S26A8_MOUSE
ID S26A8_MOUSE Reviewed; 999 AA.
AC Q8R0C3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 132.
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:0000312|EMBL:AAH27076.1};
GN Synonyms=Tat1 {ECO:0000303|PubMed:17517695};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH27076.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:15489334};
RC TISSUE=Retina {ECO:0000312|EMBL:AAH27076.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17517695; DOI=10.1093/hmg/ddm117;
RA Toure A., Lhuillier P., Gossen J.A., Kuil C.W., Lhote D., Jegou B.,
RA Escalier D., Gacon G.;
RT "The testis anion transporter 1 (Slc26a8) is required for sperm terminal
RT differentiation and male fertility in the mouse.";
RL Hum. Mol. Genet. 16:1783-1793(2007).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=22121115; DOI=10.1093/hmg/ddr558;
RA Rode B., Dirami T., Bakouh N., Rizk-Rabin M., Norez C., Lhuillier P.,
RA Lores P., Jollivet M., Melin P., Zvetkova I., Bienvenu T., Becq F.,
RA Planelles G., Edelman A., Gacon G., Toure A.;
RT "The testis anion transporter TAT1 (SLC26A8) physically and functionally
RT interacts with the cystic fibrosis transmembrane conductance regulator
RT channel: a potential role during sperm capacitation.";
RL Hum. Mol. Genet. 21:1287-1298(2012).
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. May form a
CC molecular complex involved in the regulation of chloride and
CC bicarbonate ions fluxes during sperm capacitation (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:17517695}.
CC -!- SUBUNIT: Interacts with RACGAP1. Interacts with CFTR. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17517695}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:17517695}. Note=Located at
CC the annulus ring structure within the sperm cell.
CC {ECO:0000269|PubMed:17517695}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R0C3-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q8R0C3-2; Sequence=VSP_052702, VSP_052703;
CC -!- TISSUE SPECIFICITY: Expressed in testis and epididymis. Located at the
CC end of the midpiece of the flagella, known as the annulus, in
CC spermatozoa. {ECO:0000269|PubMed:17517695}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q96RN1}.
CC -!- DISRUPTION PHENOTYPE: Sperm lacks motility and displayed a capacitation
CC defect, with reduced cAMP concentration due to misactivation of soluble
CC adenylate cyclase (see Adcy1). {ECO:0000269|PubMed:22121115}.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to a partial intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000255}.
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DR EMBL; AC170998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027076; AAH27076.1; ALT_SEQ; mRNA.
DR CCDS; CCDS70779.1; -. [Q8R0C3-1]
DR RefSeq; NP_001277249.1; NM_001290320.1. [Q8R0C3-1]
DR AlphaFoldDB; Q8R0C3; -.
DR SMR; Q8R0C3; -.
DR BioGRID; 230299; 2.
DR IntAct; Q8R0C3; 1.
DR STRING; 10090.ENSMUSP00000110412; -.
DR GlyGen; Q8R0C3; 1 site.
DR iPTMnet; Q8R0C3; -.
DR PhosphoSitePlus; Q8R0C3; -.
DR PaxDb; Q8R0C3; -.
DR PRIDE; Q8R0C3; -.
DR ProteomicsDB; 253376; -. [Q8R0C3-1]
DR ProteomicsDB; 253377; -. [Q8R0C3-2]
DR Antibodypedia; 29584; 104 antibodies from 17 providers.
DR DNASU; 224661; -.
DR Ensembl; ENSMUST00000114764; ENSMUSP00000110412; ENSMUSG00000036196. [Q8R0C3-1]
DR Ensembl; ENSMUST00000145224; ENSMUSP00000156853; ENSMUSG00000036196. [Q8R0C3-2]
DR GeneID; 224661; -.
DR KEGG; mmu:224661; -.
DR UCSC; uc008brk.1; mouse. [Q8R0C3-2]
DR UCSC; uc056zdz.1; mouse. [Q8R0C3-1]
DR CTD; 116369; -.
DR MGI; MGI:2385046; Slc26a8.
DR VEuPathDB; HostDB:ENSMUSG00000036196; -.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244925; -.
DR HOGENOM; CLU_003182_9_3_1; -.
DR InParanoid; Q8R0C3; -.
DR OMA; RINKCIK; -.
