SHAKB_DROME
ID SHAKB_DROME Reviewed; 372 AA.
AC P33085; A8JUT3; B7Z104; Q1RKZ8; Q24011; Q24520; Q26432; Q9VRB9; Q9VRC0;
AC Q9VRC2;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Innexin shaking-B;
DE AltName: Full=Protein passover;
GN Name=shakB; Synonyms=Pas, shak-B; ORFNames=CG34358;
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] (ISOFORM B).
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=1487155; DOI=10.1016/0378-1119(92)90233-f;
RA Crompton D.E., Griffin A., Davies J.A., Miklos G.L.G.;
RT "Analysis of a cDNA from the neurologically active locus shaking-B
RT (Passover) of Drosophila melanogaster.";
RL Gene 122:385-386(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NEURAL), AND DISRUPTION PHENOTYPE.
RC STRAIN=Oregon-R; TISSUE=Pupae;
RX PubMed=8500183; DOI=10.1016/0092-8674(93)90274-t;
RA Krishnan S.N., Frei E., Swain G.P., Wyman R.J.;
RT "Passover: a gene required for synaptic connectivity in the giant fiber
RT system of Drosophila.";
RL Cell 73:967-977(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LETHAL).
RC TISSUE=Embryo;
RX PubMed=7601305; DOI=10.1006/dbio.1995.1203;
RA Crompton D., Todman M., Wilkin M., Ji S., Davies J.;
RT "Essential and neural transcripts from the Drosophila shaking-B locus are
RT differentially expressed in the embryonic mesoderm and pupal nervous
RT system.";
RL Dev. Biol. 170:142-158(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LETHAL).
RX PubMed=7892218; DOI=10.1073/pnas.92.6.2021;
RA Krishnan S.N., Frei E., Schalet A.P., Wyman R.J.;
RT "Molecular basis of intracistronic complementation in the Passover locus of
RT Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:2021-2025(1995).
RN [5]
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 [6]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX PubMed=9552170;
RX DOI=10.1002/(sici)1097-4695(199804)35:1<105::aid-neu9>3.0.co;2-9;
RA Shimohigashi M., Meinertzhagen I.A.;
RT "The shaking B gene in Drosophila regulates the number of gap junctions
RT between photoreceptor terminals in the lamina.";
RL J. Neurobiol. 35:105-117(1998).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9428764; DOI=10.1038/34426;
RA Phelan P., Stebbings L.A., Baines R.A., Bacon J.P., Davies J.A., Ford C.;
RT "Drosophila Shaking-B protein forms gap junctions in paired Xenopus
RT oocytes.";
RL Nature 391:181-184(1998).
RN [10]
RP ALTERNATIVE SPLICING.
RX PubMed=10440730;
RX DOI=10.1002/(sici)1097-4695(19990905)40:3<288::aid-neu2>3.0.co;2-o;
RA Zhang Z., Curtin K.D., Sun Y.A., Wyman R.J.;
RT "Nested transcripts of gap junction gene have distinct expression
RT patterns.";
RL J. Neurobiol. 40:288-301(1999).
CC -!- FUNCTION: Structural component of the gap junctions at electrical
CC synapses in distal and mid-depth levels in the lamina. Isoform Lethal
CC forms voltage sensitive intercellular channels through homotypic
CC interactions. {ECO:0000269|PubMed:9428764, ECO:0000269|PubMed:9552170}.
CC -!- SUBUNIT: Monomer (isoform Lethal). {ECO:0000269|PubMed:9428764}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC junction.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=Lethal; Synonyms=A;
CC IsoId=P33085-1; Sequence=Displayed;
CC Name=Neural; Synonyms=C;
CC IsoId=P33085-2; Sequence=VSP_002678, VSP_002679;
CC Name=B;
CC IsoId=P33085-3; Sequence=VSP_012897, VSP_012898;
CC Name=D;
CC IsoId=P33085-4; Sequence=VSP_036913;
CC Name=E;
CC IsoId=P33085-6; Sequence=VSP_037474;
CC Name=F;
CC IsoId=P33085-5; Sequence=VSP_036914, VSP_036915;
CC -!- TISSUE SPECIFICITY: Isoform Neural is expressed in synapses of giant
CC fibers (GF), in a large thoracic cell in location of postsynaptic
CC target and optic lobe lamina and medulla. Isoform Lethal is expressed
CC in embryonic mesodermal derivatives. During metamorphosis, both
CC isoforms are dynamically expressed in pupal nervous system.
