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ANXB9_DROME
ID   ANXB9_DROME             Reviewed;         324 AA.
AC   P22464; A4V371; B5RJE6; Q8IGJ8; Q969D3; Q9NG55; Q9VDF3;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Annexin B9;
DE   AltName: Full=Annexin IX;
DE   AltName: Full=Annexin-9;
GN   Name=AnxB9; Synonyms=AnnIX; ORFNames=CG5730;
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] (ISOFORMS A AND B).
RA   Stoltzfus J.R., Grotewiel M.S.;
RT   "Novel isoform of annexin IX from Drosophila melanogaster.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
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, 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
RC   STRAIN=Berkeley; TISSUE=Embryo, and 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 29-324 (ISOFORM A), AND DEVELOPMENTAL STAGE.
RC   TISSUE=Head;
RX   PubMed=2141610; DOI=10.1016/s0021-9258(19)38604-1;
RA   Johnston P.A., Perin M.S., Reynolds G.A., Wasserman S.A., Suedhof T.C.;
RT   "Two novel annexins from Drosophila melanogaster. Cloning,
RT   characterization, and differential expression in development.";
RL   J. Biol. Chem. 265:11382-11388(1990).
CC   -!- INTERACTION:
CC       P22464-3; Q9VL93: Dmel\CG13117; NbExp=4; IntAct=EBI-26781545, EBI-179106;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=a; Synonyms=A;
CC         IsoId=P22464-1; Sequence=Displayed;
CC       Name=b; Synonyms=B, D;
CC         IsoId=P22464-2; Sequence=VSP_009664;
CC       Name=c; Synonyms=C;
CC         IsoId=P22464-3; Sequence=VSP_009665;
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development with highest
CC       expression seen in adults. {ECO:0000269|PubMed:2141610}.
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC       and phospholipid. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01245, ECO:0000305}.
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DR   EMBL; AF261718; AAF69016.1; -; mRNA.
DR   EMBL; AY007377; AAG12161.1; -; mRNA.
DR   EMBL; AE014297; AAF55841.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13848.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAS65188.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAS65189.1; -; Genomic_DNA.
DR   EMBL; AY118504; AAM49873.1; -; mRNA.
DR   EMBL; BT001749; AAN71504.1; -; mRNA.
DR   EMBL; BT044420; ACH92485.1; -; mRNA.
DR   EMBL; M34068; AAA28370.1; -; mRNA.
DR   PIR; A42234; LUFF9.
DR   RefSeq; NP_001262796.1; NM_001275867.1. [P22464-3]
DR   RefSeq; NP_001262797.1; NM_001275868.1. [P22464-3]
DR   RefSeq; NP_476603.1; NM_057255.3. [P22464-2]
DR   RefSeq; NP_476604.1; NM_057256.4. [P22464-1]
DR   RefSeq; NP_996252.1; NM_206530.2. [P22464-2]
DR   RefSeq; NP_996253.1; NM_206531.2. [P22464-3]
DR   AlphaFoldDB; P22464; -.
DR   SMR; P22464; -.
DR   BioGRID; 67463; 11.
DR   DIP; DIP-20322N; -.
DR   IntAct; P22464; 7.
DR   STRING; 7227.FBpp0088506; -.
DR   PaxDb; P22464; -.
DR   PRIDE; P22464; -.
DR   DNASU; 42492; -.
DR   EnsemblMetazoa; FBtr0089517; FBpp0088505; FBgn0000083. [P22464-1]
DR   EnsemblMetazoa; FBtr0089518; FBpp0088506; FBgn0000083. [P22464-2]
DR   EnsemblMetazoa; FBtr0089519; FBpp0088986; FBgn0000083. [P22464-3]
DR   EnsemblMetazoa; FBtr0089520; FBpp0088985; FBgn0000083. [P22464-2]
DR   EnsemblMetazoa; FBtr0336797; FBpp0307769; FBgn0000083. [P22464-3]
DR   EnsemblMetazoa; FBtr0336798; FBpp0307770; FBgn0000083. [P22464-3]
DR   GeneID; 42492; -.
