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Caprin-1 (Cytoplasmic activation- and proliferation-associated protein 1) (GPI-anchored membrane protein 1) (GPI-anchored protein p137) (GPI-p137) (p137GPI) (Membrane component chromosome 11 surface marker 1) (RNA granule protein 105)

 CAPR1_MOUSE             Reviewed;         707 AA.
Q60865; Q60758; Q61620; Q6IMN3; Q7TT26;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
08-APR-2008, sequence version 2.
28-MAR-2018, entry version 137.
RecName: Full=Caprin-1;
AltName: Full=Cytoplasmic activation- and proliferation-associated protein 1;
AltName: Full=GPI-anchored membrane protein 1;
AltName: Full=GPI-anchored protein p137;
Short=GPI-p137;
Short=p137GPI;
AltName: Full=Membrane component chromosome 11 surface marker 1;
AltName: Full=RNA granule protein 105;
Name=Caprin1; Synonyms=Gpiap, Gpiap1, Gpip137, M11s1, Rng105;
ORFNames=G5E5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J-AW-J/AW-J X CBA/CAGNLE-A/A; TISSUE=Cerebellum;
Hodes M.E.;
"Novel cDNA clone, G5E5, isolated from a mouse neonatal cerebellar
library is expressed in a variety of adult and neonatal tissues.";
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
Shiina N., Tokunaga M.;
"RNA granule protein RNG105 deficiency impairs the dendritic
localization of Na+/K+ ATPase subunit isoforms and synapse
formation.";
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-362.
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=8786113; DOI=10.1006/geno.1996.0099;
Gessler M., Klant B., Tsaoussidou S., Ellis J.A., Luzio J.P.;
"The gene encoding the GPI-anchored membrane protein p137GPI (M11S1)
maps to human chromosome 11p13 and is highly conserved in the mouse.";
Genomics 32:169-170(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 402-707.
STRAIN=C57BL/6J-AW-J/AW-J X CBA/CAGNLE-A/A; TISSUE=Cerebellum;
Hodes M.E.;
"Novel cDNA clone, G5E5, maps to chromosome 16 and is expressed in a
variety of adult and neonatal tissues.";
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
[7]
IDENTIFICATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, PHOSPHORYLATION, AND MULTIMERIZATION.
PubMed=14764709; DOI=10.4049/jimmunol.172.4.2389;
Grill B., Wilson G.M., Zhang K.-X., Wang B., Doyonnas R., Quadroni M.,
Schrader J.W.;
"Activation/division of lymphocytes results in increased levels of
cytoplasmic activation/proliferation-associated protein-1: prototype
of a new family of proteins.";
J. Immunol. 172:2389-2400(2004).
[8]
INTERACTION WITH G3BP1, AND SUBCELLULAR LOCATION.
PubMed=17210633; DOI=10.1128/MCB.02300-06;
Solomon S., Xu Y., Wang B., David M.D., Schubert P., Kennedy D.,
Schrader J.W.;
"Distinct structural features of caprin-1 mediate its interaction with
G3BP-1 and its induction of phosphorylation of eukaryotic translation
initiation factor 2alpha, entry to cytoplasmic stress granules, and
selective interaction with a subset of mRNAs.";
Mol. Cell. Biol. 27:2324-2342(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=20516077; DOI=10.1074/jbc.M110.108944;
Shiina N., Tokunaga M.;
"RNA granule protein 140 (RNG140), a paralog of RNG105 localized to
distinct RNA granules in neuronal dendrites in the adult vertebrate
brain.";
J. Biol. Chem. 285:24260-24269(2010).
[11]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-163; ARG-631; ARG-638 AND
ARG-696, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: May regulate the transport and translation of mRNAs of
proteins involved in synaptic plasticity in neurons and cell
proliferation and migration in multiple cell types
(PubMed:20516077). Binds directly and selectively to MYC and CCND2
RNAs. In neuronal cells, directly binds to several mRNAs
associated with RNA granules, including BDNF, CAMK2A, CREB1, MAP2,
NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not to rRNAs
(By similarity). {ECO:0000250|UniProtKB:Q14444,
ECO:0000269|PubMed:20516077}.
-!- SUBUNIT: May form homomultimers (PubMed:14764709). Interacts with
G3BP1; interaction is direct and takes place in cytoplasmic RNA
granules. Interacts with PQBP1 (By similarity).
{ECO:0000250|UniProtKB:Q14444, ECO:0000269|PubMed:14764709}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection,
dendrite. Note=Associated with RNA granules. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highest expression in thymus, spleen and brain
(at protein level). Lower levels in kidney, muscle and liver (at
protein level). {ECO:0000269|PubMed:14764709,
ECO:0000269|PubMed:20516077}.
-!- DEVELOPMENTAL STAGE: Up-regulated when resting T- or B-lymphocytes
or hemopoietic progenitors are activated. Down-regulated when a
monocytic leukemia cell line, M1, is induced to differentiate.
Expressed in brain at E17.5 (at protein level).
{ECO:0000269|PubMed:14764709, ECO:0000269|PubMed:20516077}.
