CAPR2_MOUSE
ID CAPR2_MOUSE Reviewed; 1031 AA.
AC Q05A80; Q58E31; Q6ZPG7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Caprin-2;
DE AltName: Full=C1q domain-containing protein 1;
DE AltName: Full=Cytoplasmic activation/proliferation-associated protein 2;
DE AltName: Full=RNA granule protein 140;
GN Name=Caprin2 {ECO:0000312|MGI:MGI:2448541};
GN Synonyms=C1qdc1 {ECO:0000312|MGI:MGI:2448541},
GN Kiaa1873 {ECO:0000312|EMBL:BAC98270.1}, Rng140;
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] {ECO:0000305, ECO:0000312|EMBL:BAC98270.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail {ECO:0000312|EMBL:BAC98270.1};
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAI25376.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:AAI25376.1}, and
RC Mammary tumor {ECO:0000312|EMBL:AAH92093.1};
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852 AND SER-853, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [4]
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).
CC -!- FUNCTION: Promotes phosphorylation of the Wnt coreceptor LRP6, leading
CC to increased activity of the canonical Wnt signaling pathway (By
CC similarity). Facilitates constitutive LRP6 phosphorylation by
CC CDK14/CCNY during G2/M stage of the cell cycle, which may potentiate
CC cells for Wnt signaling (By similarity). May regulate the transport and
CC translation of mRNAs, modulating for instance the expression of
CC proteins involved in synaptic plasticity in neurons (PubMed:20516077).
CC Involved in regulation of growth as erythroblasts shift from a highly
CC proliferative state towards their terminal phase of differentiation (By
CC similarity). May be involved in apoptosis (By similarity).
CC {ECO:0000250|UniProtKB:Q6IMN6, ECO:0000269|PubMed:20516077}.
CC -!- SUBUNIT: Homotrimer; via C1q domain. Found in a complex with LRP6, CCNY
CC and CDK14 during G2/M stage; CAPRIN2 functions as a scaffold for the
CC complex by binding to CCNY via its N terminus and to CDK14 via its C
CC terminus. Interacts with LRP5. Interacts with LRP6.
CC {ECO:0000250|UniProtKB:Q6IMN6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6IMN6}. Cell
CC membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IMN6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15489334};
CC IsoId=Q05A80-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:14621295};
CC IsoId=Q05A80-2; Sequence=VSP_052540;
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain (at protein level).
CC {ECO:0000269|PubMed:20516077}.
CC -!- DEVELOPMENTAL STAGE: Detected at 17.5 dpc in brain (at protein level).
CC {ECO:0000269|PubMed:20516077}.
CC -!- DOMAIN: The C1q domain is essential for the function in Wnt signaling.
CC {ECO:0000250|UniProtKB:Q6IMN6}.
CC -!- SIMILARITY: Belongs to the caprin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98270.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129460; BAC98270.1; ALT_INIT; mRNA.
DR EMBL; BC092093; AAH92093.1; -; mRNA.
DR EMBL; BC125373; AAI25374.1; -; mRNA.
DR EMBL; BC125375; AAI25376.1; -; mRNA.
DR CCDS; CCDS39720.1; -. [Q05A80-1]
DR RefSeq; NP_001288280.1; NM_001301351.1.
DR RefSeq; NP_853519.2; NM_181541.4. [Q05A80-1]
DR RefSeq; XP_006507102.1; XM_006507039.3. [Q05A80-1]
DR RefSeq; XP_006507105.1; XM_006507042.3. [Q05A80-2]
DR RefSeq; XP_017177051.1; XM_017321562.1.
DR AlphaFoldDB; Q05A80; -.
DR SMR; Q05A80; -.
DR BioGRID; 231272; 2.
DR STRING; 10090.ENSMUSP00000107195; -.
DR iPTMnet; Q05A80; -.
DR PhosphoSitePlus; Q05A80; -.
DR MaxQB; Q05A80; -.
DR PaxDb; Q05A80; -.
DR PRIDE; Q05A80; -.
DR ProteomicsDB; 273832; -. [Q05A80-1]
DR ProteomicsDB; 273833; -. [Q05A80-2]
DR Antibodypedia; 42424; 99 antibodies from 19 providers.
DR Ensembl; ENSMUST00000072324; ENSMUSP00000072165; ENSMUSG00000030309. [Q05A80-2]
DR Ensembl; ENSMUST00000111569; ENSMUSP00000107195; ENSMUSG00000030309. [Q05A80-1]
DR GeneID; 232560; -.
DR KEGG; mmu:232560; -.
