CAPR2_HUMAN
ID CAPR2_HUMAN Reviewed; 1127 AA.
AC Q6IMN6; E4NKG2; Q149P6; Q149P7; Q6IMN5; Q7Z371; Q8TE70; Q8TE71; Q96RN6;
AC Q9H667; Q9HAL4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
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=Gastric cancer multidrug resistance-associated protein;
DE AltName: Full=Protein EEG-1;
DE AltName: Full=RNA granule protein 140;
GN Name=CAPRIN2 {ECO:0000312|EMBL:AAI17673.1};
GN Synonyms=C1QDC1, EEG1 {ECO:0000312|EMBL:AAL71549.1}, KIAA1873, RNG140;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL71549.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Erythroblast {ECO:0000312|EMBL:AAL71549.1};
RX PubMed=14593112; DOI=10.1074/jbc.m305634200;
RA Aerbajinai W., Lee Y.T., Wojda U., Barr V.A., Miller J.L.;
RT "Cloning and characterization of a gene expressed during terminal
RT differentiation that encodes a novel inhibitor of growth.";
RL J. Biol. Chem. 279:1916-1921(2004).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAI17673.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 10), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 844-1127 (ISOFORMS 1/2/4).
RC TISSUE=Brain {ECO:0000312|EMBL:AAH66295.1}, and Uterus;
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAB13830.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-776 (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-776 (ISOFORM 4), AND VARIANT VAL-519.
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB13830.1}, and
RC Small intestine {ECO:0000312|EMBL:BAB15398.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAK83153.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 319-1127 (ISOFORM 6).
RA Shi Y.-Q., Zhai H.-H., Han Y., Wang X., Wu H.-P., Fan D.-M.;
RT "Isolation and functional characterization of a novel gene associated with
RT gastric cancer multidrug resistance.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 766-1127 (ISOFORM 7).
RC TISSUE=Cerebellum;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7] {ECO:0000305, ECO:0000312|EMBL:DAA01119.1}
RP IDENTIFICATION (ISOFORM 9).
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 FUNCTION, INTERACTION WITH LRP5 AND LRP6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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 [9]
RP IDENTIFICATION.
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH LRP6; CCNY AND CDK14, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27821587; DOI=10.1074/jbc.m116.744607;
RA Wang X., Jia Y., Fei C., Song X., Li L.;
RT "Caprin-2 positively regulates CDK14/Cyclin Y-mediated LRP5/6 constitutive
RT phosphorylation.";
RL J. Biol. Chem. 291:26427-26434(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 996-1127 IN COMPLEX WITH CALCIUM,
RP SUBUNIT, INTERACTION WITH LRP6, AND MUTAGENESIS OF ILE-1048; ASP-1078;
RP GLU-1084; ILE-1091; TRP-1114 AND TYR-1122.
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 (PubMed:18762581). Facilitates constitutive LRP6 phosphorylation by
CC CDK14/CCNY during G2/M stage of the cell cycle, which may potentiate
CC cells for Wnt signaling (PubMed:27821587). May regulate the transport
CC and translation of mRNAs, modulating for instance the expression of
CC proteins involved in synaptic plasticity in neurons (By similarity).
CC Involved in regulation of growth as erythroblasts shift from a highly
CC proliferative state towards their terminal phase of differentiation
CC (PubMed:14593112). May be involved in apoptosis (PubMed:14593112).
CC {ECO:0000250|UniProtKB:Q05A80, ECO:0000269|PubMed:14593112,
CC ECO:0000269|PubMed:18762581, ECO:0000269|PubMed:27821587}.
CC -!- SUBUNIT: Homotrimer; via C1q domain (PubMed:25331957). Found in a
CC complex with LRP6, CCNY and CDK14 during G2/M stage; CAPRIN2 functions
CC as a scaffold for the complex by binding to CCNY via its N terminus and
CC to CDK14 via its C terminus (PubMed:27821587). Interacts with LRP5
CC (PubMed:18762581). Interacts with LRP6 (PubMed:18762581,
CC PubMed:25331957). {ECO:0000269|PubMed:18762581,
CC ECO:0000269|PubMed:25331957}.
