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INX6_DROME
ID   INX6_DROME              Reviewed;         481 AA.
AC   Q9VR82; Q9UA15;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Innexin inx6;
DE            Short=Innexin-6;
DE   AltName: Full=Gap junction protein prp6;
DE   AltName: Full=Pas-related protein 6;
GN   Name=Inx6; Synonyms=prp6; ORFNames=CG17063;
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], 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   [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 [MRNA] OF 228-431.
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).
CC   -!- FUNCTION: Structural components of the gap junctions. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC       junction {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Uniform expression in the imaginal wing disk.
CC       Expressed in an outer layer of the pupal developing CNS. Also expressed
CC       in pupal retina: cone cells and primary pigment cells.
CC       {ECO:0000269|PubMed:11960713}.
CC   -!- DEVELOPMENTAL STAGE: Not expressed in embryos. Expressed in larvae and
CC       pupae. {ECO:0000269|PubMed:11960713}.
CC   -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00351}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD50380.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY057373; AAL25821.1; -; mRNA.
DR   EMBL; AE014298; AAF50922.1; -; Genomic_DNA.
DR   EMBL; AF137271; AAD50380.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_572374.1; NM_132146.2.
DR   AlphaFoldDB; Q9VR82; -.
DR   STRING; 7227.FBpp0077031; -.
DR   PaxDb; Q9VR82; -.
DR   EnsemblMetazoa; FBtr0077339; FBpp0077031; FBgn0027107.
DR   GeneID; 31645; -.
DR   KEGG; dme:Dmel_CG17063; -.
DR   CTD; 31645; -.
DR   FlyBase; FBgn0027107; Inx6.
DR   VEuPathDB; VectorBase:FBgn0027107; -.
DR   eggNOG; ENOG502QR27; Eukaryota.
DR   GeneTree; ENSGT00530000064205; -.
DR   HOGENOM; CLU_035763_1_1_1; -.
DR   InParanoid; Q9VR82; -.
DR   OMA; NFWLMDV; -.
DR   OrthoDB; 738314at2759; -.
DR   PhylomeDB; Q9VR82; -.
DR   BioGRID-ORCS; 31645; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 31645; -.
DR   PRO; PR:Q9VR82; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0027107; Expressed in testis and 1 other tissue.
DR   Genevisible; Q9VR82; DM.
DR   GO; GO:0005921; C:gap junction; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0072375; P:medium-term memory; IMP:FlyBase.
DR   GO; GO:0007602; P:phototransduction; IBA:GO_Central.
DR   InterPro; IPR000990; Innexin.
DR   PANTHER; PTHR11893; PTHR11893; 1.
DR   Pfam; PF00876; Innexin; 1.
DR   PRINTS; PR01262; INNEXIN.
DR   PROSITE; PS51013; PANNEXIN; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Gap junction; Ion channel; Ion transport;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..481
FT                   /note="Innexin inx6"
FT                   /id="PRO_0000208502"
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..144
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        166..220
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        242..302
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        324..481
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        418
FT                   /note="S -> T (in Ref. 4; AAD50380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        431
FT                   /note="S -> R (in Ref. 4; AAD50380)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   481 AA;  55661 MW;  A435A51566B83013 CRC64;
     MYAAVKPLSN YLRLKTVRIY DPIFTLHSKC TIVILLTCTF LLSAKQYFGE PILCLSSERQ
     ADYVQSYCWT MGTYILPAEV DRDGGSSWEY ALYAPTSTAA ETFNVSSLRA LVAQNEQYAR
     FISIAEGVGP ETRGVTKRMY LRYYQWVFMI LLFQSLLFYF PSFLWKVWEG QRMEQLCCEV
     GDALIVEATY RTRLQMLTRY FRAQFAPIHW CYSIKYAFCE LLNVFISILN FWLMDVVFNG
     FWYKYIHALA AIPVYDWNLW NLMTSRVFPK VAKCEMFVYG PSGTPNIMDI LCVLPLNILN
     EKIFAVLYVW FLFIALLAIM NILYRLLVIC CPELRLQLLR THLNGMPKSH VREVLASAGY
     GDWFVLMCVS INVNPTLFRE LLEQLYAKLN QARCTEPVFA EQPCQQVPQL AQVPQLFSHA
     KLDRCPSRNC SLLIDPTADR HSICTESSHR VTAMPTAPTL NLMAPNDEII SMDRFFHESH
     A
 
 
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