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Caprin-2 (C1q domain-containing protein 1) (Cytoplasmic activation/proliferation-associated protein 2) (Gastric cancer multidrug resistance-associated protein) (Protein EEG-1) (RNA granule protein 140)

 CAPR2_HUMAN             Reviewed;        1127 AA.
Q6IMN6; E4NKG2; Q149P6; Q149P7; Q6IMN5; Q7Z371; Q8TE70; Q8TE71;
Q96RN6; Q9H667; Q9HAL4;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
07-JUN-2017, entry version 108.
RecName: Full=Caprin-2;
AltName: Full=C1q domain-containing protein 1;
AltName: Full=Cytoplasmic activation/proliferation-associated protein 2;
AltName: Full=Gastric cancer multidrug resistance-associated protein;
AltName: Full=Protein EEG-1;
AltName: Full=RNA granule protein 140;
Name=CAPRIN2 {ECO:0000312|EMBL:AAI17673.1};
Synonyms=C1QDC1, EEG1 {ECO:0000312|EMBL:AAL71549.1}, KIAA1873, RNG140;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAL71549.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Erythroblast {ECO:0000312|EMBL:AAL71549.1};
PubMed=14593112; DOI=10.1074/jbc.M305634200;
Aerbajinai W., Lee Y.T., Wojda U., Barr V.A., Miller J.L.;
"Cloning and characterization of a gene expressed during terminal
differentiation that encodes a novel inhibitor of growth.";
J. Biol. Chem. 279:1916-1921(2004).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3] {ECO:0000305, ECO:0000312|EMBL:AAI17673.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 10), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 844-1127 (ISOFORMS 1/2/4).
TISSUE=Brain {ECO:0000312|EMBL:AAH66295.1}, and Uterus;
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).
[4] {ECO:0000305, ECO:0000312|EMBL:BAB13830.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-776 (ISOFORM 1),
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-776 (ISOFORM 4), AND
VARIANT VAL-519.
TISSUE=Embryo {ECO:0000312|EMBL:BAB13830.1}, and
Small intestine {ECO:0000312|EMBL:BAB15398.1};
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5] {ECO:0000305, ECO:0000312|EMBL:AAK83153.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 319-1127 (ISOFORM 6).
Shi Y.-Q., Zhai H.-H., Han Y., Wang X., Wu H.-P., Fan D.-M.;
"Isolation and functional characterization of a novel gene associated
with gastric cancer multidrug resistance.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 766-1127 (ISOFORM 7).
TISSUE=Cerebellum;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7] {ECO:0000305, ECO:0000312|EMBL:DAA01119.1}
IDENTIFICATION (ISOFORM 9).
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]
FUNCTION, INTERACTION WITH LRP5 AND LRP6, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18762581; DOI=10.1083/jcb.200803147;
Ding Y., Xi Y., Chen T., Wang J.Y., Tao D.L., Wu Z.L., Li Y.P., Li C.,
Zeng R., Li L.;
"Caprin-2 enhances canonical Wnt signaling through regulating LRP5/6
phosphorylation.";
J. Cell Biol. 182:865-872(2008).
[9]
IDENTIFICATION.
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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH LRP6; CCNY AND CDK14, AND
SUBCELLULAR LOCATION.
PubMed=27821587; DOI=10.1074/jbc.M116.744607;
Wang X., Jia Y., Fei C., Song X., Li L.;
"Caprin-2 positively regulates CDK14/Cyclin Y-mediated LRP5/6
constitutive phosphorylation.";
J. Biol. Chem. 291:26427-26434(2016).
[12]
X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 996-1127 IN COMPLEX WITH
CALCIUM, SUBUNIT, INTERACTION WITH LRP6, AND MUTAGENESIS OF ILE-1048;
ASP-1078; GLU-1084; ILE-1091; TRP-1114 AND TYR-1122.
PubMed=25331957; DOI=10.1074/jbc.M114.591636;
Miao H., Jia Y., Xie S., Wang X., Zhao J., Chu Y., Zhou Z., Shi Z.,
Song X., Li L.;
"Structural insights into the C1q domain of Caprin-2 in canonical Wnt
signaling.";
J. Biol. Chem. 289:34104-34113(2014).
-!- FUNCTION: Promotes phosphorylation of the Wnt coreceptor LRP6,
leading to increased activity of the canonical Wnt signaling
pathway (PubMed:18762581). Faciliates constitutive LRP6
phosphorylation by CDK14/CCNY during G2/M stage of the cell cycle,
which may potentiate cells for Wnt signaling (PubMed:27821587).