CC -!- INTERACTION:
CC Q6IMN6; O75197: LRP5; NbExp=3; IntAct=EBI-6918449, EBI-2466421;
CC Q6IMN6; P50542: PEX5; NbExp=3; IntAct=EBI-6918449, EBI-597835;
CC Q6IMN6-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12422830, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion. Cytoplasm.
CC Note=Expressed throughout the cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion. Note=Colocalizes with
CC aggregated mitochondria.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:27821587};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1 {ECO:0000269|PubMed:16541075};
CC IsoId=Q6IMN6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:14593112}; Synonyms=EEG-1L
CC {ECO:0000269|PubMed:14593112};
CC IsoId=Q6IMN6-2; Sequence=VSP_052536, VSP_027920;
CC Name=3 {ECO:0000269|PubMed:15489334};
CC IsoId=Q6IMN6-3; Sequence=VSP_027920, VSP_052538, VSP_052539;
CC Name=4 {ECO:0000269|PubMed:14702039};
CC IsoId=Q6IMN6-4; Sequence=VSP_052531;
CC Name=5 {ECO:0000269|PubMed:14593112}; Synonyms=EEG-1S
CC {ECO:0000269|PubMed:14593112};
CC IsoId=Q6IMN6-5; Sequence=VSP_052532, VSP_052533;
CC Name=6 {ECO:0000269|Ref.5};
CC IsoId=Q6IMN6-6; Sequence=VSP_052534, VSP_052535;
CC Name=7;
CC IsoId=Q6IMN6-7; Sequence=VSP_052537, VSP_052538, VSP_052539;
CC Name=9;
CC IsoId=Q6IMN6-9; Sequence=VSP_027920;
CC Name=10;
CC IsoId=Q6IMN6-10; Sequence=VSP_043293, VSP_052537, VSP_052538,
CC VSP_052539;
CC -!- TISSUE SPECIFICITY: Detected in all tissues tested with highest levels
CC of expression in brain and spleen. {ECO:0000269|PubMed:14593112}.
CC -!- DEVELOPMENTAL STAGE: Expression is highly regulated during erythroid
CC development with increased expression at the stage of differentiation
CC associated with the onset of global nuclear condensation and reduced
CC cell proliferation. {ECO:0000269|PubMed:14593112}.
CC -!- DOMAIN: The C1q domain is essential for the function in Wnt signaling.
CC {ECO:0000269|PubMed:18762581}.
CC -!- SIMILARITY: Belongs to the caprin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK83153.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY074490; AAL71549.1; -; mRNA.
DR EMBL; AY074491; AAL71550.1; -; mRNA.
DR EMBL; AC010198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066295; AAH66295.1; -; mRNA.
DR EMBL; BC111007; AAI11008.1; -; mRNA.
DR EMBL; BC117672; AAI17673.1; -; mRNA.
DR EMBL; BC117673; AAI17674.1; -; mRNA.
DR EMBL; AK021453; BAB13830.1; -; mRNA.
DR EMBL; AK026222; BAB15398.1; -; mRNA.
DR EMBL; AF326778; AAK83153.1; ALT_INIT; mRNA.
DR EMBL; BX538080; CAD98004.1; -; mRNA.
DR EMBL; BK001102; DAA01119.1; -; mRNA.
DR EMBL; BK001103; DAA01120.1; -; mRNA.
DR EMBL; BR000870; FAA00695.1; -; mRNA.
DR CCDS; CCDS41766.2; -. [Q6IMN6-3]
DR CCDS; CCDS55816.1; -. [Q6IMN6-10]
DR CCDS; CCDS8720.1; -. [Q6IMN6-2]
DR RefSeq; NP_001002259.1; NM_001002259.2. [Q6IMN6-1]
DR RefSeq; NP_001193785.1; NM_001206856.2. [Q6IMN6-10]
DR RefSeq; NP_001306771.1; NM_001319842.1.
DR RefSeq; NP_001306772.1; NM_001319843.1. [Q6IMN6-9]
DR RefSeq; NP_076414.2; NM_023925.4. [Q6IMN6-2]
DR RefSeq; NP_115532.3; NM_032156.4. [Q6IMN6-3]
DR RefSeq; XP_006719210.1; XM_006719147.3. [Q6IMN6-7]
DR PDB; 4OUL; X-ray; 1.95 A; A/B/C/D/E/F=996-1127.
