CAPR2_DANRE
ID CAPR2_DANRE Reviewed; 914 AA.
AC Q5RJ80; Q6PFL5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Caprin-2;
DE AltName: Full=RNA granule protein 140;
GN Name=caprin2 {ECO:0000312|EMBL:AAH57503.1}; Synonyms=rng140;
GN ORFNames=si:ch211-11c20.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAI11565.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-914.
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH57503.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=18762581; DOI=10.1083/jcb.200803147;
RA Ding Y., Xi Y., Chen T., Wang J.Y., Tao D.L., Wu Z.L., Li Y.P., Li C.,
RA Zeng R., Li L.;
RT "Caprin-2 enhances canonical Wnt signaling through regulating LRP5/6
RT phosphorylation.";
RL J. Cell Biol. 182:865-872(2008).
RN [4] {ECO:0007744|PDB:4OUS}
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 780-914 IN COMPLEX WITH CALCIUM,
RP AND SUBUNIT.
RX PubMed=25331957; DOI=10.1074/jbc.m114.591636;
RA Miao H., Jia Y., Xie S., Wang X., Zhao J., Chu Y., Zhou Z., Shi Z.,
RA Song X., Li L.;
RT "Structural insights into the C1q domain of Caprin-2 in canonical Wnt
RT signaling.";
RL J. Biol. Chem. 289:34104-34113(2014).
CC -!- FUNCTION: Promotes phosphorylation of the Wnt coreceptor LRP6, leading
CC to increased activity of the canonical Wnt signaling pathway.
CC Facilitates constitutive LRP6 phosphorylation by CDK14/CCNY during G2/M
CC stage of the cell cycle, which may potentiate cells for Wnt signaling.
CC May regulate the transport and translation of mRNAs, modulating for
CC instance the expression of proteins involved in synaptic plasticity in
CC neurons. Involved in regulation of growth as erythroblasts shift from a
CC highly proliferative state towards their terminal phase of
CC differentiation. May be involved in apoptosis.
CC {ECO:0000250|UniProtKB:Q6IMN6}.
CC -!- SUBUNIT: Homotrimer; via C1q domain. {ECO:0000269|PubMed:25331957}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6IMN6}. Cell
CC membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IMN6}.
CC -!- DOMAIN: The C1q domain is essential for the function in Wnt signaling.
CC {ECO:0000250|UniProtKB:Q6IMN6}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown results in a dorsalized
CC phenotype, with enlargement of the telencephalon and reduction of the
CC tail at 24 hours post-fertilization. Expression of the dorsal marker
CC goosecoid is expanded, whereas expression of the ventral markers eve1
CC and tbx6 is reduced. In addition, expression of the telencephalon
CC marker opl and the midbrain/hindbrain boundary marker pax2.1 is
CC expanded posteriorly. {ECO:0000269|PubMed:18762581}.
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; BX001012; CAI11565.1; -; Genomic_DNA.
DR EMBL; BC057503; AAH57503.1; -; mRNA.
DR RefSeq; NP_001013291.1; NM_001013273.1.
DR PDB; 4OUS; X-ray; 1.05 A; A=780-914.
DR PDBsum; 4OUS; -.
DR AlphaFoldDB; Q5RJ80; -.
DR SMR; Q5RJ80; -.
DR STRING; 7955.ENSDARP00000040707; -.
DR PaxDb; Q5RJ80; -.
DR Ensembl; ENSDART00000040708; ENSDARP00000040707; ENSDARG00000020749.
DR GeneID; 407729; -.
DR KEGG; dre:407729; -.
DR CTD; 65981; -.
DR ZFIN; ZDB-GENE-040812-2; caprin2.
DR eggNOG; ENOG502QQ53; Eukaryota.
DR GeneTree; ENSGT00940000153438; -.
DR HOGENOM; CLU_009305_1_0_1; -.
DR InParanoid; Q5RJ80; -.
DR OMA; LNKDQMA; -.
DR OrthoDB; 155962at2759; -.
DR PhylomeDB; Q5RJ80; -.
DR TreeFam; TF329471; -.
DR SignaLink; Q5RJ80; -.
DR PRO; PR:Q5RJ80; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000020749; Expressed in cleaving embryo and 19 other tissues.
