ID A0A1S3FCT1_DIPOR Unreviewed; 803 AA.
AC A0A1S3FCT1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Volume-regulated anion channel subunit LRRC8C {ECO:0000313|RefSeq:XP_012873777.1};
GN Name=Lrrc8c {ECO:0000313|RefSeq:XP_012873777.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012873777.1};
RN [1] {ECO:0000313|RefSeq:XP_012873777.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012873777.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_012873777.1; XM_013018323.1.
DR AlphaFoldDB; A0A1S3FCT1; -.
DR STRING; 10020.ENSDORP00000019962; -.
DR GeneID; 105987139; -.
DR KEGG; dord:105987139; -.
DR CTD; 84230; -.
DR InParanoid; A0A1S3FCT1; -.
DR OMA; YNSIMYI; -.
DR OrthoDB; 55205at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005225; F:volume-sensitive anion channel activity; IEA:Ensembl.
DR GO; GO:0140361; P:cyclic-GMP-AMP transmembrane import across plasma membrane; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0034214; P:protein hexamerization; IEA:Ensembl.
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; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF12534; Pannexin_like; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW 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 126..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 321..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..338
FT /note="LRRC8 pannexin-like TM region"
FT /evidence="ECO:0000259|Pfam:PF12534"
FT REGION 177..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 92243 MW; 966E1C5578B35F93 CRC64;
MIPVTEFRQF SEQQPAFRVL KPWWDVFTDY LSVAMLMIGV FGCTLQVMQD KIICLPKRMQ
PAQNHSSVSN VSQSVASATP LPPPKPSPAN PATVEMKGLK TDLDLQQYSF INQMCYERAL
HWYAKYFPYL VLIHTLVFML CSNFWFKFPG SSSKIEHFIS ILGKCFDSPW TTRALSEVSG
EDSEEKDNRK NNLNRSNTIQ SGPEGSLVNS QSLKSIPEKF VVDKSTAGAL DKKEGEQAKA
LFEKVKKFRL HVEEGDILYA MYVRQTILKV IKFLIIIAYN SALVSKVQFT VDCNVDIQDM
TGYKNFSCNH TMAHLFSKLS FCYLCFVSIY GLTCLYTLYW LFYRSLREYS FEYVRQETGI
DDIPDVKNDF AFMLHMIDQY DPLYSKRFAV FLSEVSENKL KQLNLNNEWT PDKLRQKLQT
NAHNRLELPL IMLSGLPDTV FEITELQSLK LEIIKNVMIP ATMAQLDNLQ ELSLHQCSVK
IHSAALSFLK DNLKVLSVKF DDMRELPPWM YGLRNLEELY LVGSLSHDIS KNVTLESLRD
LKSLKILSIK SNVAKIPQAV VDVSSHLQKM SIHNDGTKLV MLNNLKKMTN LTELELVHCD
LERIPHAVFS LLSLQELDLK ENNLKSIEEI VSFQHLRKLT VLKLWHNSIA YIPEHIKKLT
SLERLSFSHN KIEVLPSHLF LCNKIRYLDL SYNDIRFIPP EIGVLQSLQY FSITCNKVES
LPDELYFCKK LKTLKIGKNS LSVLSPKIGN LLFLSYLDVK GNHLEILPPE LGDCRALKRA
GLVVEDTLFE TLPSDIREQM KAE
//