May regulate the transport and translation of mRNAs, modulating
for instance the expression of proteins involved in synaptic
plasticity in neurons (By similarity). Involved in regulation of
growth as erythroblasts shift from a highly proliferative state
towards their terminal phase of differentiation (PubMed:14593112).
May be involved in apoptosis (PubMed:14593112).
{ECO:0000250|UniProtKB:Q05A80, ECO:0000269|PubMed:14593112,
ECO:0000269|PubMed:18762581, ECO:0000269|PubMed:27821587}.
-!- SUBUNIT: Homotrimer; via C1q domain (PubMed:25331957). Found in a
complex with LRP6, CCNY and CDK14 during G2/M stage; CAPRIN2
functions as a scaffold for the complex by binding to CCNY via its
N terminus and to CDK14 via its C terminus (PubMed:27821587).
Interacts with LRP5 (PubMed:18762581). Interacts with LRP6
(PubMed:18762581, PubMed:25331957). {ECO:0000269|PubMed:18762581,
ECO:0000269|PubMed:25331957}.
-!- INTERACTION:
O75197:LRP5; NbExp=3; IntAct=EBI-6918449, EBI-2466421;
P50542:PEX5; NbExp=3; IntAct=EBI-6918449, EBI-597835;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 2: Mitochondrion. Cytoplasm.
Note=Expressed throughout the cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 5: Mitochondrion. Note=Colocalizes
with aggregated mitochondria.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:27821587};
Peripheral membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=1 {ECO:0000269|PubMed:16541075};
IsoId=Q6IMN6-1; Sequence=Displayed;
Note=No experimental confirmation available. {ECO:0000305};
Name=2 {ECO:0000269|PubMed:14593112}; Synonyms=EEG-1L
{ECO:0000269|PubMed:14593112};
IsoId=Q6IMN6-2; Sequence=VSP_052536, VSP_027920;
Name=3 {ECO:0000269|PubMed:15489334};
IsoId=Q6IMN6-3; Sequence=VSP_027920, VSP_052538, VSP_052539;
Note=No experimental confirmation available. {ECO:0000305};
Name=4 {ECO:0000269|PubMed:14702039};
IsoId=Q6IMN6-4; Sequence=VSP_052531;
Note=No experimental confirmation available. {ECO:0000305};
Name=5 {ECO:0000269|PubMed:14593112}; Synonyms=EEG-1S
{ECO:0000269|PubMed:14593112};
IsoId=Q6IMN6-5; Sequence=VSP_052532, VSP_052533;
Name=6 {ECO:0000269|Ref.5};
IsoId=Q6IMN6-6; Sequence=VSP_052534, VSP_052535;
Name=7;
IsoId=Q6IMN6-7; Sequence=VSP_052537, VSP_052538, VSP_052539;
Note=No experimental confirmation available. {ECO:0000305};
Name=9;
IsoId=Q6IMN6-9; Sequence=VSP_027920;
Note=No experimental confirmation available.;
Name=10;
IsoId=Q6IMN6-10; Sequence=VSP_043293, VSP_052537, VSP_052538,
VSP_052539;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Detected in all tissues tested with highest
levels of expression in brain and spleen.
{ECO:0000269|PubMed:14593112}.
-!- DEVELOPMENTAL STAGE: Expression is highly regulated during
erythroid development with increased expression at the stage of
differentiation associated with the onset of global nuclear
condensation and reduced cell proliferation.
{ECO:0000269|PubMed:14593112}.
-!- DOMAIN: The C1q domain is essential for the function in Wnt
signaling. {ECO:0000269|PubMed:18762581}.
-!- SIMILARITY: Belongs to the caprin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK83153.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AY074490; AAL71549.1; -; mRNA.
EMBL; AY074491; AAL71550.1; -; mRNA.
EMBL; AC010198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC066295; AAH66295.1; -; mRNA.
EMBL; BC111007; AAI11008.1; -; mRNA.
EMBL; BC117672; AAI17673.1; -; mRNA.
