CAPR1_MOUSE
ID CAPR1_MOUSE Reviewed; 707 AA.
AC Q60865; Q60758; Q61620; Q6IMN3; Q7TT26;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Caprin-1;
DE AltName: Full=Cytoplasmic activation- and proliferation-associated protein 1;
DE AltName: Full=GPI-anchored membrane protein 1;
DE AltName: Full=GPI-anchored protein p137;
DE Short=GPI-p137;
DE Short=p137GPI;
DE AltName: Full=Membrane component chromosome 11 surface marker 1;
DE AltName: Full=RNA granule protein 105;
GN Name=Caprin1; Synonyms=Gpiap, Gpiap1, Gpip137, M11s1, Rng105;
GN ORFNames=G5E5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J-AW-J/AW-J X CBA/CAGNLE-A/A; TISSUE=Cerebellum;
RA Hodes M.E.;
RT "Novel cDNA clone, G5E5, isolated from a mouse neonatal cerebellar library
RT is expressed in a variety of adult and neonatal tissues.";
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Shiina N., Tokunaga M.;
RT "RNA granule protein RNG105 deficiency impairs the dendritic localization
RT of Na+/K+ ATPase subunit isoforms and synapse formation.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-362.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=8786113; DOI=10.1006/geno.1996.0099;
RA Gessler M., Klant B., Tsaoussidou S., Ellis J.A., Luzio J.P.;
RT "The gene encoding the GPI-anchored membrane protein p137GPI (M11S1) maps
RT to human chromosome 11p13 and is highly conserved in the mouse.";
RL Genomics 32:169-170(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 402-707.
RC STRAIN=C57BL/6J-AW-J/AW-J X CBA/CAGNLE-A/A; TISSUE=Cerebellum;
RA Hodes M.E.;
RT "Novel cDNA clone, G5E5, maps to chromosome 16 and is expressed in a
RT variety of adult and neonatal tissues.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, PHOSPHORYLATION, AND MULTIMERIZATION.
RX PubMed=14764709; DOI=10.4049/jimmunol.172.4.2389;
RA Grill B., Wilson G.M., Zhang K.-X., Wang B., Doyonnas R., Quadroni M.,
RA Schrader J.W.;
RT "Activation/division of lymphocytes results in increased levels of
RT cytoplasmic activation/proliferation-associated protein-1: prototype of a
RT new family of proteins.";
RL J. Immunol. 172:2389-2400(2004).
RN [8]
RP INTERACTION WITH G3BP1, AND SUBCELLULAR LOCATION.
RX PubMed=17210633; DOI=10.1128/mcb.02300-06;
RA Solomon S., Xu Y., Wang B., David M.D., Schubert P., Kennedy D.,
RA Schrader J.W.;
RT "Distinct structural features of caprin-1 mediate its interaction with
RT G3BP-1 and its induction of phosphorylation of eukaryotic translation
RT initiation factor 2alpha, entry to cytoplasmic stress granules, and
RT selective interaction with a subset of mRNAs.";
RL Mol. Cell. Biol. 27:2324-2342(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20516077; DOI=10.1074/jbc.m110.108944;
RA Shiina N., Tokunaga M.;
RT "RNA granule protein 140 (RNG140), a paralog of RNG105 localized to
RT distinct RNA granules in neuronal dendrites in the adult vertebrate
RT brain.";
RL J. Biol. Chem. 285:24260-24269(2010).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-163; ARG-631; ARG-638 AND
RP ARG-696, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May regulate the transport and translation of mRNAs of
CC proteins involved in synaptic plasticity in neurons and cell
CC proliferation and migration in multiple cell types (PubMed:20516077).
CC Binds directly and selectively to MYC and CCND2 RNAs. In neuronal
CC cells, directly binds to several mRNAs associated with RNA granules,
CC including BDNF, CAMK2A, CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1
CC and KPNB1 mRNAs, but not to rRNAs (By similarity).
