INX1_SCHAM
ID INX1_SCHAM Reviewed; 361 AA.
AC Q9XYN0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Innexin inx1;
DE Short=Innexin-1;
DE AltName: Full=G-Inx1;
GN Name=inx1;
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: Expressed in embryonic neural precursors including
CC the dorsal median neuroblast, glial cells, neuropilar glial ring,
CC developing myoblasts cells and in a circumferential band of epithelial
CC cells at the trochanter/coxa boundary stripe in the developing limb.
CC {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; AF115853; AAD29305.1; -; mRNA.
DR AlphaFoldDB; Q9XYN0; -.
DR SMR; Q9XYN0; -.
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..361
FT /note="Innexin inx1"
FT /id="PRO_0000208495"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 50..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..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 203..267
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 289..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 361 AA; 41879 MW; 75EC5C61951059E7 CRC64;
MYKLLGGLKE YLKWQDIVTD NAIFRLHNLF TTVLLLTCSL IITATQYVGN PIHCIVNGLP
VRPINTYCWI TSTFTMPDAF LRQVGSEVAH PGVANDFGDE DAKKYYTYYQ WVCFVLFFQA
MLCYTPKWIW DSIEGGLLRT LIMGLNRGLC QDDEKCMKKK ALIEYLLRHI KRHNMYALKY
WFCETLCLVN IIGQLYLMNH FFDGEFFSYG LRVVAFSEQS QEERVDPMVY VFPRVTKCTF
HKYGASGSIQ KHDSLCVLPL NIVNEKTYIF LWFWYIILAA LLSVLVVYRA VILAVPSVRP
ILLHARNRMV PKEVTNAICR KTDVGDWWIL YMLGRNMDPM IYGEVIADLA KKIETPSSNN
P