INX2_DROME
ID INX2_DROME Reviewed; 367 AA.
AC Q9V427; A4V431;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Innexin inx2;
DE Short=Innexin-2;
DE AltName: Full=Gap junction protein prp33;
DE AltName: Full=Pas-related protein 33;
GN Name=Inx2; Synonyms=prp33; ORFNames=CG4590;
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=Head;
RX PubMed=10352230; DOI=10.1016/s0378-1119(99)00123-7;
RA Curtin K.D., Zhang Z., Wyman R.J.;
RT "Drosophila has several genes for gap junction proteins.";
RL Gene 232:191-201(1999).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11956317; DOI=10.1242/jcs.115.9.1859;
RA Bauer R., Lehmann C., Fuss B., Eckardt F., Hoch M.;
RT "The Drosophila gap junction channel gene innexin 2 controls foregut
RT development in response to Wingless signalling.";
RL J. Cell Sci. 115:1859-1867(2002).
RN [7]
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 [8]
RP FUNCTION, INTERACTION WITH SHG AND ARM, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 [9]
RP INTERACTION WITH INX3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP 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 [10]
RP FUNCTION, 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 [11]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22001874; DOI=10.1016/j.mod.2011.09.005;
RA Mukai M., Kato H., Hira S., Nakamura K., Kita H., Kobayashi S.;
RT "Innexin2 gap junctions in somatic support cells are required for cyst
RT formation and for egg chamber formation in Drosophila.";
RL Mech. Dev. 128:510-523(2011).
CC -!- FUNCTION: Structural components of the gap junctions. Involved in gap
CC junctional communication between germline and somatic cells which is
CC essential for normal oogenesis. In embryonic epidermis, required for
CC epithelial morphogenesis. Required for keyhole formation during early
CC stages of proventriculus development in response to wg signaling. In
CC follicle cells, promotes the formation of egg chambers in part through
CC regulation of shg and baz at the boundary between germ cells and
CC follicle cells. In inner germarial sheath cells, required for survival
CC of early germ cells and for cyst formation.
CC {ECO:0000269|PubMed:11956317, ECO:0000269|PubMed:15047872,
CC ECO:0000269|PubMed:19038051, ECO:0000269|PubMed:22001874}.
CC -!- SUBUNIT: Monomer and heterooligomer with ogre or Inx3 (via cytoplasmic
CC C-terminal region). Interacts (via cytoplasmic loop) with shg (via
CC cytoplasmic region). Interacts with arm. {ECO:0000269|PubMed:10352230,
CC ECO:0000269|PubMed:10888681, ECO:0000269|PubMed:15047872,
CC ECO:0000269|PubMed:16436513}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC junction. Cytoplasm. Apical cell membrane. Apicolateral cell membrane.
CC Basolateral cell membrane. Lateral cell membrane. Note=In ovary,
CC localizes to the apicolateral membrane between follicle cells and to
CC the apical membrane between follicle cells and germline cells.
CC Accumulates in the apicolateral membrane of epithelial cells in the
CC epidermis. In salivary gland cells, accumulates in the basolateral
CC membrane. In hindgut epithelial cells, accumulates in the lateral
CC membrane. In nurse cells, localizes around the nuclei at oogenesis
CC stage 10a and then, during stages 10b and 11, in cytoplasmic clouds and
CC particles which become delivered into the oocyte during nurse cell
CC regression.
CC -!- TISSUE SPECIFICITY: In ovary, expressed in inner germarial sheath
CC cells, prefollicular cells, follicle cells, nurse cells and oocytes.
CC Expressed in embryonic epithelial cells. Expressed in foregut and
CC hindgut from stage 11-17, segmentally repeated tracheal placodes at
CC stage 14, salivary gland at stage 16 and proventriculus at stage 16-17
CC (at protein level). During germband extension stage (stage 7),
CC expressed in epidermal epithelial cells. Expressed in cephalic furrow.
CC Repeating epidermal pattern emerges at stage 11, refines to one or two
CC cells at each side of the segment borders by stage 13. Expressed in the
CC imaginal wing disk. In pupae, expressed in the CNS and in primary,
CC secondary and tertiary pigment cells of the retina. Expressed in optic
CC lamina of the adult CNS. {ECO:0000269|PubMed:10352230,
CC ECO:0000269|PubMed:10888681, ECO:0000269|PubMed:11956317,
CC ECO:0000269|PubMed:11960713, ECO:0000269|PubMed:15047872,
CC ECO:0000269|PubMed:16436513, ECO:0000269|PubMed:19038051,
CC ECO:0000269|PubMed:22001874}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically. Expressed
CC during oogenesis and embryogenesis. Expressed in larvae and pupae.
CC {ECO:0000269|PubMed:11956317, ECO:0000269|PubMed:11960713,
CC ECO:0000269|PubMed:16436513}.
