ID   PACC1_RAT               Reviewed;         350 AA.
AC   Q66H28;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
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:0000312|RGD:1359339};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-24, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; BC082061; AAH82061.1; -; mRNA.
DR   RefSeq; NP_001007680.1; NM_001007679.1.
DR   AlphaFoldDB; Q66H28; -.
DR   SMR; Q66H28; -.
DR   STRING; 10116.ENSRNOP00000005387; -.
DR   GlyGen; Q66H28; 2 sites.
DR   iPTMnet; Q66H28; -.
DR   PhosphoSitePlus; Q66H28; -.
DR   SwissPalm; Q66H28; -.
DR   jPOST; Q66H28; -.
DR   PaxDb; Q66H28; -.
DR   PRIDE; Q66H28; -.
DR   Ensembl; ENSRNOT00000005387; ENSRNOP00000005387; ENSRNOG00000003915.
DR   GeneID; 305070; -.
DR   KEGG; rno:305070; -.
DR   CTD; 55248; -.
DR   RGD; 1359339; Tmem206.
DR   eggNOG; ENOG502QS5H; Eukaryota.
DR   GeneTree; ENSGT00390000017528; -.
DR   HOGENOM; CLU_068069_0_0_1; -.
DR   InParanoid; Q66H28; -.
DR   OMA; ITYMLFA; -.
DR   OrthoDB; 829411at2759; -.
DR   PhylomeDB; Q66H28; -.
DR   TreeFam; TF333307; -.
DR   PRO; PR:Q66H28; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000003915; Expressed in ovary and 18 other tissues.
DR   Genevisible; Q66H28; RN.
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:0098656; P:anion transmembrane transport; ISO:RGD.
DR   GO; GO:1902476; P:chloride transmembrane transport; ISO:RGD.
DR   GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR   GO; GO:0015698; P:inorganic anion transport; ISO:RGD.
DR   InterPro; IPR029366; TMEM206.
DR   PANTHER; PTHR16087; PTHR16087; 1.
DR   Pfam; PF15122; TMEM206; 1.
PE   1: Evidence at protein 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_0000279474"
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:0007744|PubMed:22673903"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
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;  40073 MW;  4AA7E178DB827B75 CRC64;
     MIRQDLSTSY QELSEELEQV VENSEQADER DKELVQVQGP GVVPGVDNES ASSSIRFSKA
     CLKNVFSVLL ILIYLLLMAV AVFLVYQTIT DFREKLKHPV MSVSYKEVDR YDAPGIALYP
     GQAQLLSCKH HYEVIPPLAS PGQPGDRNCT TQRINYTHPF SNHTMQSALI VQGPQEVKKR
     ELVFLQFRLN QSDEDFSAID YLLFSSFREF MQSPDKAGFM QACESAYSSW KFSGGFRTWV
     KMSLVKTKEE DGREAVEFRQ ETSVVNYIDQ RPAAEKSTQL FFVVFEWKDP FIQKVQDIIT
     ANPWNTIALL CGAFLALFKA AEFAKLSVKW MIKIRKRYLK RRGQATNHIS