DR   KEGG; dme:Dmel_CG5730; -.
DR   UCSC; CG5730-RD; d. melanogaster.
DR   CTD; 42492; -.
DR   FlyBase; FBgn0000083; AnxB9.
DR   VEuPathDB; VectorBase:FBgn0000083; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   GeneTree; ENSGT00940000172288; -.
DR   HOGENOM; CLU_025300_0_2_1; -.
DR   InParanoid; P22464; -.
DR   OMA; QQYYPFK; -.
DR   PhylomeDB; P22464; -.
DR   BioGRID-ORCS; 42492; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; AnxB9; fly.
DR   GenomeRNAi; 42492; -.
DR   PRO; PR:P22464; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0000083; Expressed in oviduct (Drosophila) and 25 other tissues.
DR   ExpressionAtlas; P22464; baseline and differential.
DR   Genevisible; P22464; DM.
DR   GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR   GO; GO:0012505; C:endomembrane system; IDA:FlyBase.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:FlyBase.
DR   GO; GO:0030507; F:spectrin binding; IPI:FlyBase.
DR   GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IMP:FlyBase.
DR   GO; GO:0030011; P:maintenance of cell polarity; IMP:FlyBase.
DR   GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IGI:FlyBase.
DR   Gene3D; 1.10.220.10; -; 4.
DR   InterPro; IPR001464; Annexin.
DR   InterPro; IPR018502; Annexin_repeat.
DR   InterPro; IPR018252; Annexin_repeat_CS.
DR   InterPro; IPR037104; Annexin_sf.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   SMART; SM00335; ANX; 4.
DR   SUPFAM; SSF47874; SSF47874; 1.
DR   PROSITE; PS00223; ANNEXIN_1; 3.
DR   PROSITE; PS51897; ANNEXIN_2; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Annexin; Calcium; Calcium/phospholipid-binding;
KW   Reference proteome; Repeat.
FT   CHAIN           1..324
FT                   /note="Annexin B9"
FT                   /id="PRO_0000067516"
FT   REPEAT          21..92
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          93..164
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          176..248
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          252..323
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   VAR_SEQ         308..324
FT                   /note="EDAETDIGYVLVTLTAW -> DDLSGDYSYVLQCLASY (in isoform
FT                   b)"
FT                   /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.1"
FT                   /id="VSP_009664"
FT   VAR_SEQ         308..324
FT                   /note="EDAETDIGYVLVTLTAW -> GDTSGDYKRALLAIVGF (in isoform
FT                   c)"
FT                   /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.5"
FT                   /id="VSP_009665"
FT   CONFLICT        13
FT                   /note="P -> H (in Ref. 4; AAN71504)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        268
FT                   /note="M -> L (in Ref. 1; AAG12161 and 6; AAA28370)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   324 AA;  36058 MW;  6DBF1021A7CC0DCA CRC64;
     MSSAEYYPFK CTPTVYPADP FDPVEDAAIL RKAMKGFGTD EKAIIEILAR RGIVQRLEIA
     EAFKTSYGKD LISDLKSELG GKFEDVILAL MTPLPQFYAQ ELHDAISGLG TDEEAIIEIL
     CTLSNYGIKT IAQFYEQSFG KSLESDLKGD TSGHFKRLCV SLVQGNRDEN QGVDEAAAIA
     DAQALHDAGE GQWGTDESTF NSILITRSYQ QLRQIFLEYE NLSGNDIEKA IKREFSGSVE
     KGFLAIVKCC KSKIDYFSER LHDSMAGMGT KDKTLIRIIV SRSEIDLGDI KEAFQNKYGK
     SLESWIKEDA ETDIGYVLVT LTAW
 
 
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