CC -!- DISRUPTION PHENOTYPE: Flies fail to jump in response to a light-off
CC stimulus. Neural-specific mutants exhibit modified giant fiber system
CC and gustatory response. {ECO:0000269|PubMed:8500183}.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
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DR EMBL; M98872; AAA89079.1; -; mRNA.
DR EMBL; X65103; CAA46228.1; -; mRNA.
DR EMBL; L13306; AAA28745.1; -; mRNA.
DR EMBL; S78495; AAB34769.1; -; mRNA.
DR EMBL; U17330; AAC46584.1; -; mRNA.
DR EMBL; AE014298; AAF50880.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF50882.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF50883.1; -; Genomic_DNA.
DR EMBL; AE014298; ABW09456.2; -; Genomic_DNA.
DR EMBL; AE014298; ACL82952.1; -; Genomic_DNA.
DR EMBL; BT025062; ABE73233.1; -; mRNA.
DR PIR; A40734; A40734.
DR PIR; JN0441; JN0441.
DR RefSeq; NP_001097038.2; NM_001103568.3. [P33085-6]
DR RefSeq; NP_001138222.1; NM_001144750.2. [P33085-5]
DR RefSeq; NP_523425.2; NM_078701.3. [P33085-2]
DR RefSeq; NP_608410.2; NM_134566.3. [P33085-4]
DR RefSeq; NP_728361.1; NM_170660.2. [P33085-1]
DR AlphaFoldDB; P33085; -.
DR SMR; P33085; -.
DR BioGRID; 59350; 6.
DR IntAct; P33085; 1.
DR STRING; 7227.FBpp0111481; -.
DR TCDB; 1.A.25.1.4; the gap junction-forming innexin (innexin) family.
DR EnsemblMetazoa; FBtr0112569; FBpp0111481; FBgn0085387. [P33085-4]
DR EnsemblMetazoa; FBtr0112570; FBpp0111482; FBgn0085387. [P33085-2]
DR EnsemblMetazoa; FBtr0112571; FBpp0111483; FBgn0085387. [P33085-1]
DR EnsemblMetazoa; FBtr0112572; FBpp0111484; FBgn0085387. [P33085-6]
DR EnsemblMetazoa; FBtr0114645; FBpp0113137; FBgn0085387. [P33085-5]
DR GeneID; 33062; -.
DR KEGG; dme:Dmel_CG34358; -.
DR UCSC; CG34358-RD; d. melanogaster.
DR CTD; 33062; -.
DR FlyBase; FBgn0085387; shakB.
DR VEuPathDB; VectorBase:FBgn0085387; -.
DR eggNOG; ENOG502QWRS; Eukaryota.
DR HOGENOM; CLU_035763_1_1_1; -.
DR InParanoid; P33085; -.
DR OMA; TSYTFWG; -.
DR PhylomeDB; P33085; -.
DR BioGRID-ORCS; 33062; 0 hits in 1 CRISPR screen.
DR ChiTaRS; shakB; fly.
DR GenomeRNAi; 33062; -.
DR PRO; PR:P33085; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0085387; Expressed in brain and 33 other tissues.
DR ExpressionAtlas; P33085; baseline and differential.
DR Genevisible; P33085; DM.
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:FlyBase.
DR GO; GO:0005243; F:gap junction channel activity; IMP:UniProtKB.
DR GO; GO:0009881; F:photoreceptor activity; IMP:UniProtKB.
DR GO; GO:0010644; P:cell communication by electrical coupling; IMP:FlyBase.
DR GO; GO:0016264; P:gap junction assembly; IMP:UniProtKB.
DR GO; GO:0010496; P:intercellular transport; ISS:FlyBase.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0007630; P:jump response; IMP:FlyBase.
DR GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR GO; GO:0003254; P:regulation of membrane depolarization; IMP:FlyBase.
