PACC1_MOUSE
ID PACC1_MOUSE Reviewed; 350 AA.
AC Q9D771;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Proton-activated chloride channel {ECO:0000303|PubMed:31023925};
DE Short=PAC {ECO:0000303|PubMed:31023925};
DE AltName: Full=Transmembrane protein 206 {ECO:0000305};
GN Name=Pacc1 {ECO:0000250|UniProtKB:Q9H813};
GN Synonyms=Tmem206 {ECO:0000312|MGI:MGI:1914200};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina, Spinal cord, Testis, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-10 AND SER-14, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31023925; DOI=10.1126/science.aav9739;
RA Yang J., Chen J., Del Carmen Vitery M., Osei-Owusu J., Chu J., Yu H.,
RA Sun S., Qiu Z.;
RT "PAC, an evolutionarily conserved membrane protein, is a proton-activated
RT chloride channel.";
RL Science 364:395-399(2019).
CC -!- FUNCTION: Proton-activated chloride channel that mediates import of
CC chloride ion in response to extracellular acidic pH (PubMed:31023925).
CC Involved in acidosis-induced cell death by mediating chloride influx
CC and subsequent cell swelling (PubMed:31023925).
CC {ECO:0000269|PubMed:31023925}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H813};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H813}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and appear mostly normal
CC (PubMed:31023925). Cortical neurons completely lack proton-activated
CC chloride channel activity (PubMed:31023925). Neurons are partially but
CC significantly protected from delayed cell death induced by 1-hour acid
CC treatment (PubMed:31023925). {ECO:0000269|PubMed:31023925}.
CC -!- SIMILARITY: Belongs to the proton-activated chloride channel family.
CC {ECO:0000305}.
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DR EMBL; AK009526; BAB26340.1; -; mRNA.
DR EMBL; AK031270; BAC27330.1; -; mRNA.
DR EMBL; AK044482; BAC31946.1; -; mRNA.
DR EMBL; AK049641; BAC33853.1; -; mRNA.
DR EMBL; BC027151; AAH27151.1; -; mRNA.
DR CCDS; CCDS15619.1; -.
DR RefSeq; NP_080140.1; NM_025864.3.
DR AlphaFoldDB; Q9D771; -.
DR SMR; Q9D771; -.
DR STRING; 10090.ENSMUSP00000027940; -.
DR GlyGen; Q9D771; 2 sites.
DR iPTMnet; Q9D771; -.
DR PhosphoSitePlus; Q9D771; -.
DR EPD; Q9D771; -.
DR jPOST; Q9D771; -.
DR MaxQB; Q9D771; -.
DR PaxDb; Q9D771; -.
DR PRIDE; Q9D771; -.
DR ProteomicsDB; 259221; -.
DR Antibodypedia; 47113; 29 antibodies from 12 providers.
DR DNASU; 66950; -.
DR Ensembl; ENSMUST00000027940; ENSMUSP00000027940; ENSMUSG00000026627.
DR GeneID; 66950; -.
DR KEGG; mmu:66950; -.
DR UCSC; uc007ech.1; mouse.
DR CTD; 55248; -.
DR MGI; MGI:1914200; Pacc1.
DR VEuPathDB; HostDB:ENSMUSG00000026627; -.
DR eggNOG; ENOG502QS5H; Eukaryota.
DR GeneTree; ENSGT00390000017528; -.
DR HOGENOM; CLU_068069_0_0_1; -.
DR InParanoid; Q9D771; -.
DR OMA; ITYMLFA; -.
DR OrthoDB; 829411at2759; -.
DR PhylomeDB; Q9D771; -.
DR TreeFam; TF333307; -.
DR BioGRID-ORCS; 66950; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Pacc1; mouse.
DR PRO; PR:Q9D771; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9D771; protein.
DR Bgee; ENSMUSG00000026627; Expressed in islet of Langerhans and 249 other tissues.
DR Genevisible; Q9D771; MM.
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; IMP:UniProtKB.
DR GO; GO:0006821; P:chloride transport; IMP:UniProtKB.
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_0000279472"
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:0007744|PubMed:19144319"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
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; 40178 MW; 3EE2CFBE929AE003 CRC64;
MIRQELSTSY QELSEELEQV VENSEQADER DKELVQVQGP GVVPGVDNES ASSSIRFSKA
CLKNVFSVLL ILIYLLLMAV AVFLVYQTIT DFREKLKHPV MSVSYKEVDR YDAPGIAFYP
GQAQLLSCKH HYEVIPPLAS PGQPGDRNCT TQRINYTHPF FNHTMQSALI VQGPQEVKKR
ELVFLQFRLN QSNEDFSAID YLLFSSFREF MQSPDKAGFM QACESAYSSW KFSGGFRTWV
KMSLVKTKEE DGREAVEFRQ ETSVVNYIDQ RPAAERSAQL FFVVFEWKDP FIQKVQDIIT
ANPWNTIALL CGAFLALFKA AEFAKLSVKW MIKIRKRYLK RRGQATNHIS
