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P33085 (SHAKB_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Innexin shaking-B
Alternative name(s):
Protein passover
Gene names
Name:shakB
Synonyms:Pas, shak-B
ORF Names:CG34358
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Structural component of the gap junctions at electrical synapses in distal and mid-depth levels in the lamina. Isoform Lethal forms voltage sensitive intercellular channels through homotypic interactions. Ref.8 Ref.9

Subunit structure

Monomer (isoform Lethal). Ref.9

Subcellular location

Cell membrane; Multi-pass membrane protein Potential. Cell junctiongap junction.

Tissue specificity

Isoform Neural is expressed in synapses of giant fibers (GF), in a large thoracic cell in location of postsynaptic target and optic lobe lamina and medulla. Isoform Lethal is expressed in embryonic mesodermal derivatives. During metamorphosis, both isoforms are dynamically expressed in pupal nervous system.

Disruption phenotype

Flies fail to jump in response to a light-off stimulus. Neural-specific mutants exhibit modified giant fiber system and gustatory response. Ref.2

Sequence similarities

Belongs to the pannexin family.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform Lethal (identifier: P33085-1)

Also known as: A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Neural (identifier: P33085-2)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     2-58: LDIFRGLKNL...GNPIDCVHTK → VSHVKIDSPV...GNPIDCVHTR
     72-116: QSTYTLKSLF...YKYYQWVCFC → HSTYTVVDAF...TKYYQWVAFT
Isoform B (identifier: P33085-3)

The sequence of this isoform differs from the canonical sequence as follows:
     121-121: A → P
     123-372: Missing.
Isoform D (identifier: P33085-4)

The sequence of this isoform differs from the canonical sequence as follows:
     2-116: LDIFRGLKNL...YKYYQWVCFC → YKPDTLTRRG...TKYYQWVAFT
Note: No experimental confirmation available.
Isoform E (identifier: P33085-6)

The sequence of this isoform differs from the canonical sequence as follows:
     2-119: LDIFRGLKNL...YQWVCFCLFF → MGRHCHVPKQ...QKKIPTTYNE
Note: No experimental confirmation available.
Isoform F (identifier: P33085-5)

The sequence of this isoform differs from the canonical sequence as follows:
     2-36: LDIFRGLKNLVKVSHVKTDSIVFRLHYSITVMILM → KKQGSEVPFPGVHNSQGRGPLTIKHTKYYQWVAFT
     37-116: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Innexin shaking-B
PRO_0000208500

Regions

Topological domain1 – 2121Cytoplasmic Potential
Transmembrane22 – 4221Helical; Potential
Topological domain43 – 11068Extracellular Potential
Transmembrane111 – 13121Helical; Potential
Topological domain132 – 18251Cytoplasmic Potential
Transmembrane183 – 20321Helical; Potential
Topological domain204 – 26764Extracellular Potential
Transmembrane268 – 28821Helical; Potential
Topological domain289 – 37284Cytoplasmic Potential

Natural variations

Alternative sequence2 – 119118LDIFR…FCLFF → MGRHCHVPKQTHHIQFAQLA QSPAVCGLSESAANLRYKLL LICHRVGIKIPRQKKIPTTY NE in isoform E.
VSP_037474
Alternative sequence2 – 116115LDIFR…WVCFC → YKPDTLTRRGSLRSLRSAPL LSTVLESTLSLTRIHPIASL ELPGLDYAVHSQSAFGAYGL AHPRDLATCTSLRSGLAAIT AASASAAGGVSQSQSALLGR YGPNASIRHGERKIVQPKRV LSRKLKPHLVADTVKQYISR AQRTTKKGSQEQQNMEFLRG VYAFMQVSRSSVSHVKIDSP VFRLHTNATVILLITFSIAV TTRQYVGNPIDCVHTRDIPE DVLNTYCWIHSTYTVVDAFM KKQGSEVPFPGVHNSQGRGP LTIKHTKYYQWVAFT in isoform D.
VSP_036913
Alternative sequence2 – 5857LDIFR…CVHTK → VSHVKIDSPVFRLHTNATVI LLITFSIAVTTRQYVGNPID CVHTR in isoform Neural.
VSP_002678
Alternative sequence2 – 3635LDIFR…VMILM → KKQGSEVPFPGVHNSQGRGP LTIKHTKYYQWVAFT in isoform F.
VSP_036914
Alternative sequence37 – 11680Missing in isoform F.
VSP_036915
Alternative sequence72 – 11645QSTYT…WVCFC → HSTYTVVDAFMKKQGSEVPF PGVHNSQGRGPLTIKHTKYY QWVAFT in isoform Neural.
VSP_002679
Alternative sequence1211A → P in isoform B.
VSP_012897
Alternative sequence123 – 372250Missing in isoform B.
VSP_012898

Experimental info

Sequence conflict2321I → M in AAA28745. Ref.2
Sequence conflict2321I → M in ABE73233. Ref.7
Sequence conflict247 – 2493SGE → GEV in AAC46584. Ref.4
Isoform D:
Sequence conflict31K → E in ABE73233. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform Lethal (A) [UniParc].

