ID A0A3L8SH50_CHLGU Unreviewed; 728 AA.
AC A0A3L8SH50;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Prestin {ECO:0000256|ARBA:ARBA00040148};
DE AltName: Full=Solute carrier family 26 member 5 {ECO:0000256|ARBA:ARBA00042390};
GN ORFNames=DV515_00007529 {ECO:0000313|EMBL:RLW02012.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW02012.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW02012.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW02012.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW02012.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW02012.1}.
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DR EMBL; QUSF01000020; RLW02012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SH50; -.
DR STRING; 44316.ENSEGOP00005006463; -.
DR Ensembl; ENSEGOT00005007343; ENSEGOP00005006463; ENSEGOG00005005000.
DR OMA; ICWGLVD; -.
DR Proteomes; UP000276834; 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:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR InterPro; IPR018045; S04_transporter_CS.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR NCBIfam; TIGR00815; sulP; 1.
DR PANTHER; PTHR11814:SF32; PRESTIN; 1.
DR PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS01130; SLC26A; 1.
DR PROSITE; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362052};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362052};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362052}.
FT TRANSMEM 100..127
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 133..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 184..211
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 249..280
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 292..313
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 475..507
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 531..726
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
SQ SEQUENCE 728 AA; 80149 MW; D129E2FE3A240D5F CRC64;
MEHAQEQEVC LEQTQRYCVQ RPIYNQELLQ GQLHRRQRTP QTLGQRIAHS CRCSSKKAKS
HLYSFLPILK WLPRYPVKEY LLGDIISGIS TGVMQLPQGL AYALLAAVPP VFGLYSSFYP
VFLYTFFGTS KHISIGTFAV VSMMVGSVAV REVPDEIISL DSNSTNTTDV LEYYSARDAK
RVQVAVALAF LSGIIQLCLG FLRFGFLSIY LTEPLVRGFT TAAAVHVFTS QLKYLLGIKT
SRYSGPLSVV YSIAAVLSKI TTTNIAALIV GLTCIVLLLI GKEINFRFKK KLPVPIPMEI
IVVIIGTGVS AGMNLNESYK VDVVGNIPQG LRAPAVPEIH LIPAIFVDAV AIAIVGFSMA
VSMAKIFALK HGYTIDGNQE LIALGICNSV GSFFQTISIT CSMSRSLVQE STGGKTQIAG
TLSAVMVLLV IVAIGYLFEP LPQTVLAAIV MVNLKGMLKQ FGDVMHFWRT SKIELAIWVA
AFVASLFLGL DYGLLTAVTF AMITVIYRTQ SPEYRILGQI PNTDIYCDVE EYEEVKEYPG
IKIFQANTSL YFANSESYTR ALKKKTGVDP GALLKARRKA QKRHTREIKA ANEHRKKAVL
KLVSPSTNDI EASVKHEIAS DDLPVNGKLE DSSVQDMSPD EHEHFVEPKS SIHSLILDFT
PVNFVDSVGA KTLKSIIKEY KEVGVCVCIA SCSGPVMNEL TRLNFFDKSV TRELLFHSIH
DAVLASQV
//