ID S26A8_HUMAN Reviewed; 970 AA. AC Q96RN1; Q5JVR5; Q812C7; Q8TC65; Q96MA0; Q96PK8; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 169. DE RecName: Full=Testis anion transporter 1 {ECO:0000303|PubMed:11278976}; DE AltName: Full=Anion exchange transporter; DE AltName: Full=Solute carrier family 26 member 8; GN Name=SLC26A8 {ECO:0000312|EMBL:AAK95666.1}; GN Synonyms=TAT1 {ECO:0000303|PubMed:11278976}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY, RP ACTIVITY REGULATION, INTERACTION WITH RACGAP1, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, INDUCTION, GLYCOSYLATION, AND VARIANT MET-73. RC TISSUE=Testis {ECO:0000269|PubMed:11278976}; RX PubMed=11278976; DOI=10.1074/jbc.m011740200; RA Toure A., Morin L., Pineau C., Becq F., Dorseuil O., Gacon G.; RT "Tat1, a novel sulfate transporter specifically expressed in human male RT germ cells and potentially linked to rhogtpase signaling."; RL J. Biol. Chem. 276:20309-20315(2001). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK95666.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY, RP TISSUE SPECIFICITY, AND INHIBITION. RX PubMed=11834742; DOI=10.1074/jbc.m111802200; RA Lohi H., Kujala M., Maekelae S., Lehtonen E., Kestilae M., RA Saarialho-Kere U., Markovich D., Kere J.; RT "Functional characterization of three novel tissue-specific anion RT exchangers SLC26A7, -A8, and -A9."; RL J. Biol. Chem. 277:14246-14254(2002). RN [3] {ECO:0000305, ECO:0000312|EMBL:AAL26868.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS MET-73; VAL-148; RP ASN-230 AND VAL-639. RA Mount D.B.; RT "Cloning of human SLC26A8, a new member of the sulphate transporter gene RT family of anion transporter/exchangers."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000312|EMBL:Z95152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] {ECO:0000305, ECO:0000312|EMBL:AAL26868.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000305, ECO:0000312|EMBL:AAH25408.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS MET-73 AND RP VAL-639. RC TISSUE=Testis {ECO:0000312|EMBL:AAH25408.1}; 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 [7] {ECO:0000305, ECO:0000312|EMBL:BAB71408.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 450-768 (ISOFORM 4). RC TISSUE=Testis {ECO:0000312|EMBL:BAB71408.1}; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP INTERACTION WITH CFTR. 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). RN [9] {ECO:0000305} RP VARIANTS MET-73; VAL-148; ASN-230 AND VAL-639, AND MUTAGENESIS OF PRO-914. RX PubMed=15579655; DOI=10.1093/molehr/gah140; RA Makela S., Eklund R., Lahdetie J., Mikkola M., Hovatta O., Kere J.; RT "Mutational analysis of the human SLC26A8 gene: exclusion as a candidate RT for male infertility due to primary spermatogenic failure."; RL Mol. Hum. Reprod. 11:129-132(2005). RN [10] {ECO:0000305} RP SUBCELLULAR LOCATION. 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 [11] RP VARIANTS SPGF3 GLN-87; LYS-812 AND CYS-954, CHARACTERIZATION OF VARIANTS RP SPGF3 GLN-87; LYS-812 AND CYS-954, FUNCTION, INTERACTION WITH CFTR, AND RP SUBCELLULAR LOCATION. RX PubMed=23582645; DOI=10.1016/j.ajhg.2013.03.016; RA Dirami T., Rode B., Jollivet M., Da Silva N., Escalier D., Gaitch N., RA Norez C., Tuffery P., Wolf J.P., Becq F., Ray P.F., Dulioust E., Gacon G., RA Bienvenu T., Toure A.; RT "Missense mutations in SLC26A8, encoding a sperm-specific activator of RT CFTR, are associated with human asthenozoospermia."; RL Am. J. Hum. Genet. 92:760-766(2013). CC -!- FUNCTION: Antiporter that mediates the exchange of sulfate and oxalate CC against chloride ions across a membrane (PubMed:11834742, CC PubMed:11278976). Stimulates anion transport activity of CFTR CC (PubMed:22121115, PubMed:23582645). 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 (By similarity). May play a role in sperm tail CC differentiation and motility and hence male fertility (By similarity). CC {ECO:0000250|UniProtKB:Q8R0C3, ECO:0000269|PubMed:11278976, CC ECO:0000269|PubMed:11834742, ECO:0000269|PubMed:22121115, CC ECO:0000269|PubMed:23582645}. 