CC {ECO:0000250|UniProtKB:Q14444, ECO:0000269|PubMed:20516077}.
CC -!- SUBUNIT: May form homomultimers (PubMed:14764709). Interacts with
CC G3BP1; interaction is direct and takes place in cytoplasmic RNA
CC granules (PubMed:17210633). Interacts with PQBP1 (By similarity).
CC Interacts with DDX3X (By similarity). {ECO:0000250|UniProtKB:Q14444,
CC ECO:0000269|PubMed:14764709, ECO:0000269|PubMed:17210633}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14764709,
CC ECO:0000269|PubMed:17210633}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q5M9G3}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q14444}. Note=Associated with RNA granules
CC (PubMed:17210633). At the leading edge of migrating fibroblasts,
CC colocalizes with DDX3X (By similarity). {ECO:0000250|UniProtKB:Q14444,
CC ECO:0000269|PubMed:17210633}.
CC -!- TISSUE SPECIFICITY: Highest expression in thymus, spleen and brain (at
CC protein level). Lower levels in kidney, muscle and liver (at protein
CC level). {ECO:0000269|PubMed:14764709, ECO:0000269|PubMed:20516077}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated when resting T- or B-lymphocytes or
CC hemopoietic progenitors are activated. Down-regulated when a monocytic
CC leukemia cell line, M1, is induced to differentiate. Expressed in brain
CC at 17.5 dpc (at protein level). {ECO:0000269|PubMed:14764709,
CC ECO:0000269|PubMed:20516077}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the caprin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a GPI-anchored membrane protein.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA68561.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA82599.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA61750.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U27838; AAA82599.1; ALT_INIT; mRNA.
DR EMBL; AB373955; BAF96513.1; -; mRNA.
DR EMBL; BX537331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052427; AAH52427.2; -; mRNA.
DR EMBL; X89571; CAA61750.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U18773; AAA68561.1; ALT_FRAME; mRNA.
DR EMBL; BK001105; DAA01122.1; -; mRNA.
DR CCDS; CCDS16481.1; -.
DR PIR; S58008; S58008.
DR RefSeq; NP_001104759.1; NM_001111289.1.
DR RefSeq; NP_001104760.1; NM_001111290.1.
DR RefSeq; NP_001104761.1; NM_001111291.1.
DR RefSeq; NP_001104762.1; NM_001111292.1.
DR RefSeq; NP_058019.2; NM_016739.3.
DR AlphaFoldDB; Q60865; -.
DR SMR; Q60865; -.
DR BioGRID; 207501; 24.
DR IntAct; Q60865; 13.
DR MINT; Q60865; -.
DR STRING; 10090.ENSMUSP00000028607; -.
DR iPTMnet; Q60865; -.
DR PhosphoSitePlus; Q60865; -.
DR SwissPalm; Q60865; -.
DR EPD; Q60865; -.
DR jPOST; Q60865; -.
DR MaxQB; Q60865; -.
DR PaxDb; Q60865; -.
DR PeptideAtlas; Q60865; -.
DR PRIDE; Q60865; -.
DR ProteomicsDB; 281772; -.
DR Antibodypedia; 12960; 334 antibodies from 32 providers.
DR DNASU; 53872; -.
DR Ensembl; ENSMUST00000028607; ENSMUSP00000028607; ENSMUSG00000027184.
DR Ensembl; ENSMUST00000111147; ENSMUSP00000106777; ENSMUSG00000027184.
DR GeneID; 53872; -.
DR KEGG; mmu:53872; -.
DR UCSC; uc008ljb.2; mouse.
DR CTD; 4076; -.
DR MGI; MGI:1858234; Caprin1.
DR VEuPathDB; HostDB:ENSMUSG00000027184; -.
DR eggNOG; ENOG502QUGC; Eukaryota.
DR GeneTree; ENSGT00940000153438; -.
DR HOGENOM; CLU_024060_0_0_1; -.