CC -!- INDUCTION: Expression in embryos at ectoderm/endoderm boundaries during
CC gut organogenesis is induced by activation of the wg signaling cascade.
CC {ECO:0000269|PubMed:11956317}.
CC -!- DISRUPTION PHENOTYPE: Female sterility. Only one third of the zygotic
CC mutant embryos survive up to the first instar larval stage. These
CC mutant larvae display a feeding defect most probably caused by a
CC keyhole formation defect during proventriculus development. The feeding
CC defect may result in larvae death by starvation. Zygotic mutant embryos
CC display large holes in the head region and a variable spectrum of
CC segment defects. In maternal and zygotic mutant embryos, epithelial
CC tissues and organs are severely affected, the cuticle fails to form and
CC extensive cell death occurs. {ECO:0000269|PubMed:11956317,
CC ECO:0000269|PubMed:15047872, ECO:0000269|PubMed:22001874}.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
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DR EMBL; AF137269; AAD50378.1; -; mRNA.
DR EMBL; AF172257; AAF87943.1; -; mRNA.
DR EMBL; AE014298; AAF46229.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09193.1; -; Genomic_DNA.
DR EMBL; AY060368; AAL25407.1; -; mRNA.
DR RefSeq; NP_001162684.1; NM_001169213.2.
DR RefSeq; NP_001259301.1; NM_001272372.1.
DR RefSeq; NP_572375.1; NM_132147.4.
DR RefSeq; NP_727150.1; NM_167104.3.
DR AlphaFoldDB; Q9V427; -.
DR BioGRID; 58124; 5.
DR DIP; DIP-22749N; -.
DR IntAct; Q9V427; 1.
DR STRING; 7227.FBpp0070966; -.
DR TCDB; 1.A.25.1.14; the gap junction-forming innexin (innexin) family.
DR PaxDb; Q9V427; -.
DR DNASU; 31646; -.
DR EnsemblMetazoa; FBtr0071005; FBpp0070965; FBgn0027108.
DR EnsemblMetazoa; FBtr0071006; FBpp0070966; FBgn0027108.
DR EnsemblMetazoa; FBtr0301860; FBpp0291074; FBgn0027108.
DR EnsemblMetazoa; FBtr0332314; FBpp0304593; FBgn0027108.
DR GeneID; 31646; -.
DR KEGG; dme:Dmel_CG4590; -.
DR CTD; 31646; -.
DR FlyBase; FBgn0027108; Inx2.
DR VEuPathDB; VectorBase:FBgn0027108; -.
DR eggNOG; ENOG502QR27; Eukaryota.
DR HOGENOM; CLU_035763_1_1_1; -.
DR InParanoid; Q9V427; -.
DR OMA; TQNFYAF; -.
DR OrthoDB; 738314at2759; -.
DR PhylomeDB; Q9V427; -.
DR BioGRID-ORCS; 31646; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31646; -.
DR PRO; PR:Q9V427; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0027108; Expressed in wing disc and 66 other tissues.
DR ExpressionAtlas; Q9V427; baseline and differential.
DR Genevisible; Q9V427; DM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0016323; C:basolateral 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; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005243; F:gap junction channel activity; IDA:FlyBase.
DR GO; GO:0007154; P:cell communication; IDA:FlyBase.
DR GO; GO:0007440; P:foregut morphogenesis; IMP:FlyBase.
DR GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0030727; P:germarium-derived female germ-line cyst formation; IMP:FlyBase.
DR GO; GO:0010496; P:intercellular transport; IDA:FlyBase.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:FlyBase.
DR GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP: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 Differentiation; Gap junction; Ion channel; Ion transport; Membrane;
KW Oogenesis; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..367
FT /note="Innexin inx2"
FT /id="PRO_0000208496"
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..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 201..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..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 130..179
FT /note="Interaction with shg"
SQ SEQUENCE 367 AA; 42488 MW; 25DA43DF18920B99 CRC64;
MFDVFGSVKG LLKIDQVCID NNVFRMHYKA TVIILIAFSL LVTSRQYIGD PIDCIVDEIP
LGVMDTYCWI YSTFTVPERL TGITGRDVVQ PGVGSHVEGE DEVKYHKYYQ WVCFVLFFQA
ILFYVPRYLW KSWEGGRLKM LVMDLNSPIV NDECKNDRKK ILVDYFIGNL NRHNFYAFRF
FVCEALNFVN VIGQIYFVDF FLDGEFSTYG SDVLKFTELE PDERIDPMAR VFPKVTKCTF
HKYGPSGSVQ THDGLCVLPL NIVNEKIYVF LWFWFIILSI MSGISLIYRI AVVAGPKLRH
LLLRARSRLA ESEEVELVAN KCNIGDWFLL YQLGKNIDPL IYKEVISDLS REMSGDEHSA
HKRPFDA
