSETD KKEESRHKTN RSLIEAPRSK
SPGFSLLPDP EMEEESDLDL YSTIQMSKDH GLDLDLDLDR EVEPESELEP ESELDQETEL
EPEPEASPKP NRQKYWSLFR AIIPRSPTQT QARTQSVDRR HQNVKPYTSK ADTSEDALEI
//