DR InParanoid; Q60865; -.
DR OMA; VEQNYFK; -.
DR OrthoDB; 382856at2759; -.
DR PhylomeDB; Q60865; -.
DR TreeFam; TF329471; -.
DR BioGRID-ORCS; 53872; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Caprin1; mouse.
DR PRO; PR:Q60865; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q60865; protein.
DR Bgee; ENSMUSG00000027184; Expressed in undifferentiated genital tubercle and 259 other tissues.
DR ExpressionAtlas; Q60865; baseline and differential.
DR Genevisible; Q60865; MM.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:UniProtKB.
DR InterPro; IPR028816; Caprin.
DR InterPro; IPR022070; Caprin-1_C.
DR InterPro; IPR041637; Caprin-1_dimer.
DR PANTHER; PTHR22922; PTHR22922; 1.
DR Pfam; PF12287; Caprin-1_C; 1.
DR Pfam; PF18293; Caprin-1_dimer; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Coiled coil; Cytoplasm; Differentiation;
KW Glycoprotein; Methylation; Phosphoprotein; Protein synthesis inhibitor;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT CHAIN 2..707
FT /note="Caprin-1"
FT /id="PRO_0000087550"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..379
FT /note="G3BP1-binding"
FT /evidence="ECO:0000250"
FT REGION 412..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 58..92
FT /evidence="ECO:0000255"
FT COILED 123..151
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 163
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 624
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 631
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 638
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 696
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 696
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT CONFLICT 24
FT /note="S -> F (in Ref. 1; AAA82599)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="G -> D (in Ref. 1; AAA82599)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="E -> G (in Ref. 1; AAA82599)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="V -> A (in Ref. 1; AAA82599)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="E -> K (in Ref. 1; AAA82599)"
FT /evidence="ECO:0000305"
FT CONFLICT 402..404
FT /note="PQL -> ESV (in Ref. 6; AAA68561)"
FT /evidence="ECO:0000305"
FT CONFLICT 403..404
FT /note="QL -> HV (in Ref. 1; AAA82599)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="Missing (in Ref. 4; AAH52427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 78169 MW; AF8812DE013A9081 CRC64;
MPSATSHSGS GSKSSGPPPP SGSSGSEAAA GAAAPASQHP ATGTGAVQTE AMKQILGVID
KKLRNLEKKK GKLDDYQERM NKGERLNQDQ LDAVSKYQEV TNNLEFAKEL QRSFMALSQD
IQKTIKKTAR REQLMREEAE QKRLKTVLEL QYVLDKLGDD DVRTDLKQGL SGVPILSEEE
LSLLDEFYKL VDPERDMSLR LNEQYEHASI HLWDLLEGKE KPVCGTTYKA LKEIVERVFQ
SNYFDSTHNH QNGLCEEEEA ASAPTVEDQV AEAEPEPAEE YTEQSEVEST EYVNRQFMAE
TQFSSGEKEQ VDEWTVETVE VVNSLQQQPQ AASPSVPEPH SLTPVAQSDP LVRRQRVQDL
MAQMQGPYNF IQDSMLDFEN QTLDPAIVSA QPMNPTQNMD MPQLVCPQVH SESRLAQSNQ
VPVQPEATQV PLVSSTSEGY TASQPLYQPS HATEQRPQKE PMDQIQATIS LNTDQTTASS
SLPAASQPQV FQAGTSKPLH SSGINVNAAP FQSMQTVFNM NAPVPPANEP ETLKQQSQYQ
ATYNQSFSSQ PHQVEQTELQ QDQLQTVVGT YHGSQDQPHQ VPGNHQQPPQ QNTGFPRSSQ
PYYNSRGVSR GGSRGARGLM NGYRGPANGF RGGYDGYRPS FSNTPNSGYS QSQFTAPRDY
SGYQRDGYQQ NFKRGSGQSG PRGAPRGRGG PPRPNRGMPQ MNTQQVN
