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CPN_DROME
ID   CPN_DROME               Reviewed;         864 AA.
AC   Q02910; B5X510; Q95U45; Q9VGC8; Q9VGC9;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Calphotin;
GN   Name=Cpn; Synonyms=cap; ORFNames=CG4795;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=Canton-S; TISSUE=Head;
RX   PubMed=8094559; DOI=10.1073/pnas.90.4.1531;
RA   Martin J.H., Benzer S., Rudnicka M., Miller C.A.;
RT   "Calphotin: a Drosophila photoreceptor cell calcium-binding protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:1531-1535(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=Canton-S; TISSUE=Retinal photoreceptor;
RX   PubMed=8434015; DOI=10.1073/pnas.90.4.1536;
RA   Ballinger D.G., Xue N., Harshman K.D.;
RT   "A Drosophila photoreceptor cell-specific protein, calphotin, binds calcium
RT   and contains a leucine zipper.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:1536-1540(1993).
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, 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND RNA EDITING OF
RP   POSITION 402.
RC   STRAIN=Berkeley; TISSUE=Head;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   RNA EDITING OF POSITION 402.
RX   PubMed=17018572; DOI=10.1261/rna.254306;
RA   Stapleton M., Carlson J.W., Celniker S.E.;
RT   "RNA editing in Drosophila melanogaster: new targets and functional
RT   consequences.";
RL   RNA 12:1922-1932(2006).
CC   -!- FUNCTION: Plays important roles in both rhabdomere development and in
CC       photoreceptor cell survival. Might function as a calcium-sequestering
CC       'sponge' to regulate the amount of free cytoplasmic calcium. It binds
CC       0.3 mole of Ca(2+) per mole of protein. {ECO:0000269|PubMed:8094559,
CC       ECO:0000269|PubMed:8434015}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8094559}.
CC       Note=Hypodense compartment.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=B;
CC         IsoId=Q02910-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=Q02910-2; Sequence=VSP_013780;
CC   -!- TISSUE SPECIFICITY: Soma and axons of photoreceptor cells of compound
CC       eyes and ocelli. {ECO:0000269|PubMed:8094559,
CC       ECO:0000269|PubMed:8434015}.
CC   -!- DEVELOPMENTAL STAGE: Expressed early in photoreceptor cell development.
CC   -!- RNA EDITING: Modified_positions=402 {ECO:0000269|PubMed:12537569,
CC       ECO:0000269|PubMed:17018572}; Note=Partially edited. Target of Adar.;
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DR   EMBL; L02111; AAA28405.1; -; mRNA.
DR   EMBL; L05080; AAA28420.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF54754.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF54755.1; -; Genomic_DNA.
DR   EMBL; AY058315; AAL13544.1; -; mRNA.
DR   EMBL; BT046129; ACI46517.1; -; mRNA.
DR   PIR; A47282; A47282.
DR   PIR; A47283; A47283.
DR   RefSeq; NP_731673.1; NM_169454.2. [Q02910-2]
DR   RefSeq; NP_731674.1; NM_169455.2. [Q02910-1]
DR   AlphaFoldDB; Q02910; -.
DR   BioGRID; 66588; 26.
DR   IntAct; Q02910; 3.
DR   STRING; 7227.FBpp0082021; -.
DR   PaxDb; Q02910; -.
DR   PRIDE; Q02910; -.
DR   DNASU; 41474; -.
DR   EnsemblMetazoa; FBtr0082547; FBpp0082020; FBgn0261714. [Q02910-2]
DR   EnsemblMetazoa; FBtr0082548; FBpp0082021; FBgn0261714. [Q02910-1]
DR   GeneID; 41474; -.
DR   KEGG; dme:Dmel_CG4795; -.
DR   CTD; 41474; -.
DR   FlyBase; FBgn0261714; Cpn.
DR   VEuPathDB; VectorBase:FBgn0261714; -.
DR   eggNOG; KOG1216; Eukaryota.
DR   InParanoid; Q02910; -.
DR   OMA; TNYEGQQ; -.
DR   PhylomeDB; Q02910; -.
DR   SignaLink; Q02910; -.
DR   BioGRID-ORCS; 41474; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 41474; -.