DR ExpressionAtlas; Q5RJ80; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:ZFIN.
DR GO; GO:2000055; P:positive regulation of Wnt signaling pathway involved in dorsal/ventral axis specification; IMP:BHF-UCL.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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; 2.
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 3D-structure; Calcium; Cell membrane; Cytoplasm; Differentiation;
KW Growth regulation; Membrane; Metal-binding; Protein synthesis inhibitor;
KW Reference proteome; RNA-binding.
FT CHAIN 1..914
FT /note="Caprin-2"
FT /id="PRO_0000302084"
FT DOMAIN 780..914
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 259..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 865
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 871
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:0000269|PubMed:25331957"
FT CONFLICT 726
FT /note="S -> N (in Ref. 2; AAH57503)"
FT /evidence="ECO:0000305"
FT STRAND 786..791
FT /evidence="ECO:0007829|PDB:4OUS"
FT STRAND 798..803
FT /evidence="ECO:0007829|PDB:4OUS"
FT STRAND 808..813
FT /evidence="ECO:0007829|PDB:4OUS"
FT TURN 819..822
FT /evidence="ECO:0007829|PDB:4OUS"
FT STRAND 823..825
FT /evidence="ECO:0007829|PDB:4OUS"
FT STRAND 827..840
FT /evidence="ECO:0007829|PDB:4OUS"
FT STRAND 842..845
FT /evidence="ECO:0007829|PDB:4OUS"
FT STRAND 847..853
FT /evidence="ECO:0007829|PDB:4OUS"
FT STRAND 856..863
FT /evidence="ECO:0007829|PDB:4OUS"
FT STRAND 872..881
FT /evidence="ECO:0007829|PDB:4OUS"
FT STRAND 886..894
FT /evidence="ECO:0007829|PDB:4OUS"
FT STRAND 904..913
FT /evidence="ECO:0007829|PDB:4OUS"
SQ SEQUENCE 914 AA; 101570 MW; B84AEF8EFE4B780F CRC64;
MRKTETMVQL SPSRTLETLT PSELTVEKDD GQGSPKPESP RMLSALQLAL SSTTVYCGYE
KYIEDGLICL KHKIRNIEKK KLKLERYSDK LKKGEKLNED QLEAVGKYDE VVHNLKFAKE
LQKTIGSLTQ DLLKAQRKAV RQEKQMKTDE EKSRLSLMLQ VQYVLHSLQR EDVRKNFCNT
RQYSCYMSTQ DMEGLMDLAS LVGCKRDYSI SLEDQMRRAA IVYWELLEGN EKPVAGSTYK
HMKEKLLRLV DSGFFDNIPL PKSDSQEKTE TIKPDSQSRP SGLTTLVKLS SNEVPSKEFL
NRRYMPETDE RRRGETASPR NWKEDFLAMK EREPPDSWEM EELADPPASS QSPIQKPWKG
AAGLIPKTVD IVKRSTTDPK EKRQRKKAEQ DSKSMPVAVE VFSSPSPLPK DPVQRRQQLE
TLMDQISGSF SFMQESLLDG ESSPVNTQTK RCRPSPGSST PIVQRELTKS PSDILPSSQR
STPLRILLSG EGKGCLSNGD RSINGSDLEL HSEDKPRKQA EGFNSPPLYR RGSSISVSLE
NQSTVQAGRQ MLCNGVSSSG SAQTFSTPPS RRSISAENPF HNIHSVFNVI GESSGMKADE
SGFSESIHRS FTSAKTSSVT TASTQTPPEL NPPEEDLQIE GQYPLECAVS AGGPVFSSSH
SRVGQSCYSR GAVRGGYDAY RVNVRSPGGS FMSQTHREPA SALYMARENG YQQNFKRGAG
TATQRSSAGW SDSSQVSSPD RDGAYPLDSG LSDTLSIPAM EVPMNPQGPH TLMPVHVYPL
TQLRVAFSAA RTANFAPGTL DQPIAFDLLH TNLGDMFDTG SGRFTCPATG AYVFIFHILK
LAISVPLYIN LMRNEEVMVS AYANDGAPDH ETASNHAVLQ LFQGDQVWLR LHRGAIYGSS
WKYSTFSGFL LYQD