-!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent
manner. {ECO:0000250}.
-!- SIMILARITY: Belongs to the caprin family. {ECO:0000305}.
-!- CAUTION: Was originally thought to be a GPI-anchored membrane
protein. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA68561.1; Type=Frameshift; Positions=566; Evidence={ECO:0000305};
Sequence=AAA82599.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA61750.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U27838; AAA82599.1; ALT_INIT; mRNA.
EMBL; AB373955; BAF96513.1; -; mRNA.
EMBL; BX537331; CAM21440.1; -; Genomic_DNA.
EMBL; BC052427; AAH52427.2; -; mRNA.
EMBL; X89571; CAA61750.1; ALT_SEQ; Genomic_DNA.
EMBL; U18773; AAA68561.1; ALT_FRAME; mRNA.
EMBL; BK001105; DAA01122.1; -; mRNA.
CCDS; CCDS16481.1; -.
PIR; S58008; S58008.
RefSeq; NP_001104759.1; NM_001111289.1.
RefSeq; NP_001104760.1; NM_001111290.1.
RefSeq; NP_001104761.1; NM_001111291.1.
RefSeq; NP_001104762.1; NM_001111292.1.
RefSeq; NP_058019.2; NM_016739.3.
UniGene; Mm.427589; -.
UniGene; Mm.488635; -.
ProteinModelPortal; Q60865; -.
SMR; Q60865; -.
BioGrid; 207501; 9.
IntAct; Q60865; 16.
MINT; Q60865; -.
STRING; 10090.ENSMUSP00000028607; -.
iPTMnet; Q60865; -.
PhosphoSitePlus; Q60865; -.
SwissPalm; Q60865; -.
EPD; Q60865; -.
MaxQB; Q60865; -.
PaxDb; Q60865; -.
PeptideAtlas; Q60865; -.
PRIDE; Q60865; -.
Ensembl; ENSMUST00000028607; ENSMUSP00000028607; ENSMUSG00000027184.
Ensembl; ENSMUST00000111147; ENSMUSP00000106777; ENSMUSG00000027184.
GeneID; 53872; -.
KEGG; mmu:53872; -.
UCSC; uc008ljb.2; mouse.
CTD; 4076; -.
MGI; MGI:1858234; Caprin1.
eggNOG; ENOG410IEA8; Eukaryota.
eggNOG; ENOG4110M5Q; LUCA.
GeneTree; ENSGT00760000119052; -.
HOGENOM; HOG000290177; -.
HOVERGEN; HBG051781; -.
InParanoid; Q60865; -.
KO; K18743; -.
OMA; VEQNYFK; -.
OrthoDB; EOG091G0575; -.
PhylomeDB; Q60865; -.
TreeFam; TF329471; -.
ChiTaRS; Caprin1; mouse.
PRO; PR:Q60865; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027184; -.
CleanEx; MM_CAPRIN1; -.
ExpressionAtlas; Q60865; baseline and differential.
Genevisible; Q60865; MM.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:MGI.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:UniProtKB.
InterPro; IPR028816; Caprin.
InterPro; IPR022070; Caprin-1_C.
PANTHER; PTHR22922; PTHR22922; 1.
Pfam; PF12287; Caprin-1_C; 1.
1: Evidence at protein level;
Acetylation; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Differentiation; Glycoprotein; Methylation; Phosphoprotein;
Protein synthesis inhibitor; Reference proteome; RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q14444}.
CHAIN 2 707 Caprin-1.
/FTId=PRO_0000087550.
REGION 358 379 G3BP1-binding. {ECO:0000250}.
COILED 58 92 {ECO:0000255}.
COILED 123 151 {ECO:0000255}.
MOD_RES 2 2 N-acetylproline.
{ECO:0000250|UniProtKB:Q14444}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:Q14444}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000250|UniProtKB:Q14444}.
MOD_RES 163 163 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000250|UniProtKB:Q14444}.
MOD_RES 341 341 Phosphoserine.
{ECO:0000250|UniProtKB:Q14444}.
MOD_RES 624 624 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q14444}.
MOD_RES 631 631 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 638 638 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 696 696 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 696 696 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q14444}.
CONFLICT 24 24 S -> F (in Ref. 1; AAA82599).
{ECO:0000305}.
CONFLICT 45 45 G -> D (in Ref. 1; AAA82599).
{ECO:0000305}.
CONFLICT 105 105 E -> G (in Ref. 1; AAA82599).
{ECO:0000305}.
CONFLICT 266 266 V -> A (in Ref. 1; AAA82599).
{ECO:0000305}.
CONFLICT 338 338 E -> K (in Ref. 1; AAA82599).
{ECO:0000305}.
CONFLICT 402 404 PQL -> ESV (in Ref. 6; AAA68561).
{ECO:0000305}.
CONFLICT 403 404 QL -> HV (in Ref. 1; AAA82599).
{ECO:0000305}.
CONFLICT 603 603 Missing (in Ref. 4; AAH52427).
{ECO:0000305}.
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


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