DR GO; GO:0009416; P:response to light stimulus; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; 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 Alternative splicing; Behavior; Cell junction; Cell membrane; Gap junction;
KW Ion channel; Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..372
FT /note="Innexin shaking-B"
FT /id="PRO_0000208500"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 43..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..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 204..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..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 2..119
FT /note="LDIFRGLKNLVKVSHVKTDSIVFRLHYSITVMILMSFSLIITTRQYVGNPID
FT CVHTKDIPEDVLNTYCWIQSTYTLKSLFLKKQGVSVPYPGIGNSDGDPADKKHYKYYQW
FT VCFCLFF -> MGRHCHVPKQTHHIQFAQLAQSPAVCGLSESAANLRYKLLLICHRVGI
FT KIPRQKKIPTTYNE (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_037474"
FT VAR_SEQ 2..116
FT /note="LDIFRGLKNLVKVSHVKTDSIVFRLHYSITVMILMSFSLIITTRQYVGNPID
FT CVHTKDIPEDVLNTYCWIQSTYTLKSLFLKKQGVSVPYPGIGNSDGDPADKKHYKYYQW
FT VCFC -> YKPDTLTRRGSLRSLRSAPLLSTVLESTLSLTRIHPIASLELPGLDYAVHS
FT QSAFGAYGLAHPRDLATCTSLRSGLAAITAASASAAGGVSQSQSALLGRYGPNASIRHG
FT ERKIVQPKRVLSRKLKPHLVADTVKQYISRAQRTTKKGSQEQQNMEFLRGVYAFMQVSR
FT SSVSHVKIDSPVFRLHTNATVILLITFSIAVTTRQYVGNPIDCVHTRDIPEDVLNTYCW
FT IHSTYTVVDAFMKKQGSEVPFPGVHNSQGRGPLTIKHTKYYQWVAFT (in isoform
FT D)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_036913"
FT VAR_SEQ 2..58
FT /note="LDIFRGLKNLVKVSHVKTDSIVFRLHYSITVMILMSFSLIITTRQYVGNPID
FT CVHTK -> VSHVKIDSPVFRLHTNATVILLITFSIAVTTRQYVGNPIDCVHTR (in
FT isoform Neural)"
FT /evidence="ECO:0000303|PubMed:8500183"
FT /id="VSP_002678"
FT VAR_SEQ 2..36
FT /note="LDIFRGLKNLVKVSHVKTDSIVFRLHYSITVMILM -> KKQGSEVPFPGVH
FT NSQGRGPLTIKHTKYYQWVAFT (in isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_036914"
FT VAR_SEQ 37..116
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_036915"
FT VAR_SEQ 72..116
FT /note="QSTYTLKSLFLKKQGVSVPYPGIGNSDGDPADKKHYKYYQWVCFC -> HST
FT YTVVDAFMKKQGSEVPFPGVHNSQGRGPLTIKHTKYYQWVAFT (in isoform
FT Neural)"
FT /evidence="ECO:0000303|PubMed:8500183"
FT /id="VSP_002679"
FT VAR_SEQ 121
FT /note="A -> P (in isoform B)"
FT /evidence="ECO:0000303|PubMed:1487155"
FT /id="VSP_012897"
FT VAR_SEQ 123..372
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:1487155"
FT /id="VSP_012898"
FT CONFLICT 232
FT /note="I -> M (in Ref. 2; AAA28745 and 7; ABE73233)"
FT /evidence="ECO:0000305"
FT CONFLICT 247..249
FT /note="SGE -> GEV (in Ref. 4; AAC46584)"
FT /evidence="ECO:0000305"
FT CONFLICT P33085-4:3
FT /note="K -> E (in Ref. 7; ABE73233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 44355 MW; 3DD1049D8F1D4481 CRC64;
MLDIFRGLKN LVKVSHVKTD SIVFRLHYSI TVMILMSFSL IITTRQYVGN PIDCVHTKDI
PEDVLNTYCW IQSTYTLKSL FLKKQGVSVP YPGIGNSDGD PADKKHYKYY QWVCFCLFFQ
AILFYTPRWL WKSWEGGKIH ALIMDLDIGI CSEAEKKQKK KLLLDYLWEN LRYHNWWAYR
YYVCELLALI NVIGQMFLMN RFFDGEFITF GLKVIDYMET DQEDRMDPMI YIFPRMTKCT
FFKYGSSGEV EKHDAICILP LNVVNEKIYI FLWFWFILLT FLTLLTLIYR VVIIFSPRMR
VYLFRMRFRL VRRDAIEIIV RRSKMGDWFL LYLLGENIDT VIFRDVVQDL ANRLGHNQHH
RVPGLKGEIQ DA
