S26A8_BOVIN
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 25-MAY-2022, entry version 77.
DE RecName: Full=Testis anion transporter 1;
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: Acts as a DIDS-sensitive anion exchanger mediating chloride,
CC sulfate and oxalate transport. May fulfill critical anion exchange
CC functions in male germ line during meiosis and hence may play a role in
CC spermatogenesis. May be involved in a new regulatory pathway linking
CC sulfate transport to RhoGTPase signaling in male germ cells. A critical
CC component of the sperm annulus that is essential for correct sperm tail
CC differentiation and motility and hence male fertility (By similarity).
CC {ECO:0000250|UniProtKB:Q8R0C3, ECO:0000250|UniProtKB:Q96RN1}.
CC -!- SUBUNIT: Interacts with RACGAP1. {ECO:0000250|UniProtKB:Q96RN1}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8R0C3,
CC ECO:0000250|UniProtKB:Q96RN1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8R0C3, ECO:0000250|UniProtKB:Q96RN1}.
CC Note=Located at the annulus ring structure within the sperm cell.
CC {ECO:0000250|UniProtKB:Q8R0C3, 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}.
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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 PaxDb; A6QNW6; -.
DR GeneID; 530509; -.
DR KEGG; bta:530509; -.
DR CTD; 116369; -.
DR eggNOG; KOG0236; Eukaryota.
DR InParanoid; A6QNW6; -.
DR OrthoDB; 289441at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
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:0030317; P:flagellated sperm motility; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0048240; P:sperm capacitation; IEA:InterPro.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR030303; SLC26A8.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR PANTHER; PTHR11814:SF11; PTHR11814:SF11; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SSF52091; 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
