INX2_SCHAM
ID INX2_SCHAM Reviewed; 359 AA.
AC Q9XYN1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Innexin inx2;
DE Short=Innexin-2;
DE AltName: Full=G-Inx2;
GN Name=inx2;
OS Schistocerca americana (American grasshopper).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
OX NCBI_TaxID=7009;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
RC TISSUE=Body wall, Embryo, and Ventral nerve cord;
RX PubMed=10079517;
RX DOI=10.1002/(sici)1520-6408(1999)24:1/2<137::aid-dvg13>3.0.co;2-7;
RA Ganfornina M.D., Sanchez D., Herrera M., Bastiani M.J.;
RT "Developmental expression and molecular characterization of two gap
RT junction channel proteins expressed during embryogenesis in the grasshopper
RT Schistocerca americana.";
RL Dev. Genet. 24:137-150(1999).
CC -!- FUNCTION: Structural components of the gap junctions.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC junction.
CC -!- TISSUE SPECIFICITY: Widespread expression in embryo, in anterior and
CC posterior row of neural precursors, midline precursors and in
CC epithelial sheet of stomodeum. {ECO:0000269|PubMed:10079517}.
CC -!- DEVELOPMENTAL STAGE: Embryonic development.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
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DR EMBL; AF115854; AAD29306.1; -; mRNA.
DR AlphaFoldDB; Q9XYN1; -.
DR SMR; Q9XYN1; -.
DR GO; GO:0005921; C:gap junction; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005243; F:gap junction channel activity; TAS: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; Ion channel; Ion transport;
KW Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..359
FT /note="Innexin inx2"
FT /id="PRO_0000208497"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 44..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 131..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 202..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 288..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 359 AA; 41446 MW; 9C313EEFDF14F1EE CRC64;
MFDVFGSVKG LLKLDSVCID NNLFRLHYKA TVIILIAFSL LVTSRQYIGD PIDCIVDEIP
LAVMDTYCWI YSTFTIPNRL NGKIGLEVAH PGVGAHVAGK DEVKYHKYYQ WVCFVLFFQA
ILFYIPRYLW KTWEGGRIKM LVLDLNSPVV NEQSKADRKK LLVDYFATNL HTQNFYAYRF
FICEALNFVN VVGQIYFMDL FLDGEFTTYG SDVVRFTEME PEERSDPMSR VFPKVTKCTF
HKYGPSGSVQ TFDGLCVLPL NIVNEKIYVF LWFWFVILSV LTGIGLVYRL ATAMGPQMRM
YLLRARSRLA PQDQIETISN KCQIGDWFVL YQLGKNIDPL IYKELVADLA KKLEGKEIV