INX3_DROME
ID INX3_DROME Reviewed; 395 AA.
AC Q9VAS7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Innexin inx3;
DE Short=Innexin-3;
GN Name=Inx3; ORFNames=CG1448;
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], SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=10888681; DOI=10.1091/mbc.11.7.2459;
RA Stebbings L.A., Todman M.G., Phelan P., Bacon J.P., Davies J.A.;
RT "Two Drosophila innexins are expressed in overlapping domains and cooperate
RT to form gap-junction channels.";
RL Mol. Biol. Cell 11:2459-2470(2000).
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=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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 FUNCTION, INTERACTION WITH INX2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=16436513; DOI=10.1091/mbc.e05-11-1059;
RA Lehmann C., Lechner H., Loer B., Knieps M., Herrmann S., Famulok M.,
RA Bauer R., Hoch M.;
RT "Heteromerization of innexin gap junction proteins regulates epithelial
RT tissue organization in Drosophila.";
RL Mol. Biol. Cell 17:1676-1685(2006).
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366; SER-377 AND TYR-381, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Structural components of the gap junctions. Essential for
CC proper epithelial development of the epidermis.
CC {ECO:0000269|PubMed:16436513}.
CC -!- SUBUNIT: Heterooligomer of Inx2 (via cytoplasmic C-terminal region) and
CC Inx3 (via cytoplasmic C-terminal region).
CC {ECO:0000269|PubMed:10888681}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC junction. Cytoplasm. Lateral cell membrane. Apicolateral cell membrane.
CC Note=In ovary, localizes to the lateral membrane of follicle cells
CC covering the oocyte and to the apicolateral membrane of follicle cells
CC covering the nurse cells. In nurse cells, localizes to the membrane and
CC around the nuclei.
CC -!- TISSUE SPECIFICITY: In ovary, expressed in nurse cells and follicle
CC cells. Expressed in embryonic epithelial cells. Ubiquitously expressed
CC in stage 5 embryos. Expressed in foregut and hindgut from stage 11-17
CC and in proventriculus, epidermis and CNS in stage 16 embryos (at
CC protein level). Expressed in anterior and ventral regions in stage 8
CC embryos. Repeating epidermal pattern emerges at stage 11, refines to
CC one or two cells at each side of the segment borders by stage 13.
CC Expressed in the imaginal wing disk. In pupae, expressed in the CNS and
CC in secondary and tertiary pigment cells of the retina.
CC {ECO:0000269|PubMed:10888681, ECO:0000269|PubMed:11960713,
CC ECO:0000269|PubMed:16436513, ECO:0000269|PubMed:19038051}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis (at protein level).
CC Expressed in larvae and pupae. {ECO:0000269|PubMed:11960713,
CC ECO:0000269|PubMed:16436513}.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
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DR EMBL; AF172258; AAF87944.1; -; mRNA.
DR EMBL; AE014297; AAF56822.1; -; Genomic_DNA.
DR EMBL; AY058643; AAL13872.1; -; mRNA.
DR RefSeq; NP_001263050.1; NM_001276121.1.
DR RefSeq; NP_001287575.1; NM_001300646.1.
DR RefSeq; NP_524730.1; NM_079991.3.
DR AlphaFoldDB; Q9VAS7; -.
DR BioGRID; 68931; 4.
DR DIP; DIP-21773N; -.
DR IntAct; Q9VAS7; 4.
DR STRING; 7227.FBpp0303338; -.
DR iPTMnet; Q9VAS7; -.
DR PaxDb; Q9VAS7; -.
DR PRIDE; Q9VAS7; -.
DR DNASU; 44266; -.
DR EnsemblMetazoa; FBtr0085350; FBpp0084719; FBgn0265274.
DR EnsemblMetazoa; FBtr0330306; FBpp0303338; FBgn0265274.
DR EnsemblMetazoa; FBtr0345207; FBpp0311402; FBgn0265274.
DR GeneID; 44266; -.
DR KEGG; dme:Dmel_CG1448; -.
DR CTD; 44266; -.
DR FlyBase; FBgn0265274; Inx3.
DR VEuPathDB; VectorBase:FBgn0265274; -.
DR eggNOG; ENOG502S565; Eukaryota.
DR HOGENOM; CLU_035763_1_1_1; -.
DR InParanoid; Q9VAS7; -.
DR OMA; FAYFFCE; -.
DR OrthoDB; 738314at2759; -.
DR PhylomeDB; Q9VAS7; -.
DR BioGRID-ORCS; 44266; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Inx3; fly.
DR GenomeRNAi; 44266; -.
DR PRO; PR:Q9VAS7; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0265274; Expressed in wing disc and 54 other tissues.
DR ExpressionAtlas; Q9VAS7; baseline and differential.
DR Genevisible; Q9VAS7; DM.
DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005921; C:gap junction; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005243; F:gap junction channel activity; IDA:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0010496; P:intercellular transport; IDA:FlyBase.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR GO; GO:0007603; P:phototransduction, visible light; IGI: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; Cytoplasm; Developmental protein;
KW Gap junction; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..395
FT /note="Innexin inx3"
FT /id="PRO_0000208498"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 59..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 136..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 205..272
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 294..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 381
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 395 AA; 45357 MW; 86593F952D9DDC07 CRC64;
MAVFGMVSAV SGFIKIRYLL DKAVIDNMVF RCHYRITTAI LFTCCIIVTA NNLIGDPISC
INDGAIPMHV INTFCWITYT YTIPGQQHRQ IGTDVAGPGL GNEYGQEKRY HSYYQWVPFV
LFFQGLMFYV PHWVWKNMED GKIRMITDGL RGMVSVPDDY RRDRQDRILK YFVNSLNTHN
GYSFAYFFCE LLNFINVIVN IFMVDKFLGG AFMSYGTDVL KFSNMDQDKR FDPMIEIFPR
LTKCTFHKFG PSGSVQKHDT LCVLALNILN EKIYIFLWFW FIILATISGV AVLYSLVVIM
MPTTRETIIK RSYRSAQRKE IAGLVRRLEI GDFLILHFLS QNLSTRSYSD MLQQLCGLLG
ASRTPSAPST LEMNRISHPI YPPVETFGGG KETET
