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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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