ID   CLCC1_XENLA             Reviewed;         508 AA.
AC   Q91892;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Chloride channel CLIC-like protein 1;
DE   AltName: Full=Mid-1-related chloride channel protein 1;
DE            Short=MCLC;
DE   Flags: Precursor;
GN   Name=clcc1;
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 [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=8632145; DOI=10.1046/j.1471-4159.1996.66062248.x;
RA   Holthuis J.C., Martens G.J.M.;
RT   "The neuroendocrine proteins secretogranin II and III are regionally
RT   conserved and coordinately expressed with proopiomelanocortin in Xenopus
RT   intermediate pituitary.";
RL   J. Neurochem. 66:2248-2256(1996).
CC   -!- FUNCTION: Seems to act as a chloride ion channel (By similarity). Plays
CC       a role in retina development (By similarity).
CC       {ECO:0000250|UniProtKB:Q99LI2, ECO:0000250|UniProtKB:Q9WU61}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein
CC       {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9WU61};
CC       Multi-pass membrane protein {ECO:0000255}. Nucleus membrane
CC       {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Within the endoplasmic reticulum (ER), localizes to
CC       the mitochondria-associated ER membrane, a zone of contact between the
CC       ER and mitochondrial membranes. {ECO:0000250|UniProtKB:Q96S66}.
CC   -!- SIMILARITY: Belongs to the chloride channel MCLC family. {ECO:0000305}.
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DR   EMBL; X92871; CAA63477.1; -; mRNA.
DR   RefSeq; NP_001081605.1; NM_001088136.1.
DR   AlphaFoldDB; Q91892; -.
DR   TCDB; 1.A.36.1.5; the intracellular chloride channel (icc) family.
DR   GeneID; 397947; -.
DR   KEGG; xla:397947; -.
DR   CTD; 397947; -.
DR   Xenbase; XB-GENE-1010586; clcc1.S.
DR   OrthoDB; 1001950at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 397947; Expressed in pancreas and 19 other tissues.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR009231; Chloride_chnl_CLIC-like.
DR   PANTHER; PTHR34093; PTHR34093; 1.
DR   Pfam; PF05934; MCLC; 1.
PE   2: Evidence at transcript level;
KW   Chloride; Chloride channel; Endoplasmic reticulum; Golgi apparatus;
KW   Ion channel; Ion transport; Membrane; Nucleus; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..508
FT                   /note="Chloride channel CLIC-like protein 1"
FT                   /id="PRO_0000297685"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          388..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  57913 MW;  581C2A870B771BA7 CRC64;
     MRLFLLVALY LSPVYGDYTD EWIDPSDMLN YDAASGKMKN KPQVESTQSY YSVENTVSQD
     ATQQPAQKAN ELHQNPDMTC SAEYQEYKTK LENLKGQLEE TKRMEKSKSK SQAIFKRYLN
     KILIEAGRIG LPDESYPKAH YDAEVVFTME MLQEIQSFLN NGDWNVGALD DALSSTLVQF
     KHHNEEEWKW KFEDSFGVDV YTLFMLILCV LCLVKLIATE IWTHIGWFTQ LKRLLILSTV
     ISFGWNWMYL YKVAFAERQA ELAKLQDFDK CSQKISWSES LFDWMKGAAT FQNDPCEDYF
     KALIVSPTLM VPPTKALALT FTNFITEPLK HIGKGIGEFL NALLSEIPLF FQVPVLIFIA
     VLLLAFFYGA GTAVMNPVNL YRRLTGPERE KPLPVEPTRS NRKRFIEDVR VPPALGQLPR
     DNDVVNIPKQ QPLDDIDGSN NPPVTAPADP SDTGQVKSNN TGEPLVQEDH SIKKSIKESR
     NDERPNTESP EAKPQRPEEP VVETLRST