DR OrthoDB; 289441at2759; -.
DR PhylomeDB; Q8R0C3; -.
DR TreeFam; TF313784; -.
DR BioGRID-ORCS; 224661; 3 hits in 49 CRISPR screens.
DR ChiTaRS; Slc26a8; mouse.
DR PRO; PR:Q8R0C3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8R0C3; protein.
DR Bgee; ENSMUSG00000036196; Expressed in spermatocyte and 86 other tissues.
DR ExpressionAtlas; Q8R0C3; baseline and differential.
DR Genevisible; Q8R0C3; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:0005254; F:chloride channel activity; ISO:MGI.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0019531; F:oxalate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0006820; P:anion transport; ISO:MGI.
DR GO; GO:0006821; P:chloride transport; ISO:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0019532; P:oxalate transport; ISO:MGI.
DR GO; GO:0048240; P:sperm capacitation; IEA:InterPro.
DR GO; GO:0008272; P:sulfate transport; ISO:MGI.
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 Alternative splicing; Anion exchange; Developmental protein;
KW Differentiation; Glycoprotein; Ion transport; Meiosis; Membrane;
KW Reference proteome; Spermatogenesis; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..999
FT /note="Testis anion transporter 1"
FT /id="PRO_0000322588"
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..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..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..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..999
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 541..796
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 661..999
FT /note="Interaction with RACGAP1"
FT /evidence="ECO:0000250|UniProtKB:Q96RN1"
FT REGION 678..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..945
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 486..521
FT /note="IIWMVTFSSAILLGLDVGLLISLAFTFFVITIRSHR -> VSTDASSGCNLG
FT VRGAEAHTHTLPHGQFPGLDPWGQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052702"
FT VAR_SEQ 522..999
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052703"
SQ SEQUENCE 999 AA; 112978 MW; 2664974E42D4996D CRC64;
MQTERSLQSF SNRYTQIPFV YDVKRSVYNE ENFQQEHRKK GPTSGNVDID ITTFKHHVQC
GCSWHKFLRC MLTVFPFLEW ICLYRFKDWL LGDLLAGLSV GLVQVPQGLI LSLLTRQLIP
PLNVTYAAFC SSVIYVIFGS CHQMSIGPFF LVSALMINVL KDRPFNNGHL ILGTFVKDDF
SVPTFYLSYN RSLSMVASTT FLTGIIQLSM GMLGMGFMAT YLPEAATSAY LAAVALHIIL
AQMTCILGIM VSFHAGPISF IYNIINYCIA LPKANSTSIL LFITSVVALR INKCIRITFN
RYPIEFPMEL LLILGFSLLT SKITMATENS KMLMNMIPYS FVFPENPEFG ILSRVVLQAL
SLSFVSSFLL ISLGKKIANF HNYRTNSNQD LIAIGLCNLL SSFFKCCVFT GSLSRTTIQD
KSGGRQQFAS LVGAGVMLLL MVKMESFFHN LPNAVLAGII LSNVVPYLEA IYNLPSLWRQ
DQYECIIWMV TFSSAILLGL DVGLLISLAF TFFVITIRSH RTKILVLGQI PNTNIYRNVN
DYREVILIPG VKIFQCCSSI TFVNVYHLKQ KVLKEVNMVK LPLKEEEIYT LFHESETSIA
ENKLCRCFCD CEELEPEIRV VYTERYENRQ EQDSSINLIR CSYLGSGDSS QVTSEEQIPY
TVSSTSQRNI VQSYEDTEKA WLPNSPPRNS PLPPPEASES LAQSRSRSII MPYSDTSVQN
NTHTIILDFS MVHYVDNRAL VILRQMCNAF YNANILVLIS GCHTSVVKSF EKNDFFDEGI
TKAQLFLSLH DAVLFALSRK FSEPSDLSMD ETETVIQETY SESDKNGNLS NLRLKTGKAI
IEGSQHASPG FTKNLKPGKD DLEFDLELDP MLSFEQSSGM DLNLDLDLDL DQSELDPGSE
LDSEIQAKPE LELESELETD AQTEPETEEE PELEPEPEPE PETEPEPEPE RERKTRTRSQ
SPWRNYFTAY RFGSSNSQSR APPQTRPEKR KPHNYPNSP
