ID   PACC1_PONAB             Reviewed;         350 AA.
AC   Q5RDP8;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 51.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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. Involved in
CC       acidosis-induced cell death by mediating chloride influx and subsequent
CC       cell swelling. {ECO:0000250|UniProtKB:Q9H813}.
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; CR857855; CAH90109.1; -; mRNA.
DR   RefSeq; NP_001125013.1; NM_001131541.1.
DR   AlphaFoldDB; Q5RDP8; -.
DR   SMR; Q5RDP8; -.
DR   STRING; 9601.ENSPPYP00000024234; -.
DR   GeneID; 100171892; -.
DR   KEGG; pon:100171892; -.
DR   CTD; 55248; -.
DR   eggNOG; ENOG502QS5H; Eukaryota.
DR   HOGENOM; CLU_1342892_0_0_1; -.
DR   InParanoid; Q5RDP8; -.
DR   OrthoDB; 829411at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..350
FT                   /note="Proton-activated chloride channel"
FT                   /id="PRO_0000279473"
FT   TOPO_DOM        1..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H813"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..301
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..350
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H813"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H813"
FT   MOD_RES         10
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D771"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D771"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q66H28"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   350 AA;  40014 MW;  26983C3D41794699 CRC64;
     MIRQERSTSY QELSEELDQV VENSELADEQ DKETVKVQGP GVLPGLDSES ASSSIRFSKA
     CLKNVFPVLL IFIYLLLMAV AVFLVYQTIT DFREKLKHPV MSVSYKEVDR YDAPGIALYP
     GQAQLLSCKH HYEVIPPLTS PGQPGDMNCT TQRINYTDPF SNQTVKSALI VQGPREVKKR
     ELVFLQFRLN KSSEDFSAID YLLFSSFQEF LQSPNRVGFM QACESAYSSW KFSGGFRTWV
     KMSLVKTKEE DGREAVEFRQ ETSVVNYIDQ RPAAEKSAQL FFVVFEWKDP FIQKVQDIIT
     ANPWNTIALL CGAFLALFKA AEFAKLSIKW MIKIRKRYLK RRGQATSHIS