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:0000269|PubMed:11278976, ECO:0000305|PubMed:11834742}; 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:0000305|PubMed:11834742}; CC -!- ACTIVITY REGULATION: Activity is inhibited by 4,4'-Di- CC isothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of CC several anion channels and transporters) and gluconate. CC {ECO:0000269|PubMed:11278976}. CC -!- SUBUNIT: Interacts with RACGAP1 (PubMed:11278976). Interacts with CFTR; CC stimulates anion transport activity of CFTR (PubMed:22121115, CC PubMed:23582645). {ECO:0000269|PubMed:11278976, CC ECO:0000269|PubMed:22121115, ECO:0000269|PubMed:23582645}. CC -!- INTERACTION: CC Q96RN1; P13569: CFTR; NbExp=2; IntAct=EBI-1792052, EBI-349854; CC Q96RN1; Q9H0H5: RACGAP1; NbExp=2; IntAct=EBI-1792052, EBI-717233; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11278976}; 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:0000269|PubMed:17517695, ECO:0000269|PubMed:22121115, CC ECO:0000269|PubMed:23582645}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1 {ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:11834742, CC ECO:0000269|Ref.3}; CC IsoId=Q96RN1-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:15489334}; CC IsoId=Q96RN1-2; Sequence=VSP_052705; CC Name=3 {ECO:0000269|PubMed:14574404}; CC IsoId=Q96RN1-3; Sequence=VSP_052704, VSP_052706; CC Name=4 {ECO:0000269|PubMed:14702039}; CC IsoId=Q96RN1-4; Sequence=VSP_052707, VSP_052708; CC -!- TISSUE SPECIFICITY: Expression observed exclusively in testis, CC restricted to the meiotic phase of the germ cell (PubMed:11834742). CC Abundant expression located in the seminiferous tubules, concentrated CC on the luminal side of the tubuli harboring the spermatocytes and CC spermatids (PubMed:11834742, PubMed:11278976). CC {ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:11834742}. CC -!- INDUCTION: Repressed by tunicamycin, an inhibitor of N-glycosylation. CC {ECO:0000269|PubMed:11278976}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11278976}. CC -!- DISEASE: Spermatogenic failure 3 (SPGF3) [MIM:606766]: A disorder CC characterized by primary infertility, sperm morphologic abnormalities, CC and moderate to severe asthenozoospermia, condition in which the CC percentage of progressively motile sperm is abnormally low. CC {ECO:0000269|PubMed:23582645}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family. CC {ECO:0000255}. CC -!- SEQUENCE CAUTION: CC Sequence=AAO26699.1; Type=Miscellaneous discrepancy; Note=Incorrectly indicated as originating from mouse.; Evidence={ECO:0000305}; CC Sequence=BAB71408.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; AF331522; AAK95666.1; -; mRNA. DR EMBL; AF314959; AAL26868.1; -; mRNA. DR EMBL; AF403499; AAO26699.1; ALT_SEQ; mRNA. DR EMBL; AL133507; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z95152; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03862.1; -; Genomic_DNA. DR EMBL; BC025408; AAH25408.1; -; mRNA. DR EMBL; AK057276; BAB71408.1; ALT_INIT; mRNA. DR CCDS; CCDS4813.1; -. [Q96RN1-1] DR CCDS; CCDS4814.1; -. [Q96RN1-2] DR RefSeq; NP_001180405.1; NM_001193476.1. [Q96RN1-1] DR RefSeq; NP_443193.1; NM_052961.3. [Q96RN1-1] DR RefSeq; NP_619732.2; NM_138718.2. [Q96RN1-2] DR RefSeq; XP_016865724.1; XM_017010235.1. [Q96RN1-1] DR AlphaFoldDB; Q96RN1; -. DR EMDB; EMD-33284; -. DR SMR; Q96RN1; -. DR BioGRID; 125501; 2. DR IntAct; Q96RN1; 2. DR STRING; 9606.ENSP00000347778; -. DR TCDB; 2.A.53.2.14; the sulfate permease (sulp) family. DR GlyCosmos; Q96RN1; 1 site, No reported glycans. DR GlyGen; Q96RN1; 1 site. DR iPTMnet; Q96RN1; -. DR PhosphoSitePlus; Q96RN1; -. DR BioMuta; SLC26A8; -. DR DMDM; 74761075; -. DR EPD; Q96RN1; -. DR MassIVE; Q96RN1; -. DR PaxDb; 9606-ENSP00000417638; -. DR PeptideAtlas; Q96RN1; -. DR ProteomicsDB; 77989; -. [Q96RN1-1] DR ProteomicsDB; 77990; -. [Q96RN1-2] DR ProteomicsDB; 77991; -. [Q96RN1-3] DR ProteomicsDB; 