DR PDB; 4OUM; X-ray; 1.49 A; A=996-1127.
DR PDB; 5J97; X-ray; 2.55 A; A/B=199-329.
DR PDBsum; 4OUL; -.
DR PDBsum; 4OUM; -.
DR PDBsum; 5J97; -.
DR AlphaFoldDB; Q6IMN6; -.
DR SMR; Q6IMN6; -.
DR BioGRID; 122431; 12.
DR IntAct; Q6IMN6; 9.
DR STRING; 9606.ENSP00000298892; -.
DR GlyGen; Q6IMN6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6IMN6; -.
DR PhosphoSitePlus; Q6IMN6; -.
DR BioMuta; CAPRIN2; -.
DR DMDM; 74748798; -.
DR EPD; Q6IMN6; -.
DR jPOST; Q6IMN6; -.
DR MassIVE; Q6IMN6; -.
DR MaxQB; Q6IMN6; -.
DR PeptideAtlas; Q6IMN6; -.
DR PRIDE; Q6IMN6; -.
DR ProteomicsDB; 66433; -. [Q6IMN6-1]
DR ProteomicsDB; 66434; -. [Q6IMN6-10]
DR ProteomicsDB; 66435; -. [Q6IMN6-2]
DR ProteomicsDB; 66436; -. [Q6IMN6-3]
DR ProteomicsDB; 66437; -. [Q6IMN6-4]
DR ProteomicsDB; 66438; -. [Q6IMN6-5]
DR ProteomicsDB; 66439; -. [Q6IMN6-6]
DR ProteomicsDB; 66440; -. [Q6IMN6-7]
DR ProteomicsDB; 66441; -. [Q6IMN6-9]
DR Antibodypedia; 42424; 99 antibodies from 19 providers.
DR DNASU; 65981; -.
DR Ensembl; ENST00000298892.9; ENSP00000298892.5; ENSG00000110888.18. [Q6IMN6-2]
DR Ensembl; ENST00000395805.6; ENSP00000379150.2; ENSG00000110888.18. [Q6IMN6-10]
DR Ensembl; ENST00000417045.5; ENSP00000391479.1; ENSG00000110888.18. [Q6IMN6-3]
DR Ensembl; ENST00000454014.6; ENSP00000403876.2; ENSG00000110888.18. [Q6IMN6-5]
DR Ensembl; ENST00000684863.1; ENSP00000510181.1; ENSG00000110888.18. [Q6IMN6-4]
DR Ensembl; ENST00000687797.1; ENSP00000510623.1; ENSG00000110888.18. [Q6IMN6-1]
DR GeneID; 65981; -.
DR KEGG; hsa:65981; -.
DR UCSC; uc001rjh.2; human. [Q6IMN6-1]
DR CTD; 65981; -.
DR DisGeNET; 65981; -.
DR GeneCards; CAPRIN2; -.
DR HGNC; HGNC:21259; CAPRIN2.
DR HPA; ENSG00000110888; Tissue enhanced (brain).
DR MIM; 610375; gene.
DR neXtProt; NX_Q6IMN6; -.
DR OpenTargets; ENSG00000110888; -.
DR PharmGKB; PA162381044; -.
DR VEuPathDB; HostDB:ENSG00000110888; -.
DR eggNOG; ENOG502QQ53; Eukaryota.
DR GeneTree; ENSGT00940000153438; -.
DR HOGENOM; CLU_009305_0_0_1; -.
DR InParanoid; Q6IMN6; -.
DR OMA; LNKDQMA; -.
DR OrthoDB; 155962at2759; -.
DR PhylomeDB; Q6IMN6; -.
DR TreeFam; TF329471; -.
DR PathwayCommons; Q6IMN6; -.
DR SignaLink; Q6IMN6; -.
DR SIGNOR; Q6IMN6; -.
DR BioGRID-ORCS; 65981; 24 hits in 1074 CRISPR screens.
DR ChiTaRS; CAPRIN2; human.
DR GeneWiki; CAPRIN2; -.
DR GenomeRNAi; 65981; -.
DR Pharos; Q6IMN6; Tbio.
DR PRO; PR:Q6IMN6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6IMN6; protein.