DR   PRO; PR:Q02910; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0261714; Expressed in head capsule and 7 other tissues.
DR   Genevisible; Q02910; DM.
DR   GO; GO:0030424; C:axon; IDA:FlyBase.
DR   GO; GO:0044297; C:cell body; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005509; F:calcium ion binding; IDA:FlyBase.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR   GO; GO:0051208; P:sequestering of calcium ion; IDA:FlyBase.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Cytoplasm; Reference proteome; RNA editing;
KW   Sensory transduction; Vision.
FT   CHAIN           1..864
FT                   /note="Calphotin"
FT                   /id="PRO_0000079290"
FT   REGION          816..858
FT                   /note="Leucine-zipper"
FT   VAR_SEQ         644..665
FT                   /note="Missing (in isoform A)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_013780"
FT   VARIANT         402
FT                   /note="S -> G (in RNA edited version)"
FT   CONFLICT        36
FT                   /note="A -> AVAPAVVA (in Ref. 2; AAA28420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="I -> T (in Ref. 2; AAA28420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        64
FT                   /note="I -> V (in Ref. 2; AAA28420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76
FT                   /note="A -> T (in Ref. 1; AAA28405)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="Missing (in Ref. 1; AAA28405)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127..128
FT                   /note="AP -> VQ (in Ref. 1; AAA28405)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="V -> I (in Ref. 1; AAA28405)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="T -> S (in Ref. 1; AAA28405)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        535
FT                   /note="A -> E (in Ref. 2; AAA28420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        646..647
FT                   /note="YP -> FPEA (in Ref. 1; AAA28405 and 2; AAA28420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        698
FT                   /note="T -> I (in Ref. 1; AAA28405)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        702
FT                   /note="L -> V (in Ref. 1; AAA28405)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        720
FT                   /note="E -> D (in Ref. 1; AAA28405)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        784
FT                   /note="A -> P (in Ref. 1; AAA28405 and 2; AAA28420)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   864 AA;  84596 MW;  5B3635A283E5C658 CRC64;
     MEPGTIPSPV SAPVAAPVTP SAVAAPVQVV SPAAVAPAPA APIAVTPVAP PPTLASVQPA
     TVTIPAPAPI AAASVAPVAS VAPPVVAAPT PPAASPVSTP PVAVAQIPVA VSAPVAPPVA
     ATPTPVAPIP VAAPVIATPP VAASAPTPAA VTPVVSPVIA TPPVVPANTT VPVAAPVAAV
     PAAVPVVAPV LAPAVAPAVA PVVAETPAPP PVAEIPVATI PECVAPLIPE VSVVATKPLA
     AAEPVVVAPP ATETPVVAPA AASPHVSVAP AVETAVVAPV SASTEPPVAA ATLTTAPETP
     ALAPVVAESQ VAANTVVATP PTPAPEPETI APPVVAETPE VASVAVAETT PPVVPPVAAE
     SIPAPVVATT PVPATLAVTD PDVTASAVPE LPPVIAPSPV PSAVAETPVD LAPPVLPPVA
     AEPVPAVVAE ETPETPAPAS APVTIAALDI PEVAPVIAAP SDAPAEAPSA AAPIVSTPPT
     TASVPETTAP PAAVPTEPID VSVLSEAAIE TPVAPPVEVT TEVAVADVAP PEAAADLIIE
     PVEPPAPIPD LLEQTTSVPA VEAAESTSSP IPETSLPPPN EAVASPEVAV APITAPEPIP
     EPEPSLATPT EPIPVEAPVV IQEAVDAVEV PVTETSTSIP ETTVEYPVAE KVLDPAITEA
     PVTTQEPDVA NINDGAPATE ITTPAVEIVT AAAEVSDTAI PLIDPPVPQE IAVAEIPETE
     TKPAEVIVEQ STIPIEAPVP EVSKYAEPVI SEAPAAEVPI TAGDNPDNTS VGISEVVPTI
     AEKAVEEVPT SEIPEQSSSP SDSVPVAKIT PLLRDLQTTD VSLLAIAATL DAIGEKLKDQ
     KARNQQVMDR LCEIEKILGP PKSN
 
 
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