77992; -. [Q96RN1-4] DR Antibodypedia; 29584; 117 antibodies from 18 providers. DR DNASU; 116369; -. DR Ensembl; ENST00000355574.6; ENSP00000347778.2; ENSG00000112053.14. [Q96RN1-1] DR Ensembl; ENST00000394602.6; ENSP00000378100.2; ENSG00000112053.14. [Q96RN1-2] DR Ensembl; ENST00000490799.6; ENSP00000417638.1; ENSG00000112053.14. [Q96RN1-1] DR GeneID; 116369; -. DR KEGG; hsa:116369; -. DR MANE-Select; ENST00000490799.6; ENSP00000417638.1; NM_052961.4; NP_443193.1. DR UCSC; uc003oll.4; human. [Q96RN1-1] DR AGR; HGNC:14468; -. DR CTD; 116369; -. DR DisGeNET; 116369; -. DR GeneCards; SLC26A8; -. DR HGNC; HGNC:14468; SLC26A8. DR HPA; ENSG00000112053; Tissue enriched (testis). DR MalaCards; SLC26A8; -. DR MIM; 606766; phenotype. DR MIM; 608480; gene. DR neXtProt; NX_Q96RN1; -. DR OpenTargets; ENSG00000112053; -. DR Orphanet; 276234; Non-syndromic male infertility due to sperm motility disorder. DR PharmGKB; PA37885; -. DR VEuPathDB; HostDB:ENSG00000112053; -. DR eggNOG; KOG0236; Eukaryota. DR GeneTree; ENSGT01100000263544; -. DR HOGENOM; CLU_003182_9_3_1; -. DR InParanoid; Q96RN1; -. DR OMA; RINKCIK; -. DR OrthoDB; 1067648at2759; -. DR PhylomeDB; Q96RN1; -. DR TreeFam; TF313784; -. DR PathwayCommons; Q96RN1; -. DR SignaLink; Q96RN1; -. DR BioGRID-ORCS; 116369; 18 hits in 1138 CRISPR screens. DR ChiTaRS; SLC26A8; human. DR GeneWiki; SLC26A8; -. DR GenomeRNAi; 116369; -. DR Pharos; Q96RN1; Tbio. DR PRO; PR:Q96RN1; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q96RN1; Protein. DR Bgee; ENSG00000112053; Expressed in left testis and 100 other cell types or tissues. DR ExpressionAtlas; Q96RN1; baseline and differential. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0097227; C:sperm annulus; IDA:UniProtKB. DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0005254; F:chloride channel activity; IDA:UniProtKB. DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0160044; F:sulfate:chloride antiporter activity; IDA:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB. DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW. DR GO; GO:0019532; P:oxalate transport; IDA:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW. DR GO; GO:0008272; P:sulfate transport; IDA: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. DR Genevisible; Q96RN1; HS. PE 1: Evidence at protein 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..970 FT /note="Testis anion transporter 1" FT /id="PRO_0000322586" FT TOPO_DOM 1..95 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 96..116 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 117..119 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 120..140 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 141..146 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 147..167 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 168..202 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 203..223 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 224..232 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 233..253 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 254..270 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 271..291 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 292..307 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 308..328 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 329..355 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 356..376 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 377..392 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 393..413 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 414..429 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 430..450 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 451..452 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 453..473 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 474..497 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 498..518 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 519..970 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 