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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
 
 
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