DR Bgee; ENSG00000110888; Expressed in dorsal root ganglion and 201 other tissues.
DR ExpressionAtlas; Q6IMN6; baseline and differential.
DR Genevisible; Q6IMN6; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
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; IPI:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA: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; IDA: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:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
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 3D-structure; Alternative splicing; Calcium; Cell membrane; Coiled coil;
KW Cytoplasm; Differentiation; Growth regulation; Membrane; Metal-binding;
KW Mitochondrion; Phosphoprotein; Protein synthesis inhibitor;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1127
FT /note="Caprin-2"
FT /id="PRO_0000302082"
FT DOMAIN 993..1127
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 67..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 129..156
FT /evidence="ECO:0000255"
FT COILED 194..216
FT /evidence="ECO:0000255"
FT COMPBIAS 85..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1078
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:0000269|PubMed:25331957,
FT ECO:0007744|PDB:4OUL"
FT BINDING 1084
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 ECO:0007744|PDB:4OUL"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05A80"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05A80"
FT VAR_SEQ 1..333
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_052531"
FT VAR_SEQ 270..278
FT /note="SVEDQMEQS -> RQTLEGSTV (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14593112"
FT /id="VSP_052532"
FT VAR_SEQ 279..1127
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14593112"
FT /id="VSP_052533"
FT VAR_SEQ 596
FT /note="P -> S (in isoform 6)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_052534"
FT VAR_SEQ 597..1127
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_052535"
FT VAR_SEQ 682..716
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043293"
FT VAR_SEQ 717..765
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593112"
FT /id="VSP_052536"
FT VAR_SEQ 823..843
FT /note="Missing (in isoform 7 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_052537"
FT VAR_SEQ 823
FT /note="Missing (in isoform 2, isoform 3 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14593112,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_027920"
FT VAR_SEQ 940..961
FT /note="GWSDSSQVSSPERDNETFNSGD -> NCFIMRNSLLLIKQQGGVILLR (in
FT isoform 3, isoform 7 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_052538"
FT VAR_SEQ 962..1127
FT /note="Missing (in isoform 3, isoform 7 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_052539"
FT VARIANT 114
FT /note="P -> S (in dbSNP:rs17688567)"
FT /id="VAR_048445"
FT VARIANT 237
FT /note="K -> R (in dbSNP:rs12146709)"
FT /id="VAR_048446"
FT VARIANT 519
FT /note="M -> V (in dbSNP:rs2304630)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_034939"
FT VARIANT 655
FT /note="S -> L (in dbSNP:rs2304628)"
FT /id="VAR_048447"
FT MUTAGEN 1048
FT /note="I->R: Impaired homotrimer formation. No effect on
FT LRP6 binding although LRP6 phosphorylation is significantly
FT reduced."
FT /evidence="ECO:0000269|PubMed:25331957"
FT MUTAGEN 1078
FT /note="D->A: Loss of calcium binding and increased
FT homotrimer stability; when associated with Ala-1084."
FT /evidence="ECO:0000269|PubMed:25331957"
FT MUTAGEN 1084
FT /note="E->A: Loss of calcium binding and increased
FT homotrimer stability; when associated with Ala-1078."
FT /evidence="ECO:0000269|PubMed:25331957"
FT MUTAGEN 1091
FT /note="I->S: Impaired homotrimer formation. No effect on
FT LRP6 binding although LRP6 phosphorylation is significantly
FT reduced."
FT /evidence="ECO:0000269|PubMed:25331957"
FT MUTAGEN 1114
FT /note="W->S: No effect on homotrimer formation."
FT /evidence="ECO:0000269|PubMed:25331957"
FT MUTAGEN 1122
FT /note="Y->S: No effect on homotrimer formation."