543..795 FT /note="STAS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198" FT REGION 664..970 FT /note="Interaction with RACGAP1" FT /evidence="ECO:0000269|PubMed:11278976" FT REGION 858..970 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 858..872 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 873..916 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 932..947 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 192 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 2..419 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14574404" FT /id="VSP_052704" FT VAR_SEQ 210..314 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_052705" FT VAR_SEQ 420..428 FT /note="IQDKSGGRQ -> VSLQLALSP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14574404" FT /id="VSP_052706" FT VAR_SEQ 745..768 FT /note="ICNAFQNANILILIAGCHSSIVRA -> VSTEEALAGALIPLLPSQPHPDPD FT (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_052707" FT VAR_SEQ 769..970 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_052708" FT VARIANT 73 FT /note="V -> M (not a cause of male infertility; FT dbSNP:rs743923)" FT /evidence="ECO:0000269|PubMed:11278976, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15579655, FT ECO:0000269|Ref.3" FT /id="VAR_039464" FT VARIANT 87 FT /note="R -> Q (in SPGF3; there is a reduced interactions FT with CFTR and complete failure to activate CFTR-dependent FT anion transport; dbSNP:rs140210148)" FT /evidence="ECO:0000269|PubMed:23582645" FT /id="VAR_070058" FT VARIANT 148 FT /note="I -> V (not a cause of male infertility; FT dbSNP:rs17713154)" FT /evidence="ECO:0000269|PubMed:15579655, ECO:0000269|Ref.3" FT /id="VAR_039465" FT VARIANT 230 FT /note="S -> N (not a cause of male infertility; FT dbSNP:rs17707331)" FT /evidence="ECO:0000269|PubMed:15579655, ECO:0000269|Ref.3" FT /id="VAR_039466" FT VARIANT 639 FT /note="I -> V (not a cause of male infertility; FT dbSNP:rs2295852)" FT /evidence="ECO:0000269|PubMed:11278976, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15579655, FT ECO:0000269|Ref.3" FT /id="VAR_039467" FT VARIANT 812 FT /note="E -> K (in SPGF3; there is a reduced interactions FT with CFTR and complete failure to activate CFTR-dependent FT anion transport; dbSNP:rs142724470)" FT /evidence="ECO:0000269|PubMed:23582645" FT /id="VAR_070059" FT VARIANT 954 FT /note="R -> C (in SPGF3; there is a reduced interactions FT with CFTR and complete failure to activate CFTR-dependent FT anion transport; dbSNP:rs398123027)" FT /evidence="ECO:0000269|PubMed:23582645" FT /id="VAR_070060" FT MUTAGEN 914 FT /note="P->S: Not a cause of male infertility." FT /evidence="ECO:0000269|PubMed:15579655" FT CONFLICT 168 FT /note="N -> D (in Ref. 3; AAL26868/AAO26699)" FT /evidence="ECO:0000305" FT CONFLICT 560 FT /note="S -> C (in Ref. 3; AAL26868/AAO26699)" FT /evidence="ECO:0000305" SQ SEQUENCE 970 AA; 109006 MW; 7F932A9CFE3A9EC4 CRC64; MAQLERSAIS GFSSKSRRNS FAYDVKREVY NEETFQQEHK RKASSSGNMN INITTFRHHV QCRCSWHRFL RCVLTIFPFL EWMCMYRLKD WLLGDLLAGI SVGLVQVPQG LTLSLLARQL IPPLNIAYAA FCSSVIYVIF GSCHQMSIGS FFLVSALLIN VLKVSPFNNG QLVMGSFVKN EFSAPSYLMG YNKSLSVVAT TTFLTGIIQL IMGVLGLGFI ATYLPESAMS AYLAAVALHI MLSQLTFIFG IMISFHAGPI SFFYDIINYC VALPKANSTS ILVFLTVVVA LRINKCIRIS FNQYPIEFPM ELFLIIGFTV IANKISMATE TSQTLIDMIP YSFLLPVTPD FSLLPKIILQ AFSLSLVSSF LLIFLGKKIA SLHNYSVNSN QDLIAIGLCN VVSSFFRSCV FTGAIARTII QDKSGGRQQF ASLVGAGVML LLMVKMGHFF YTLPNAVLAG IILSNVIPYL ETISNLPSLW RQDQYDCALW MMTFSSSIFL GLDIGLIISV VSAFFITTVR SHRAKILLLG QIPNTNIYRS INDYREIITI PGVKIFQCCS SITFVNVYYL KHKLLKEVDM VKVPLKEEEI FSLFNSSDTN LQGGKICRCF CNCDDLEPLP RILYTERFEN KLDPEASSIN LIHCSHFESM NTSQTASEDQ VPYTVSSVSQ KNQGQQYEEV EEVWLPNNSS RNSSPGLPDV AESQGRRSLI PYSDASLLPS VHTIILDFSM VHYVDSRGLV VLRQICNAFQ NANILILIAG CHSSIVRAFE RNDFFDAGIT KTQLFLSVHD AVLFALSRKV IGSSELSIDE SETVIRETYS ETDKNDNSRY KMSSSFLGSQ KNVSPGFIKI QQPVEEESEL DLELESEQEA GLGLDLDLDR ELEPEMEPKA ETETKTQTEM EPQPETEPEM EPNPKSRPRA HTFPQQRYWP MYHPSMASTQ SQTQTRTWSV ERRRHPMDSY SPEGNSNEDV //