INX1_DROME
ID INX1_DROME Reviewed; 362 AA.
AC P27716; Q0KHV4; Q9W3T8;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Innexin inx1;
DE Short=Innexin-1;
DE AltName: Full=Protein optic ganglion reduced;
DE Short=Protein ogre;
GN Name=ogre; Synonyms=inx1, l(1)ogre; ORFNames=CG3039;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo;
RX PubMed=1963867; DOI=10.1093/genetics/126.4.1033;
RA Watanabe T., Kankel D.R.;
RT "Molecular cloning and analysis of l(1)ogre, a locus of Drosophila
RT melanogaster with prominent effects on the postembryonic development of the
RT central nervous system.";
RL Genetics 126:1033-1044(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11960713; DOI=10.1016/s0925-4773(02)00025-4;
RA Stebbings L.A., Todman M.G., Phillips R., Greer C.E., Tam J., Phelan P.,
RA Jacobs K., Bacon J.P., Davies J.A.;
RT "Gap junctions in Drosophila: developmental expression of the entire
RT innexin gene family.";
RL Mech. Dev. 113:197-205(2002).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15047872; DOI=10.1091/mbc.e04-01-0056;
RA Bauer R., Lehmann C., Martini J., Eckardt F., Hoch M.;
RT "Gap junction channel protein innexin 2 is essential for epithelial
RT morphogenesis in the Drosophila embryo.";
RL Mol. Biol. Cell 15:2992-3004(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19038051; DOI=10.1186/1471-213x-8-111;
RA Bohrmann J., Zimmermann J.;
RT "Gap junctions in the ovary of Drosophila melanogaster: localization of
RT innexins 1, 2, 3 and 4 and evidence for intercellular communication via
RT innexin-2 containing channels.";
RL BMC Dev. Biol. 8:111-111(2008).
CC -!- FUNCTION: Structural component of the gap junctions. Essential for
CC generation and/or maintenance of postembryonic neuroblasts and normal
CC development of optic lobe. {ECO:0000269|PubMed:1963867}.
CC -!- SUBUNIT: Heterooligomer of Inx2 and ogre.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC junction. Basolateral cell membrane. Note=Accumulates in the
CC basolateral membrane of follicle cells in oocytes and epithelial cells
CC in embryonic salivary gland and hindgut.
CC -!- TISSUE SPECIFICITY: In ovary, expressed in follicle cells. Expressed
CC around the periphery of the embryo during cellular blastoderm
CC formation. Repeating epidermal pattern emerges from stage 11, high
CC levels of expression detected along the borders of each segment from
CC stage 13. At stage 13, expressed in the dorsal branch of the tracheal
CC system. During stage 15, detected in a few cells at each of the branch
CC points of the dorsal trunk and at low levels in cardioblasts. In
CC embryos, also expressed in the salivary gland and the hindgut (at
CC protein level). At stage 17, expressed in the dorsal side of the CNS.
CC Expressed in the imaginal wing disk. Expressed in larval CNS and in
CC tissues outside of the CNS. In pupae, expressed in the CNS and in
CC primary, secondary and tertiary pigment cells of the retina.
CC {ECO:0000269|PubMed:11960713, ECO:0000269|PubMed:15047872,
CC ECO:0000269|PubMed:19038051, ECO:0000269|PubMed:1963867}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis. Embryonic
CC expression commences during cellular blastoderm formation, increases
CC rapidly after cellularization and is maintained during the early stages
CC of gastrulation. Expressed in larvae and pupae.
CC {ECO:0000269|PubMed:11960713}.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X61180; CAA43486.1; -; mRNA.
DR EMBL; AE014298; AAF46225.1; -; Genomic_DNA.
DR EMBL; BT004911; AAO49164.1; -; mRNA.
DR PIR; S17285; S17285.
DR RefSeq; NP_001245557.1; NM_001258628.3.
DR RefSeq; NP_001245558.1; NM_001258629.2.
DR RefSeq; NP_001259299.1; NM_001272370.1.
DR RefSeq; NP_001259300.1; NM_001272371.1.
DR RefSeq; NP_524824.1; NM_080085.5.
DR RefSeq; NP_727147.1; NM_167101.3.
DR AlphaFoldDB; P27716; -.
DR BioGRID; 69639; 3.
DR DIP; DIP-22933N; -.
DR IntAct; P27716; 2.
DR STRING; 7227.FBpp0301607; -.
DR TCDB; 1.A.25.1.3; the gap junction-forming innexin (innexin) family.
DR PaxDb; P27716; -.
DR DNASU; 45382; -.
DR EnsemblMetazoa; FBtr0071036; FBpp0070995; FBgn0004646.
DR EnsemblMetazoa; FBtr0071037; FBpp0070996; FBgn0004646.
DR EnsemblMetazoa; FBtr0309873; FBpp0301607; FBgn0004646.
DR EnsemblMetazoa; FBtr0309874; FBpp0301608; FBgn0004646.
DR EnsemblMetazoa; FBtr0309875; FBpp0301609; FBgn0004646.
DR EnsemblMetazoa; FBtr0334881; FBpp0306903; FBgn0004646.
DR GeneID; 45382; -.
DR KEGG; dme:Dmel_CG3039; -.
DR CTD; 45382; -.
DR FlyBase; FBgn0004646; ogre.
DR VEuPathDB; VectorBase:FBgn0004646; -.
DR eggNOG; ENOG502QWKB; Eukaryota.
DR HOGENOM; CLU_035763_1_1_1; -.
DR InParanoid; P27716; -.
DR OMA; GHHEHLY; -.
DR OrthoDB; 738314at2759; -.
DR PhylomeDB; P27716; -.
DR SignaLink; P27716; -.
DR BioGRID-ORCS; 45382; 0 hits in 1 CRISPR screen.
DR ChiTaRS; ogre; fly.
DR GenomeRNAi; 45382; -.
DR PRO; PR:P27716; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004646; Expressed in wing disc and 56 other tissues.
DR ExpressionAtlas; P27716; baseline and differential.
DR Genevisible; P27716; DM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005921; C:gap junction; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005243; F:gap junction channel activity; IBA:GO_Central.
DR GO; GO:0010496; P:intercellular transport; ISS:FlyBase.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR GO; GO:0007603; P:phototransduction, visible light; IGI:FlyBase.
DR GO; GO:0007632; P:visual behavior; ISS:FlyBase.
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; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..362
FT /note="Innexin inx1"
FT /id="PRO_0000208494"
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..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 132..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 199..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..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 362 AA; 42582 MW; 267F5E360B67E894 CRC64;
MYKLLGSLKS YLKWQDIQTD NAVFRLHNSF TTVLLLTCSL IITATQYVGQ PISCIVNGVP
PHVVNTFCWI HSTFTMPDAF RRQVGREVAH PGVANDFGDE DAKKYYTYYQ WVCFVLFFQA
MACYTPKFLW NKFEGGLMRM IVMGLNITIC TREEKEAKRD ALLDYLIKHV KRHKLYAIRY
WACEFLCCIN IIVQMYLMNR FFDGEFLSYG TNIMKLSDVP QEQRVDPMVY VFPRVTKCTF
HKYGPSGSLQ KHDSLCILPL NIVNEKTYVF IWFWFWILLV LLIGLIVFRG CIIFMPKFRP
RLLNASNRMI PMEICRSLSR KLDIGDWWLI YMLGRNLDPV IYKDVMSEFA KQVEPSKHDR
AK
