INX6_CAEEL
ID INX6_CAEEL Reviewed; 389 AA.
AC Q9U3N4; Q17395;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Innexin-6;
DE AltName: Full=Protein opu-6;
GN Name=inx-6; Synonyms=opu-6; ORFNames=C36H8.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-389.
RX PubMed=8707836; DOI=10.1083/jcb.134.2.537;
RA Starich T.A., Lee R.Y., Panzarella C., Avery L., Shaw J.E.;
RT "eat-5 and unc-7 represent a multigene family in Caenorhabditis elegans
RT involved in cell-cell coupling.";
RL J. Cell Biol. 134:537-548(1996).
CC -!- FUNCTION: Structural component of the gap junctions.
CC {ECO:0000250|UniProtKB:O61715}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC junction {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
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DR EMBL; Z69658; CAB60997.1; -; Genomic_DNA.
DR EMBL; U59213; AAB09672.1; -; mRNA.
DR RefSeq; NP_502435.1; NM_070034.4.
DR PDB; 5H1Q; EM; 3.30 A; A/B/C/D/E/F/G/H=1-389.
DR PDB; 5H1R; EM; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-389.
DR PDB; 6KFF; EM; 3.80 A; A/B/C/D/E/F/G/H=1-389.
DR PDB; 6KFG; EM; 3.80 A; A/B/C/D/E/F/G/H=1-389.
DR PDB; 6KFH; EM; 3.60 A; A/B/C/D/E/F/G/H=1-389.
DR PDBsum; 5H1Q; -.
DR PDBsum; 5H1R; -.
DR PDBsum; 6KFF; -.
DR PDBsum; 6KFG; -.
DR PDBsum; 6KFH; -.
DR AlphaFoldDB; Q9U3N4; -.
DR SMR; Q9U3N4; -.
DR BioGRID; 43323; 2.
DR STRING; 6239.C36H8.2; -.
DR TCDB; 1.A.25.1.7; the gap junction-forming innexin (innexin) family.
DR EPD; Q9U3N4; -.
DR PaxDb; Q9U3N4; -.
DR PeptideAtlas; Q9U3N4; -.
DR EnsemblMetazoa; C36H8.2.1; C36H8.2.1; WBGene00002128.
DR GeneID; 178231; -.
DR KEGG; cel:CELE_C36H8.2; -.
DR UCSC; C36H8.2; c. elegans.
DR CTD; 178231; -.
DR WormBase; C36H8.2; CE24831; WBGene00002128; inx-6.
DR eggNOG; ENOG502SI7H; Eukaryota.
DR HOGENOM; CLU_035763_0_1_1; -.
DR InParanoid; Q9U3N4; -.
DR OMA; YQWVVLV; -.
DR OrthoDB; 738314at2759; -.
DR PhylomeDB; Q9U3N4; -.
DR PRO; PR:Q9U3N4; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00002128; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005921; C:gap junction; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005243; F:gap junction channel activity; ISS:UniProtKB.
DR GO; GO:0055077; F:gap junction hemi-channel activity; ISS:UniProtKB.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR000990; Innexin.
DR PANTHER; PTHR11893; PTHR11893; 1.
DR Pfam; PF00876; Innexin; 1.
DR PRINTS; PR01262; INNEXIN.
DR PROSITE; PS51013; PANNEXIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Gap junction; Ion channel;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..389
FT /note="Innexin-6"
FT /id="PRO_0000208508"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:5H1Q"
FT HELIX 31..46
FT /evidence="ECO:0007829|PDB:5H1Q"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:5H1Q"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5H1Q"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:5H1Q"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:5H1Q"
FT TURN 93..98
FT /evidence="ECO:0007829|PDB:5H1Q"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:5H1Q"
FT HELIX 108..133
FT /evidence="ECO:0007829|PDB:5H1Q"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:5H1Q"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:5H1Q"
FT HELIX 161..181
FT /evidence="ECO:0007829|PDB:5H1Q"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:5H1Q"
FT HELIX 188..212
FT /evidence="ECO:0007829|PDB:5H1Q"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:5H1Q"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:5H1Q"
FT TURN 235..239
FT /evidence="ECO:0007829|PDB:5H1Q"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:5H1Q"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:5H1Q"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5H1Q"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:5H1Q"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:5H1Q"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:5H1Q"
FT HELIX 270..304
FT /evidence="ECO:0007829|PDB:5H1Q"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:5H1Q"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:5H1Q"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:5H1Q"
FT HELIX 328..334
FT /evidence="ECO:0007829|PDB:5H1Q"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:5H1Q"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:5H1Q"
FT HELIX 352..364
FT /evidence="ECO:0007829|PDB:5H1Q"
SQ SEQUENCE 389 AA; 45132 MW; 1447745FAC84C3D8 CRC64;
MASQVGAINS VNALISRVFV QPKGDLADRL NSRVTVVILA VSSALLLSSH FIGDPITCWT
PAQFNAQWVN FVNQYCFVHG TYFVPLDQQL AFEEEERTKV SIQYYQWVPY VFALQAFLFY
IPRFIWKAMI AYSGYDLAAA VKYVDRFWSE NRDKDDKFKT RLAAFEGRPS VYIWDGIRLA
RKKRSRNMAL FYTLSTVWQA VNAWIQFYIL TQLLDSSIYT LWGPSILGDL LQGNDWQTTG
HFPRIVHCDF NRRRPASVQL DTVLCVLTLN IYYEKLFIFL WFWLVFVAVV STVNCFKWIY
YLCNKTKAQK TIKNYLSTAP IKSTISDDQF FSALGEDGLF IMDQMALNLG DIPASYLTIS
MRNICQDFIE SEDYIDEERT PFVKSIKHT
