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Database: UniProt
Entry: A0A3B3SQ68_9TELE
LinkDB: A0A3B3SQ68_9TELE
Original site: A0A3B3SQ68_9TELE 
ID   A0A3B3SQ68_9TELE        Unreviewed;       797 AA.
AC   A0A3B3SQ68;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Volume-regulated anion channel subunit LRRC8C-like {ECO:0000313|Ensembl:ENSPKIP00000032894.1};
GN   Name=LRRC8C {ECO:0000313|Ensembl:ENSPKIP00000032894.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000032894.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000032894.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC         ChEBI:CHEBI:17996; Evidence={ECO:0000256|ARBA:ARBA00024167};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324,
CC         ChEBI:CHEBI:16382; Evidence={ECO:0000256|ARBA:ARBA00024145};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=taurine(out) = taurine(in); Xref=Rhea:RHEA:66328,
CC         ChEBI:CHEBI:507393; Evidence={ECO:0000256|ARBA:ARBA00024158};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the LRRC8 family.
CC       {ECO:0000256|ARBA:ARBA00010471}.
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DR   Ensembl; ENSPKIT00000013773.1; ENSPKIP00000032894.1; ENSPKIG00000012817.1.
DR   Ensembl; ENSPKIT00000013794.1; ENSPKIP00000032913.1; ENSPKIG00000012817.1.
DR   GeneTree; ENSGT00940000159250; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR021040; LRRC8_Pannexin-like.
DR   PANTHER; PTHR48051; -; 1.
DR   PANTHER; PTHR48051:SF22; VOLUME-REGULATED ANION CHANNEL SUBUNIT LRRC8C-LIKE; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF12534; Pannexin_like; 1.
DR   SMART; SM00365; LRR_SD22; 4.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 3.
PE   3: Inferred from homology;
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        30..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        251..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        315..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..331
FT                   /note="LRRC8 pannexin-like TM region"
FT                   /evidence="ECO:0000259|Pfam:PF12534"
SQ   SEQUENCE   797 AA;  92639 MW;  581B907150786FE4 CRC64;
     MIPVTEFRQF SEQQPAFRVL KPWWDVFTDY LSVAMLMIGV FGCTLQVMQD KVICLPKRMS
     LPNETVPSQN TSEIMLDPTL APHANFSPEP VVHEMKGLKT NLDLQQYNYI NQMCYDRALH
     WYAKYFPYLV LIHTIIFMVC SNFWFKFPGS SSKIEHFISI LGKCFDSPWT TRALSEVSGD
     NPEKKESKKP NLNISTLESN LEESHSLRSI AEKFVVDKPA ARALDKKEGE QAKALFERVK
     KFRLHVEEGE LLYIMYVRQT VLKVLKFILI IIYNSNLVPH VRMNVMCNVD IQDMTGYKHF
     FCNHTMADLF SKLSYCYLCF VSVYGLTCLY TSIWLFYRSL KEYSFEYVRQ ETGIDDIPDV
     KNDFAFMLHM IDQYDPLYSK RFAVFLSEVS ENKLKQLNLN HELTAEKLRQ RLQINSSNRL
     ELKFFMLSGL PDTIFEVTEL QSLKLEIMNN VTIPAAIAQL EDLQELSLYQ CSVKTHTAAT
     SFLRENLKIL RVKFDDSREL PHWIYSLRNL EELYLIGSLS PDISKNIALE TLRELKSLKI
     LSLKSNLTKI PQSIVDVSSH LQQFCVHNDG TKLVMLNNLK KMVNLTILEL VHSDLERIPS
     GIFTLTCLQD LDLKDNNLKS IEEIVHFQQL RKLTSLKLWY NAITYIPENI KKLGSLEHLH
     FNHNKIEILP SHLFLCNKLR YLDLSFNDIR FIPPEIGVLQ SLQYFSVTCN KIENLPDELF
     FCKKLKTLKL GKNTLSLLSP KISYLVLLTH LELKGNHLEV LPAELRSCRN LTRSGFVVED
     NLFETLPSDV REQMKLE
//
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