S26A8_HUMAN
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 03-AUG-2022, entry version 161.
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: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, INTERACTION WITH RACGAP1,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, GLYCOSYLATION, AND
RP 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, TISSUE SPECIFICITY, AND
RP 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 FUNCTION IN SPERM CAPACITATION, AND 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, AND CHARACTERIZATION OF
RP VARIANTS SPGF3 GLN-87; LYS-812 AND CYS-954.
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: 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.
CC {ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:11834742,
CC ECO:0000269|PubMed:22121115}.
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), gluconate, and by
CC thiosulfate.
CC -!- SUBUNIT: Interacts with RACGAP1. Interacts with CFTR.
CC {ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:22121115}.
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,
CC ECO:0000269|PubMed:17517695}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:17517695}.
CC Note=Located at the annulus ring structure within the sperm cell.
CC {ECO:0000269|PubMed:11278976, ECO:0000269|PubMed:17517695}.
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. Abundant expression
CC located in the seminiferous tubules, concentrated on the luminal side
CC of the tubuli harboring the spermatocytes and spermatids. Expressed in
CC spermatozoa. {ECO:0000269|PubMed:11278976,
CC 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};
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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 SMR; Q96RN1; -.
DR BioGRID; 125501; 2.
DR IntAct; Q96RN1; 2.
DR STRING; 9606.ENSP00000417638; -.
DR TCDB; 2.A.53.2.14; the sulfate permease (sulp) family.
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; Q96RN1; -.
DR PeptideAtlas; Q96RN1; -.
DR PRIDE; Q96RN1; -.
DR ProteomicsDB; 77989; -. [Q96RN1-1]
DR ProteomicsDB; 77990; -. [Q96RN1-2]
DR ProteomicsDB; 77991; -. [Q96RN1-3]
DR ProteomicsDB; 77992; -. [Q96RN1-4]
DR Antibodypedia; 29584; 104 antibodies from 17 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 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; ENSGT01050000244925; -.
DR HOGENOM; CLU_003182_9_3_1; -.
DR InParanoid; Q96RN1; -.
DR OMA; RINKCIK; -.
DR PhylomeDB; Q96RN1; -.
DR TreeFam; TF313784; -.
DR PathwayCommons; Q96RN1; -.
DR SignaLink; Q96RN1; -.
DR BioGRID-ORCS; 116369; 16 hits in 1062 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 98 other tissues.
DR ExpressionAtlas; Q96RN1; baseline and differential.
DR Genevisible; Q96RN1; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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; 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:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0006820; P:anion transport; IDA:UniProtKB.
DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0048240; P:sperm capacitation; IEA:InterPro.
DR GO; GO:0008272; P:sulfate transport; IDA:UniProtKB.
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 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
