ID   INX7_CAEEL              Reviewed;         556 AA.
AC   Q21123;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Innexin-7;
DE   AltName: Full=Protein opu-7;
GN   Name=inx-7; Synonyms=opu-7; ORFNames=K02B2.4;
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   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-267, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
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; FO080181; CCD61803.1; -; Genomic_DNA.
DR   PIR; D88700; D88700.
DR   RefSeq; NP_500894.1; NM_068493.5.
DR   AlphaFoldDB; Q21123; -.
DR   BioGRID; 42486; 1.
DR   STRING; 6239.K02B2.4; -.
DR   iPTMnet; Q21123; -.
DR   EPD; Q21123; -.
DR   PaxDb; Q21123; -.
DR   EnsemblMetazoa; K02B2.4a.1; K02B2.4a.1; WBGene00002129.
DR   GeneID; 177364; -.
DR   KEGG; cel:CELE_K02B2.4; -.
DR   UCSC; K02B2.4; c. elegans.
DR   CTD; 177364; -.
DR   WormBase; K02B2.4a; CE04690; WBGene00002129; inx-7.
DR   eggNOG; ENOG502RRNR; Eukaryota.
DR   HOGENOM; CLU_035763_0_2_1; -.
DR   InParanoid; Q21123; -.
DR   OMA; PHKICRF; -.
DR   OrthoDB; 738314at2759; -.
DR   PhylomeDB; Q21123; -.
DR   PRO; PR:Q21123; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00002129; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; Q21123; baseline and differential.
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   Cell junction; Cell membrane; Gap junction; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..556
FT                   /note="Innexin-7"
FT                   /id="PRO_0000208509"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   REGION          431..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..450
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..556
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
SQ   SEQUENCE   556 AA;  63797 MW;  A78C865A45C0C1B6 CRC64;
     MFVFRVLNTV PYTNRTGAKD LVASIHSFLT SNLLVGLAVL ISWKQFGGTP IECMVPLDFT
     SAWVQYSNNY CWAQPTYFIP FTEELVEQVV DPADVVADGI TIGNGGNRPR FVKKGGEKIS
     YYQWMSFFLL FEAACFRLPC FIWKYFASQS GMQVGEILRV ASDENNAVPL VKKANIDALC
     IHLRGVLRFQ KRLKLKKIVP HKILRFLNIK YSAYYVTFIY FVAKVAFLLN VILQSKLLNK
     YMLPHDRQQN FGFDMWKTIF YGSTNGNETW RENGVFPRVT LCDFETRDMG NVQMHTVQCV
     LLLNLFTEKI FVFLWAWYIL LTAFTVGNLF SWLFAVFNET YNEHFILNHL EMCETPFDKD
     DLKNREHVTR FITLYLGTDG LFLLQLIAQH ADVVFTTELI AALFKTYIEI EAQRATLKQM
     NAVLPLLRPN DESQVESGKN TAPSTSHNVR RRGTEQLEKN VKSRQGSLST QLRPFNSFEE
     PDQPTKKFDD SSSEDENSKK GSKKPSPTKK KASSKNSPQS SSNSRRPSLA HTASPAFTHH
     HEPDSKIPKT AEKKHW