FT /evidence="ECO:0000269|PubMed:25331957"
FT CONFLICT 298
FT /note="Y -> D (in Ref. 4; BAB13830)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="P -> S (in Ref. 5; AAK83153)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="V -> A (in Ref. 4; BAB13830)"
FT /evidence="ECO:0000305"
FT HELIX 199..227
FT /evidence="ECO:0007829|PDB:5J97"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:5J97"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:5J97"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:5J97"
FT HELIX 271..287
FT /evidence="ECO:0007829|PDB:5J97"
FT HELIX 298..311
FT /evidence="ECO:0007829|PDB:5J97"
FT STRAND 999..1004
FT /evidence="ECO:0007829|PDB:4OUM"
FT STRAND 1011..1016
FT /evidence="ECO:0007829|PDB:4OUM"
FT STRAND 1020..1026
FT /evidence="ECO:0007829|PDB:4OUM"
FT TURN 1032..1035
FT /evidence="ECO:0007829|PDB:4OUM"
FT STRAND 1036..1038
FT /evidence="ECO:0007829|PDB:4OUM"
FT STRAND 1041..1053
FT /evidence="ECO:0007829|PDB:4OUM"
FT STRAND 1055..1058
FT /evidence="ECO:0007829|PDB:4OUM"
FT STRAND 1060..1066
FT /evidence="ECO:0007829|PDB:4OUM"
FT STRAND 1069..1076
FT /evidence="ECO:0007829|PDB:4OUM"
FT STRAND 1079..1082
FT /evidence="ECO:0007829|PDB:4OUM"
FT STRAND 1085..1094
FT /evidence="ECO:0007829|PDB:4OUM"
FT STRAND 1099..1107
FT /evidence="ECO:0007829|PDB:4OUM"
FT STRAND 1117..1126
FT /evidence="ECO:0007829|PDB:4OUM"
SQ SEQUENCE 1127 AA; 125925 MW; D74D1D284B69FA0F CRC64;
MEVQVSQASL GFELTSVEKS LREWSRLSRE VIAWLCPSSP NFILNFPPPP SASSVSMVQL
FSSPFGYQSP SGHSEEEREG NMKSAKPQVN HSQHGESQRA LSPLQSTLSS AASPSQAYET
YIENGLICLK HKIRNIEKKK LKLEDYKDRL KSGEHLNPDQ LEAVEKYEEV LHNLEFAKEL
QKTFSGLSLD LLKAQKKAQR REHMLKLEAE KKKLRTILQV QYVLQNLTQE HVQKDFKGGL
NGAVYLPSKE LDYLIKFSKL TCPERNESLS VEDQMEQSSL YFWDLLEGSE KAVVGTTYKH
LKDLLSKLLN SGYFESIPVP KNAKEKEVPL EEEMLIQSEK KTQLSKTESV KESESLMEFA
QPEIQPQEFL NRRYMTEVDY SNKQGEEQPW EADYARKPNL PKRWDMLTEP DGQEKKQESF
KSWEASGKHQ EVSKPAVSLE QRKQDTSKLR STLPEEQKKQ EISKSKPSPS QWKQDTPKSK
AGYVQEEQKK QETPKLWPVQ LQKEQDPKKQ TPKSWTPSMQ SEQNTTKSWT TPMCEEQDSK
QPETPKSWEN NVESQKHSLT SQSQISPKSW GVATASLIPN DQLLPRKLNT EPKDVPKPVH
QPVGSSSTLP KDPVLRKEKL QDLMTQIQGT CNFMQESVLD FDKPSSAIPT SQPPSATPGS
PVASKEQNLS SQSDFLQEPL QATSSPVTCS SNACLVTTDQ ASSGSETEFM TSETPEAAIP
PGKQPSSLAS PNPPMAKGSE QGFQSPPASS SSVTINTAPF QAMQTVFNVN APLPPRKEQE
IKESPYSPGY NQSFTTASTQ TPPQCQLPSI HVEQTVHSQE TAANYHPDGT IQVSNGSLAF
YPAQTNVFPR PTQPFVNSRG SVRGCTRGGR LITNSYRSPG GYKGFDTYRG LPSISNGNYS
QLQFQAREYS GAPYSQRDNF QQCYKRGGTS GGPRANSRAG WSDSSQVSSP ERDNETFNSG
DSGQGDSRSM TPVDVPVTNP AATILPVHVY PLPQQMRVAF SAARTSNLAP GTLDQPIVFD
LLLNNLGETF DLQLGRFNCP VNGTYVFIFH MLKLAVNVPL YVNLMKNEEV LVSAYANDGA
PDHETASNHA ILQLFQGDQI WLRLHRGAIY GSSWKYSTFS GYLLYQD