Last modified December 1, 2000. Version 3.
Checksum: 3DD1049D8F1D4481

FASTA37244,355
        10         20         30         40         50         60 
MLDIFRGLKN LVKVSHVKTD SIVFRLHYSI TVMILMSFSL IITTRQYVGN PIDCVHTKDI 

        70         80         90        100        110        120 
PEDVLNTYCW IQSTYTLKSL FLKKQGVSVP YPGIGNSDGD PADKKHYKYY QWVCFCLFFQ 

       130        140        150        160        170        180 
AILFYTPRWL WKSWEGGKIH ALIMDLDIGI CSEAEKKQKK KLLLDYLWEN LRYHNWWAYR 

       190        200        210        220        230        240 
YYVCELLALI NVIGQMFLMN RFFDGEFITF GLKVIDYMET DQEDRMDPMI YIFPRMTKCT 

       250        260        270        280        290        300 
FFKYGSSGEV EKHDAICILP LNVVNEKIYI FLWFWFILLT FLTLLTLIYR VVIIFSPRMR 

       310        320        330        340        350        360 
VYLFRMRFRL VRRDAIEIIV RRSKMGDWFL LYLLGENIDT VIFRDVVQDL ANRLGHNQHH 

       370 
RVPGLKGEIQ DA 

« Hide

Isoform Neural (C) [UniParc].

Checksum: B914B25C8D6E8DD5
Show »

FASTA36142,904
Isoform B [UniParc].

Checksum: D71A9AC29FB0A361
Show »

FASTA12214,147
Isoform D [UniParc].

Checksum: 3C517141DBCE54EA
Show »

FASTA53261,391
Isoform E [UniParc].

Checksum: 2124C91421ADF507
Show »

FASTA31637,711
Isoform F [UniParc].

Checksum: 2BEC859714E49365
Show »

FASTA29235,073

References

« Hide 'large scale' references
[1]"Analysis of a cDNA from the neurologically active locus shaking-B (Passover) of Drosophila melanogaster."
Crompton D.E., Griffin A., Davies J.A., Miklos G.L.G.
Gene 122:385-386(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
Strain: Oregon-R.
Tissue: Embryo.
[2]"Passover: a gene required for synaptic connectivity in the giant fiber system of Drosophila."
Krishnan S.N., Frei E., Swain G.P., Wyman R.J.
Cell 73:967-977(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NEURAL), DISRUPTION PHENOTYPE.
Strain: Oregon-R.
Tissue: Pupae.
[3]"Essential and neural transcripts from the Drosophila shaking-B locus are differentially expressed in the embryonic mesoderm and pupal nervous system."
Crompton D., Todman M., Wilkin M., Ji S., Davies J.
Dev. Biol. 170:142-158(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LETHAL).
Tissue: Embryo.
[4]"Molecular basis of intracistronic complementation in the Passover locus of Drosophila."
Krishnan S.N., Frei E., Schalet A.P., Wyman R.J.
Proc. Natl. Acad. Sci. U.S.A. 92:2021-2025(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LETHAL).
[5]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[6]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[7]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
Strain: Berkeley.
[8]"The shaking B gene in Drosophila regulates the number of gap junctions between photoreceptor terminals in the lamina."
Shimohigashi M., Meinertzhagen I.A.
J. Neurobiol. 35:105-117(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Drosophila Shaking-B protein forms gap junctions in paired Xenopus oocytes."
Phelan P., Stebbings L.A., Baines R.A., Bacon J.P., Davies J.A., Ford C.
Nature 391:181-184(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[10]"Nested transcripts of gap junction gene have distinct expression patterns."
Zhang Z., Curtin K.D., Sun Y.A., Wyman R.J.
J. Neurobiol. 40:288-301(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M98872 mRNA. Translation: AAA89079.1.
X65103 mRNA. Translation: CAA46228.1.
L13306 mRNA. Translation: AAA28745.1.
S78495 mRNA. Translation: AAB34769.1.
U17330 mRNA. Translation: AAC46584.1.
AE014298 Genomic DNA. Translation: AAF50880.2.
AE014298 Genomic DNA. Translation: AAF50882.2.
AE014298 Genomic DNA. Translation: AAF50883.1.
AE014298 Genomic DNA. Translation: ABW09456.2.
AE014298 Genomic DNA. Translation: ACL82952.1.
BT025062 mRNA. Translation: ABE73233.1.
PIRA40734.
JN0441.
RefSeqNP_001097038.2. NM_001103568.2.
NP_001138222.1. NM_001144750.1.
NP_523425.2. NM_078701.3.
NP_608410.2. NM_134566.2.
NP_728361.1. NM_170660.1.
UniGeneDm.2607.

3D structure databases

ModBaseSearch...

Protein family/group databases

TCDB1.A.25.1.4. gap junction-forming innexin family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0112571; FBpp0111483; FBgn0085387.
GeneID33062.
KEGGdme:Dmel_CG34358.

Organism-specific databases

CTD33062.
FlyBaseFBgn0085387. shakB.

Phylogenomic databases

eggNOGNOG74896.
GeneTreeENSGT00530000064205.
InParanoidQ9VRC2.
OMACAPRIRY.
OrthoDBEOG4QBZMV.

Gene expression databases

BgeeP33085.
GermOnlineCG32508. Drosophila melanogaster.

Family and domain databases

InterProIPR000990. Innexin.
[Graphical view]
PANTHERPTHR11893. PTHR11893. 1 hit.
PfamPF00876. Innexin. 1 hit.
[Graphical view]
PRINTSPR01262. INNEXIN.
PROSITEPS51013. PANNEXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi33062.
NextBio781749.

Entry information

Entry nameSHAKB_DROME
AccessionPrimary (citable) accession number: P33085
Secondary accession number(s): A8JUT3 expand/collapse secondary AC list , B7Z104, Q1RKZ8, Q24011, Q24520, Q26432, Q9VRB9, Q9VRC0, Q9VRC2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: December 1, 2000
Last modified: May 1, 2013
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families