CLCC1_BOVIN
ID CLCC1_BOVIN Reviewed; 542 AA.
AC Q1LZF8;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Chloride channel CLIC-like protein 1;
DE Flags: Precursor;
GN Name=CLCC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Interacts with mitochondrial protein PIGBOS1 (via C-terminus);
CC the interaction occurs at the mitochondria-associated endoplasmic
CC reticulum (ER) membrane, a zone of contact between the ER and
CC mitochondrial membranes, but does not appear to play a role in ER-
CC mitochondria tethering and is not affected by ER stress (By
CC similarity). Interacts with CALR (By similarity).
CC {ECO:0000250|UniProtKB:Q96S66}.
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; BC116020; AAI16021.1; -; mRNA.
DR RefSeq; NP_001069252.1; NM_001075784.1.
DR RefSeq; XP_005204173.1; XM_005204116.3.
DR RefSeq; XP_010801469.1; XM_010803167.2.
DR RefSeq; XP_015319222.1; XM_015463736.1.
DR AlphaFoldDB; Q1LZF8; -.
DR STRING; 9913.ENSBTAP00000022767; -.
DR PaxDb; Q1LZF8; -.
DR PRIDE; Q1LZF8; -.
DR Ensembl; ENSBTAT00000022767; ENSBTAP00000022767; ENSBTAG00000017129.
DR GeneID; 519085; -.
DR KEGG; bta:519085; -.
DR CTD; 23155; -.
DR VEuPathDB; HostDB:ENSBTAG00000017129; -.
DR VGNC; VGNC:27394; CLCC1.
DR eggNOG; ENOG502QSP7; Eukaryota.
DR GeneTree; ENSGT00390000016611; -.
DR HOGENOM; CLU_034552_1_1_1; -.
DR InParanoid; Q1LZF8; -.
DR OMA; ELWTYVH; -.
DR OrthoDB; 1001950at2759; -.
DR TreeFam; TF328890; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000017129; Expressed in oocyte and 108 other tissues.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IBA:GO_Central.
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; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..542
FT /note="Chloride channel CLIC-like protein 1"
FT /id="PRO_0000297681"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 369..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S66"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S66"
FT MOD_RES 482
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96S66"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S66"
SQ SEQUENCE 542 AA; 61812 MW; E5C0A0BC45BDAB94 CRC64;
MLYSLLLCEC LWLITAYAHD DEWIDPTDML NYDAASGRMR KSQVKYGISE KEEVNPDLSC
ANELSECYNR LDSLTYKIDE CEKQKRKDYE SQSNPVFRRY LNKILIETKK LGLPDENKHD
MHYDAEIILK RQTLLEIQKF LSGEDWKPGA LDDALSDILI NFKFHDFETW KWRFEEFFGV
DPYNVFMVLL CLLCIVALVA TELWTYVRWY TQLKRVFFIS FLISLGWNWM YLYKLAFAQH
QAEVAKMEPL NNVCAEKMNW SGSLWEWLRS SWTYKDDPCQ KYYELLLVNP IWLVPPTKAL
AVTFTNFVTE PLKHVGKGAG EFIKALMKEI PVLLHIPVLI IMALAVLSFC YGAGKSVNML
RHVGGPEREA PQALQAGERR RQQKIDYRPH GGAGDADFYY RGQISPIEQG PNDNTYEGRR
DVLRERDVGL RFQTGNKSPE VLRPFDLQEA EAREHPKVVP GLKSPNLESK PREMGEIPGE
STPTESSTES SQPAKPVSGQ KVSEGVEGCP AVEKAQLRTD AAGGPEEGST CSPASTAVEV
CG
