INX12_CAEEL
ID INX12_CAEEL Reviewed; 408 AA.
AC O01634;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Innexin-12;
DE AltName: Full=Protein opu-12;
GN Name=inx-12 {ECO:0000312|WormBase:ZK770.3};
GN Synonyms=opu-12 {ECO:0000312|WormBase:ZK770.3};
GN ORFNames=ZK770.3 {ECO:0000312|WormBase:ZK770.3};
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-99, 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).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=21408209; DOI=10.1371/journal.pgen.1002010;
RA Nelson M.D., Zhou E., Kiontke K., Fradin H., Maldonado G., Martin D.,
RA Shah K., Fitch D.H.;
RT "A bow-tie genetic architecture for morphogenesis suggested by a genome-
RT wide RNAi screen in Caenorhabditis elegans.";
RL PLoS Genet. 7:E1002010-E1002010(2011).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23671426; DOI=10.1371/journal.pgen.1003510;
RA Kovacevic I., Orozco J.M., Cram E.J.;
RT "Filamin and phospholipase C-epsilon are required for calcium signaling in
RT the Caenorhabditis elegans spermatheca.";
RL PLoS Genet. 9:E1003510-E1003510(2013).
CC -!- FUNCTION: Structural component of the gap junctions (By similarity).
CC Plays a role in oocyte directional transit in the spermatheca during
CC ovulation by facilitating the directional propagation of the calcium
CC signal in the spermatheca (PubMed:23671426). Plays a role in male tail
CC tip morphogenesis (PubMed:21408209). {ECO:0000250|UniProtKB:Q9V427,
CC ECO:0000269|PubMed:21408209, ECO:0000269|PubMed:23671426}.
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 -!- DEVELOPMENTAL STAGE: Expressed in hyp8-11 tail tip cells during the L4
CC larval stage. {ECO:0000269|PubMed:21408209}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes defective oocyte
CC transit through the spermatheca. Calcium oscillations triggered during
CC ovulation are random resulting in uncoordinated spermatheca
CC constrictions. Oocytes enter the spermatheca normally but change
CC direction several times before returning into the gonad or proceeding
CC into the uterus. RNAi-mediated knockdown disrupts tail tip
CC morphogenesis resulting in retention of the pointed larval tail tip in
CC adult males (also known as the Lep phenotype) (PubMed:21408209).
CC {ECO:0000269|PubMed:21408209, ECO:0000269|PubMed:23671426}.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
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DR EMBL; BX284601; CCD66426.1; -; Genomic_DNA.
DR PIR; T34467; T34467.
DR RefSeq; NP_491213.1; NM_058812.5.
DR AlphaFoldDB; O01634; -.
DR SMR; O01634; -.
DR BioGRID; 37418; 1.
DR DIP; DIP-26804N; -.
DR STRING; 6239.ZK770.3.1; -.
DR iPTMnet; O01634; -.
DR EPD; O01634; -.
DR PaxDb; O01634; -.
DR PeptideAtlas; O01634; -.
DR PRIDE; O01634; -.
DR EnsemblMetazoa; ZK770.3.1; ZK770.3.1; WBGene00002134.
DR GeneID; 171944; -.
DR KEGG; cel:CELE_ZK770.3; -.
DR UCSC; ZK770.3.1; c. elegans.
DR CTD; 171944; -.
DR WormBase; ZK770.3; CE15413; WBGene00002134; inx-12.
DR eggNOG; ENOG502QS5B; Eukaryota.
DR HOGENOM; CLU_035763_0_1_1; -.
DR InParanoid; O01634; -.
DR OMA; NTCTATE; -.
DR OrthoDB; 738314at2759; -.
DR PhylomeDB; O01634; -.
DR PRO; PR:O01634; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00002134; Expressed in larva and 4 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 GO; GO:0110039; P:positive regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
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..408
FT /note="Innexin-12"
FT /id="PRO_0000208513"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
SQ SEQUENCE 408 AA; 47091 MW; E3EDFF80FE7C41A5 CRC64;
MNVIQNLLSA VSPQPDGDFV DKLNYCATTI GLVLASAFIT GWSFVGSPID CWFPAYYKGW
WAEYALDYCY VQNTFFVPFS EDKAERSYNW EQLVADKQNT TSLKQTNQIG YYQWVPFILA
LQAMLFYFPV VIWRLFYGMA GQNVTSLCNT CTATEGNEES RKGTITTIAG YISQKRHRNL
IVKQLSGFQN RANGSAVITS YLFMKALFLI NVLFQFVLLK RMLGVDSYFW GAEVTSDLWS
GNEWPETGNF PRVTMCEYEV RNLDNIHKHS VQCVLMINMF NEKIFVALWW WLCFLTVVTI
TNTIYWFWRA SGTSVSKNFI RPYVEDIDPK VKNNRGKLQQ FVSEFLSPDT VFILRLIELN
NGKTPVVELI RDMWRRFNTA VPPPYSAPPL LVKDGAPLLK NFQDESEM
