ID A0A2K5H8A6_COLAP Unreviewed; 788 AA.
AC A0A2K5H8A6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Solute carrier family 26 member 9 {ECO:0000256|RuleBase:RU362052};
DE AltName: Full=Anion transporter/exchanger protein 9 {ECO:0000256|RuleBase:RU362052};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000000588.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000000588.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Ion transporter that can act both as an ion channel and anion
CC exchanger. Mainly acts as a chloride channel, which mediate uncoupled
CC chloride anion transport in an alternate-access mechanism where a
CC saturable binding site is alternately exposed to either one or the
CC other side of the membrane. Also acts as a DIDS- and
CC thiosulfate- sensitive anion exchanger the exchange of chloride for
CC bicarbonate ions across the cell membrane.
CC {ECO:0000256|RuleBase:RU362052}.
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|ARBA:ARBA00008692, ECO:0000256|RuleBase:RU362052}.
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DR RefSeq; XP_011813107.1; XM_011957717.1.
DR AlphaFoldDB; A0A2K5H8A6; -.
DR Ensembl; ENSCANT00000002537.1; ENSCANP00000000588.1; ENSCANG00000001656.1.
DR GeneID; 105523010; -.
DR KEGG; cang:105523010; -.
DR CTD; 115019; -.
DR OMA; WKDMMGT; -.
DR OrthoDB; 1067648at2759; -.
DR Proteomes; UP000233080; Unplaced.
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:0098661; P:inorganic anion transmembrane transport; IEA:UniProtKB-UniRule.
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 NCBIfam; TIGR00815; sulP; 1.
DR PANTHER; PTHR11814:SF17; SOLUTE CARRIER FAMILY 26 MEMBER 9; 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; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362052};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
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 90..117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 174..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 211..232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 252..270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 282..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 333..350
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 370..394
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 406..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 463..495
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 519..734
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
SQ SEQUENCE 788 AA; 86617 MW; 7B0889CAF6E0A95C CRC64;
MSQPRPRYVV DRAAYSLTLF DDEFEKKDRT YPVGEKLRNT FRCSSAKIKA VVFGLLPVLS
WLPKYKIKDY IVPDLLGGLS GGSIQVPQGM AFALLANLPA VNGLYSSFFP LLTYFFLGGV
HQMVPGTFAV ISILVGNICL QLAPESKFQV FNNATNESYV DTAAMEAERL HVSATLACLT
AIIQIGLGFM QFGFVAIYLS ESFIRGFMTA AGLQILISVL KYIFGLTIPS YAGPGSIVFT
FIDICKNLPH TNIASLIFAL ISGAFLVLVK ELNARYMHKI RFPIPTEMIV VVVATAISGG
YKMPKKYHMQ IVGEIQHGFP TPVSPVVSQW KDMIGTAFSL AIVGYVINLA MGRTLANKHG
YDVDSNQEMI ALGCSNFFGS FFKIHVICCA LSVTLAVDGA GGKSQVASLC VSLVVMITML
VLGTYLYPLP KSVLGALIAV NLKNSLKQLT DPYYLWRKSK LDCCIWVVSF LSSFFLSLPY
GVAVGVAFSV LVVVFQTQFR NGYALAQVMD TDIYVNPKTY NRAQDIQGIK IITYCSPLYF
ANSEIFRQKV IAKTGMDPQK VLLAKQKYLK KQEKRRMRPT QQRRSLFMKT KTVSLQELQQ
DFENASPTDP NNNQTQANGT SVSYITFSSS AAQSEPPASP EAPGEPSDTL ASVPPFVTFH
TLILDMSGVS FVDLMGIKAL AKLSSTYGKI GVKVFLVNIH AQVYNDISHG GVFEDGSLEC
KHVFPSIHDA VLFAQANARD VTPGHSFQGA PGDPELSLYD SEEDIPSYWD LEQEMFGSMF
HTETLTAL
//