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Database: UniProt
Entry: G3X0X5_SARHA
LinkDB: G3X0X5_SARHA
Original site: G3X0X5_SARHA 
ID   G3X0X5_SARHA            Unreviewed;       858 AA.
AC   G3X0X5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Leucine rich repeat containing 8 VRAC subunit D {ECO:0000313|Ensembl:ENSSHAP00000021330.1};
GN   Name=LRRC8D {ECO:0000313|Ensembl:ENSSHAP00000021330.1};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000021330.1, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000021330.1, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000021330.1}
RP   IDENTIFICATION.
RG   Ensembl;
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_003767267.1; XM_003767219.2.
DR   STRING; 9305.ENSSHAP00000021330; -.
DR   Ensembl; ENSSHAT00000021503.2; ENSSHAP00000021330.1; ENSSHAG00000018078.2.
DR   Ensembl; ENSSHAT00000030136.1; ENSSHAP00000042383.1; ENSSHAG00000018078.2.
DR   Ensembl; ENSSHAT00000040133.1; ENSSHAP00000033246.1; ENSSHAG00000018078.2.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000154043; -.
DR   HOGENOM; CLU_019019_0_0_1; -.
DR   OMA; DFDHVCE; -.
DR   OrthoDB; 55205at2759; -.
DR   TreeFam; TF331443; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; 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:0015810; P:aspartate transmembrane transport; IEA:Ensembl.
DR   GO; GO:0071470; P:cellular response to osmotic stress; IEA:Ensembl.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0034214; P:protein hexamerization; IEA:Ensembl.
DR   GO; GO:0015734; P:taurine transport; IEA:Ensembl.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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:SF3; LEUCINE RICH REPEAT CONTAINING 8 VRAC SUBUNIT A; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF12534; Pannexin_like; 1.
DR   SMART; SM00365; LRR_SD22; 5.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 4.
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007648};
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        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..384
FT                   /note="LRRC8 pannexin-like TM region"
FT                   /evidence="ECO:0000259|Pfam:PF12534"
FT   REGION          106..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   858 AA;  97924 MW;  1C30F169AD26FA00 CRC64;
     MFTLAEVASL NDIQPTYRIL KPWWDVFMDY LAVVMLMVAI FAGTMQLTKD QVVCLPVLPS
     SVNSKAHLAS GSADMTTDAP KFEVATDQDR WTAKPTSFDE AVAVTSGSPL SKTSSPHTDS
     PVPNQEVRKE IRDPTGRKTN LDFQQYVFIN QMCYHLALPW YSKYFPYLAL IHTIILMVSS
     NFWFKYPKTC SKVEHFVSIL GKCFESPWTT KALSETACED SEENKQRLTG AQSLPKHVST
     SSDEGSPSAS TPMINKTGFK FSAEKPVIEV PSMTILDKKD GEQAKALFEK VRKFRAHVED
     SDLIYKLYVV QTVIKTAKFI FILCYTANFV NAISFEHTCK PKVEHLTGYE EFECTHNMAY
     MLKKLLISYI SIICVYGFIC LYTLFWLFRI PLKEYSFEKV REESSFSDIP DVKNDFAFLL
     HMVDQYDQLY SKRFGVFLSE VSENKLREIS LNHEWTFEKL RQHVSRNAQD KQELHLFMLS
     GVPDAVFDLT DLDVLKLELI PEAKIPAKIS QMTNLQELHL CHCPAKVEQT AFSFLRDHLR
     CLHVKFTDVA EIPAWVYLLK NLRELYLVGN LNSENNKMIG LESLRELRHL KILHVKSNLT
     KVPSNITDVA PHLTKLVIHN DGTKLVVLNS LKKMMNVAEL ELQNCELERI PHAIFSLSNL
     QELDLKSNNI RTIEEIISFQ HLKRLTCLKL WHNKIVNIPP SITHVKNLES LYFSNNKLES
     LPGAVFSLQK LRCLDVSYNN ISVIPVEIGS LQNLQHLHLT GNKVDVLPKQ LFKCIKLRTL
     SLGQNCITSI PEKISQFSQL TQLELKGNCL DRLPAQLGQC RLLKKSGLVV EDHLFDTLPT
     EVKEALNQDT NTPFANGI
//
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