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CAPR1_DROME
ID   CAPR1_DROME             Reviewed;         961 AA.
AC   Q9I7D3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Caprin homolog;
GN   Name=Capr; ORFNames=CG18811;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16979555; DOI=10.1016/j.cub.2006.07.062;
RA   Cermelli S., Guo Y., Gross S.P., Welte M.A.;
RT   "The lipid-droplet proteome reveals that droplets are a protein-storage
RT   depot.";
RL   Curr. Biol. 16:1783-1795(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-806, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA   Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy for
RT   (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT   Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758; THR-764; SER-765;
RP   SER-777; THR-778; SER-791 AND SER-798, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:16979555}.
CC   -!- SIMILARITY: Belongs to the caprin family. {ECO:0000305}.
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DR   EMBL; AE014296; AAG22572.1; -; Genomic_DNA.
DR   EMBL; BT016057; AAV36942.1; -; mRNA.
DR   RefSeq; NP_001287107.1; NM_001300178.1.
DR   RefSeq; NP_652671.1; NM_144414.2.
DR   PDB; 6BK4; X-ray; 1.80 A; A/B=186-309.
DR   PDBsum; 6BK4; -.
DR   AlphaFoldDB; Q9I7D3; -.
DR   SMR; Q9I7D3; -.
DR   BioGRID; 72829; 9.
DR   IntAct; Q9I7D3; 2.
DR   MINT; Q9I7D3; -.
DR   STRING; 7227.FBpp0074865; -.
DR   iPTMnet; Q9I7D3; -.
DR   PaxDb; Q9I7D3; -.
DR   PRIDE; Q9I7D3; -.
DR   DNASU; 59172; -.
DR   EnsemblMetazoa; FBtr0075098; FBpp0074865; FBgn0042134.
DR   EnsemblMetazoa; FBtr0345806; FBpp0311792; FBgn0042134.
DR   GeneID; 59172; -.
DR   KEGG; dme:Dmel_CG18811; -.
DR   UCSC; CG18811-RA; d. melanogaster.
DR   CTD; 59172; -.
DR   FlyBase; FBgn0042134; Capr.
DR   VEuPathDB; VectorBase:FBgn0042134; -.
DR   eggNOG; ENOG502QUGC; Eukaryota.
DR   GeneTree; ENSGT00940000153438; -.
DR   HOGENOM; CLU_307626_0_0_1; -.
DR   InParanoid; Q9I7D3; -.
DR   OMA; VEQNYFK; -.
DR   OrthoDB; 714608at2759; -.
DR   PhylomeDB; Q9I7D3; -.
DR   SignaLink; Q9I7D3; -.
DR   BioGRID-ORCS; 59172; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 59172; -.
DR   PRO; PR:Q9I7D3; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0042134; Expressed in cleaving embryo and 24 other tissues.
DR   ExpressionAtlas; Q9I7D3; baseline and differential.
DR   Genevisible; Q9I7D3; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IDA:FlyBase.
DR   GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR   GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR   GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IGI:FlyBase.
DR   InterPro; IPR028816; Caprin.
DR   InterPro; IPR041637; Caprin-1_dimer.
DR   PANTHER; PTHR22922; PTHR22922; 1.
DR   Pfam; PF18293; Caprin-1_dimer; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Lipid droplet; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..961
FT                   /note="Caprin homolog"
FT                   /id="PRO_0000372862"
FT   REGION          60..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          678..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          109..188
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        373..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..768
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        775..806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        808..837
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        941..961
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656"
FT   MOD_RES         758
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         764
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         765
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         777
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         778
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         791
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         798
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         806
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656"
FT   HELIX           195..213
FT                   /evidence="ECO:0007829|PDB:6BK4"
FT   HELIX           217..225
FT                   /evidence="ECO:0007829|PDB:6BK4"
FT   HELIX           235..248
FT                   /evidence="ECO:0007829|PDB:6BK4"
FT   HELIX           261..276
FT                   /evidence="ECO:0007829|PDB:6BK4"
FT   STRAND          280..283
FT                   /evidence="ECO:0007829|PDB:6BK4"
FT   HELIX           288..301
FT                   /evidence="ECO:0007829|PDB:6BK4"
SQ   SEQUENCE   961 AA;  103590 MW;  4B6C49C630F0CED5 CRC64;
     MPSAANTATV TAAIATTVAA SASNTNNNSV SKEKRSSIIS LGGSVIPGTA VAAGAGVATT
     NGQSNSSAAA TADGSQTDLA SSNNNGNAAK SKANAVSAAA VVPEPYNPLK QLLVTIEHKI
     RNLEKRKTKL ESYRAIQSSG KELSGDQASA VAKYDAVLAN LEFARELAKH IQQQSKEAEK
     EQKKQARKDN LAKTIAETAK IREVLIIQNV LNCFNDDQVR SDFLNGENGA KKLENTELEL
     LEKFFIETQT RRPETADDVS FIATAQKSAE LFYSTINARP KSFGEVSFEK LRSLFQQIQD
     SGYLDKYYLV PLAENAVANS TDSGTGSGDG ESGDLLNDGS GELDAELPSE PSARNSLEEG
     LDKLHLGVQA ELDQHQSYQQ QQERPSHLLE PQHQRAPSLE HQQNSMVQQV STQVYQAAPQ
     AGGTTTPVHV LYAPAPPAQQ QPQQPPPHPH QLLSSPVNLQ ALQTGTAAPP AQQQQPHPTH
     FAPNVRAVEQ NYFKQPPQHP QGPGIQAPQT PQQQQFMQHS RPLAEVLGTG RFHFLQDSEL
     DNPEALAPPP PTNQGLVFEQ QPQQPNHVEE PTQAILTLTF TNQSFPSQQP QPQQQGPQQQ
     QQLFSPVLIH EQRQQPPQQQ PQPMLIMPRL PTQQPQQPAP QGIGMQAGDV TSGFSYENAV
     VSYEQQIQQQ LKQQQQQQQQ QQQNLQQLDE PSSVNSSSSV GAGGDVENNE WHARNNDTNA
     AATAALTNVL KGETTQATPP APPTKWSSEM NAMSSAASNG SSNTSHKQEW ATPRDHSTGG
     GNSGYADNNE SNNHWNNSQG DGRRNSGNYQ RRGGDRDNRD RDQGGRGDER RNGGDRGNYR
     SRQYGNSSNT NGRNSGNSSG VYFRNNESGN GGGNNYYQNG GGGGGTYNKE SRYESSGGGG
     GSYRGQRGGN QQRNVNGSYG GGRPMGDRGR GGAGNQGGGG GGYINRQNQS QRMPLGLENK
     N
 
 
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