ID L5M692_MYODS Unreviewed; 880 AA.
AC L5M692;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 03-MAY-2023, entry version 43.
DE RecName: Full=Testis anion transporter 1 {ECO:0000256|RuleBase:RU362052};
DE AltName: Full=Solute carrier family 26 member 8 {ECO:0000256|RuleBase:RU362052};
GN ORFNames=MDA_GLEAN10010693 {ECO:0000313|EMBL:ELK33800.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK33800.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362052}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362052}.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000256|RuleBase:RU362052}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362052}.
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DR EMBL; KB103811; ELK33800.1; -; Genomic_DNA.
DR AlphaFoldDB; L5M692; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0098661; P:inorganic anion transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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; 2.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW Developmental protein {ECO:0000256|RuleBase:RU362052};
KW Differentiation {ECO:0000256|RuleBase:RU362052};
KW Meiosis {ECO:0000256|RuleBase:RU362052};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362052};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Spermatogenesis {ECO:0000256|RuleBase:RU362052};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362052};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362052}; Transport {ECO:0000256|RuleBase:RU362052}.
FT TRANSMEM 95..119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 163..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 191..215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 267..285
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 305..328
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 366..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 421..704
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 543..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..808
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 880 AA; 99634 MW; B831BAA73A6EC329 CRC64;
MMQPPRSYQD FDSRYRENSY SYDVKRDVYN EETFQQDYRR RSASSGNLDI DITTFKHHIQ
CSCSWDRFLN CMITIFPFLE WMCLYRFKEW LLGDLLAGIS VGLVQIPQGA FFLVSALTID
VLTLYPFNNG HLILGTFLKE DFSDPLFFTA YNQSLSVVAS TTFLTGVIQL LMGMLGFGFI
ATYLPEAAIN AYLTAVALHI IVSQMTSILG IMISFHAGPT AFFYVLGFSA LASKISIATD
TGKTFMDMIP YRFLFPVMPN LDNLRDIVLD AFSLAIVSSS LLVFLGKKIA NFHNYNVNSN
QDLMVIGICN VISSFFRSCV FTGAIIRTMI QDKSGGRQQF ASLIGAGLML LLMVKVESFF
YELPNIIWMV TFTAAIVLGL DVGLMVSVAF AFFVITIQSH RTKILLLGQI PNTNIYRSIQ
DYREILTFPG VKIFQCCNSI TFVNVYDLKH MLLEEVRLPS PLFSTGSPRL PQGPSLLPLA
IYPTTLKPPS AFQVEMVRVP LKEEEVYRLF PAREGGPQEG KMCECYCNCD ELEPPPRVVY
TERYETKQDR KPSSMSMNQG TRMDSGDMSQ YSSEEQIPNT VSSILQRNQG QSYENILLPN
KPYRNDPKPL PDASGSQVRS RSDLSFMPST HTIILDFSMV HFVDSRAVVV LRQMCNAFHN
ANIMVLIAGT HSSVVKAFER NEFFDDGITK TQLFLTLHDA VLFALSRKFS ETSELSVDES
ETVIQETYSD KGRDARQKRS SSILEGPKNL SSSYARMQRP ILEEESDLDV ELEPILESDT
GLDQDLEMER ESELEPESEL EPETELEPEL EPEPKPENEL DLEFKPKPAL KSIPRPQTYP
RQQYWPPSSP SQNPPGTRSV DKRQPYLIPY SSQDSDTEDP
//