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 24-JAN-2024, entry version 148. 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 Small intestine RC {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}; 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; 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 CCDS; CCDS91672.1; -. [Q6IMN6-4] 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 GlyCosmos; Q6IMN6; 1 site, 1 glycan. DR GlyGen; Q6IMN6; 3 sites, 1 O-linked glycan (3 sites). 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 PaxDb; 9606-ENSP00000298892; -. DR PeptideAtlas; 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; 124 antibodies from 20 providers. DR DNASU; 65981; -. DR Ensembl; ENST00000298892.9; ENSP00000298892.5; ENSG00000110888.19. [Q6IMN6-2] DR Ensembl; ENST00000395805.6; ENSP00000379150.2; ENSG00000110888.19. [Q6IMN6-10] DR Ensembl; ENST00000417045.5; ENSP00000391479.1; ENSG00000110888.19. [Q6IMN6-3] DR Ensembl; ENST00000454014.6; ENSP00000403876.2; ENSG00000110888.19. [Q6IMN6-5] DR Ensembl; ENST00000684863.1; ENSP00000510181.1; ENSG00000110888.19. [Q6IMN6-4] DR Ensembl; ENST00000687797.1; ENSP00000510623.1; ENSG00000110888.19. [Q6IMN6-1] DR GeneID; 65981; -. DR KEGG; hsa:65981; -. DR UCSC; uc001rjh.2; human. [Q6IMN6-1] DR AGR; HGNC:21259; -. DR CTD; 65981; -. DR DisGeNET; 65981; -. DR GeneCards; CAPRIN2; -. DR HGNC; HGNC:21259; CAPRIN2. DR HPA; ENSG00000110888; Low tissue specificity. 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; NHNQHGE; -. DR OrthoDB; 5403347at2759; -. DR PhylomeDB; Q6IMN6; -. DR TreeFam; TF329471; -. DR PathwayCommons; Q6IMN6; -. DR SignaLink; Q6IMN6; -. DR SIGNOR; Q6IMN6; -. DR BioGRID-ORCS; 65981; 24 hits in 1152 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 202 other cell types or tissues. DR ExpressionAtlas; Q6IMN6; baseline and differential. 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:0009950; P:dorsal/ventral axis specification; ISS:BHF-UCL. 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: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:SF5; CAPRIN-2; 1. DR PANTHER; PTHR22922; GPI-ANCHORED PROTEIN P137; 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; TNF-like; 1. DR PROSITE; PS50871; C1Q; 1. DR Genevisible; Q6IMN6; HS. 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 //