PACC1_XENLA
ID PACC1_XENLA Reviewed; 350 AA.
AC Q0IHD6;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Proton-activated chloride channel {ECO:0000250|UniProtKB:Q9H813};
DE Short=PAC {ECO:0000250|UniProtKB:Q9H813};
DE AltName: Full=Transmembrane protein 206 {ECO:0000305};
GN Name=pacc1 {ECO:0000250|UniProtKB:Q9H813};
GN Synonyms=tmem206 {ECO:0000250|UniProtKB:Q9H813};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fat body;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Proton-activated chloride channel that mediates import of
CC chloride ion in response to extracellular acidic pH.
CC {ECO:0000250|UniProtKB:Q7SY31}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H813};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H813}.
CC -!- SIMILARITY: Belongs to the proton-activated chloride channel family.
CC {ECO:0000305}.
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DR EMBL; BC123202; AAI23203.1; -; mRNA.
DR RefSeq; NP_001090342.1; NM_001096873.1.
DR AlphaFoldDB; Q0IHD6; -.
DR SMR; Q0IHD6; -.
DR DNASU; 779252; -.
DR GeneID; 779252; -.
DR CTD; 779252; -.
DR Xenbase; XB-GENE-985609; pacc1.L.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 779252; Expressed in internal ear and 16 other tissues.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0061797; F:pH-gated chloride channel activity; ISS:UniProtKB.
DR GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR InterPro; IPR029366; TMEM206.
DR PANTHER; PTHR16087; PTHR16087; 1.
DR Pfam; PF15122; TMEM206; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Chloride; Chloride channel; Ion channel; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..350
FT /note="Proton-activated chloride channel"
FT /id="PRO_0000279476"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H813"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..297
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9H813"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 350 AA; 40659 MW; 2ABDB4F82DCDAC78 CRC64;
MEAIRKELSR SYQELNDETD PIARDPEGAQ EEEQEEAASA VVPDRDSDRS NTRVHFSRTC
LKNVFSVLLI FVYLLLMGVA VFLVYQTITD FRDKLKHPVM SVSYKEVNVY DAPGIALYPG
KARLLSCKHH LYDHIPPLID PGQPGENTCI TQNISYTDPY TNSTVKHALI VQGPRDVRRR
ELVFLQFHLN ETKQDFSAID YLLFSSYDAF LKSTNRVRFM QDCESSFSSW KFSGGFRTWV
KMSLVKTKEE DGSQSVEFRQ ETSVVNFIDR RENPDKGDQL FFVVFEWKDP YIQEIQDIIT
ANPWSMIALL CSVFLVLFKA ADFAKLSVKW MIKVRRRHLK KRTRELNHIS