DR UCSC; uc009eto.2; mouse. [Q05A80-2]
DR UCSC; uc009etp.2; mouse. [Q05A80-1]
DR CTD; 65981; -.
DR MGI; MGI:2448541; Caprin2.
DR VEuPathDB; HostDB:ENSMUSG00000030309; -.
DR eggNOG; ENOG502QQ53; Eukaryota.
DR GeneTree; ENSGT00940000153438; -.
DR HOGENOM; CLU_009305_0_0_1; -.
DR InParanoid; Q05A80; -.
DR OMA; LNKDQMA; -.
DR PhylomeDB; Q05A80; -.
DR TreeFam; TF329471; -.
DR BioGRID-ORCS; 232560; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Caprin2; mouse.
DR PRO; PR:Q05A80; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q05A80; protein.
DR Bgee; ENSMUSG00000030309; Expressed in lens of camera-type eye and 241 other tissues.
DR ExpressionAtlas; Q05A80; baseline and differential.
DR Genevisible; Q05A80; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
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 GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR028816; Caprin.
DR InterPro; IPR022070; Caprin-1_C.
DR InterPro; IPR041637; Caprin-1_dimer.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR22922; PTHR22922; 1.
DR Pfam; PF00386; C1q; 1.
DR Pfam; PF12287; Caprin-1_C; 1.
DR Pfam; PF18293; Caprin-1_dimer; 1.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cytoplasm; Differentiation;
KW Growth regulation; Membrane; Metal-binding; Phosphoprotein;
KW Protein synthesis inhibitor; Reference proteome; RNA-binding.
FT CHAIN 1..1031
FT /note="Caprin-2"
FT /id="PRO_0000302083"
FT DOMAIN 897..1031
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 982
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:Q6IMN6"
FT BINDING 988
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:Q6IMN6"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 284..502
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_052540"
FT CONFLICT 843
FT /note="Missing (in Ref. 1; BAC98270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1031 AA; 114491 MW; DA2A62E64372F6A6 CRC64;
MKSAKSQVNQ DQQGENQRAL SPLQSTLSSA ASPSQAYETY IDNGLICLKH KIRNIEKKKL
KLEDYKDRLK NGEQLNPDQL EAVEKYEEVL HNLEFAKELQ KTFSALSQDL LKAQKKAQRR
EHMLKLETEK KKLRTMLQIQ YVLQNLTQEH VQKDFKGGLN GAMYLPSKEL DYLIKFSKLT
CPERNESLSV EDQMEQSSLY FWDLLEGSEK TVVGTTYKHV KDLLSKLLHS GYFESVPVLR
NSKEKAEEVL MQSEMKKQLL KSESIKESES LTELVQPEIQ PQEFLNRRYM TEVKFSRKQE
NVEQSWEADY ARKPSLLKCW NTLPEPDGQE KKKESLESWK SSLKTQEVSK PVVSLVQGKL
RPTLQEEQKQ QVPITPVSQW KPESPKSKVG SPQEEQNVQE TPKPWVVQSQ KEQDPKKLPP
GSWAVSVQSE QSGSRSWTTP VCREQASVQP GTPVSWENNA ENQKHSLVPQ SQISLKSWGA
ASAGLLPNGQ VLTRKLNVEP KDVPKPLPQP IDSSSALPKD PVLRKEKLQD LMSQIQGTYN
FMQESVLDFD KPSSAIPSSQ PPSACPVSTV SAEQNLSNQS DFLQEPSQAS SPVTCSSNAC
LVTTDQASSG SETEFTTSET PEMVVSPCKP KPASALASPN PPLSKSFQLP PASGSSEAIS
TAPFQAMQTV FNVNAPLPPR KEQEMKEPPY SSGYNQNFTS SSTQTVSQCQ LPAVHIDQTT
QPPETGAGYH PDGTVQVSNG SLAFYPAPTS MFPRPAQPFI SSRGTLRGCS HGGRLLMSSY
QSPGGYKGFD SYRGLPSVSS GNYSQLQLQA REYSGTAYSQ RDNFQQCYKR SGTSSGLQAN
SRAGWSDSSQ VSSPERDSET FNSGDSGLGD SRSMTPVDVP VTSPAAAILP VHIYPLPQQM
RVAFSAARTS NLAPGTLDQP IVFDLLLNNL GETFDLQLGR FNCPVNGTYV FIFHMLKLAV
NVPLYVNLMK NEEVLVSAYA NDGAPDHETA SNHAVLQLLQ GDQIWLRLHR GAIYGSSWKY
STFSGYLLYQ D