EMBL; BC117673; AAI17674.1; -; mRNA.
EMBL; AK021453; BAB13830.1; -; mRNA.
EMBL; AK026222; BAB15398.1; -; mRNA.
EMBL; AF326778; AAK83153.1; ALT_INIT; mRNA.
EMBL; BX538080; CAD98004.1; -; mRNA.
EMBL; BK001102; DAA01119.1; -; mRNA.
EMBL; BK001103; DAA01120.1; -; mRNA.
EMBL; BR000870; FAA00695.1; -; mRNA.
CCDS; CCDS41766.2; -. [Q6IMN6-3]
CCDS; CCDS55816.1; -. [Q6IMN6-10]
CCDS; CCDS8720.1; -. [Q6IMN6-2]
RefSeq; NP_001002259.1; NM_001002259.2. [Q6IMN6-1]
RefSeq; NP_001193785.1; NM_001206856.2. [Q6IMN6-10]
RefSeq; NP_001306771.1; NM_001319842.1.
RefSeq; NP_001306772.1; NM_001319843.1. [Q6IMN6-9]
RefSeq; NP_076414.2; NM_023925.4. [Q6IMN6-2]
RefSeq; NP_115532.3; NM_032156.4. [Q6IMN6-3]
RefSeq; XP_006719210.1; XM_006719147.3. [Q6IMN6-7]
UniGene; Hs.234355; -.
PDB; 4OUL; X-ray; 1.95 A; A/B/C/D/E/F=996-1127.
PDB; 4OUM; X-ray; 1.49 A; A=996-1127.
PDBsum; 4OUL; -.
PDBsum; 4OUM; -.
ProteinModelPortal; Q6IMN6; -.
SMR; Q6IMN6; -.
BioGrid; 122431; 6.
IntAct; Q6IMN6; 4.
iPTMnet; Q6IMN6; -.
PhosphoSitePlus; Q6IMN6; -.
BioMuta; CAPRIN2; -.
DMDM; 74748798; -.
EPD; Q6IMN6; -.
MaxQB; Q6IMN6; -.
PeptideAtlas; Q6IMN6; -.
PRIDE; Q6IMN6; -.
Ensembl; ENST00000298892; ENSP00000298892; ENSG00000110888. [Q6IMN6-2]
Ensembl; ENST00000395805; ENSP00000379150; ENSG00000110888. [Q6IMN6-10]
Ensembl; ENST00000417045; ENSP00000391479; ENSG00000110888. [Q6IMN6-3]
Ensembl; ENST00000454014; ENSP00000403876; ENSG00000110888. [Q6IMN6-5]
GeneID; 65981; -.
KEGG; hsa:65981; -.
UCSC; uc001rjh.2; human. [Q6IMN6-1]
CTD; 65981; -.
DisGeNET; 65981; -.
GeneCards; CAPRIN2; -.
HGNC; HGNC:21259; CAPRIN2.
HPA; HPA039746; -.
MIM; 610375; gene.
neXtProt; NX_Q6IMN6; -.
OpenTargets; ENSG00000110888; -.
PharmGKB; PA162381044; -.
GeneTree; ENSGT00760000119052; -.
HOGENOM; HOG000082543; -.
HOVERGEN; HBG057777; -.
InParanoid; Q6IMN6; -.
KO; K18744; -.
OMA; AIYGSSW; -.
OrthoDB; EOG091G0UOF; -.
PhylomeDB; Q6IMN6; -.
TreeFam; TF329471; -.
SignaLink; Q6IMN6; -.
SIGNOR; Q6IMN6; -.
ChiTaRS; CAPRIN2; human.
GeneWiki; CAPRIN2; -.
GenomeRNAi; 65981; -.
PRO; PR:Q6IMN6; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000110888; -.
ExpressionAtlas; Q6IMN6; baseline and differential.
Genevisible; Q6IMN6; HS.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005102; F:receptor binding; IPI:BHF-UCL.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISS:UniProtKB.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
Gene3D; 2.60.120.40; -; 1.
InterPro; IPR001073; C1q_dom.
InterPro; IPR028816; Caprin.
InterPro; IPR022070; Caprin-1_C.
InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
PANTHER; PTHR22922; PTHR22922; 1.
Pfam; PF00386; C1q; 1.
Pfam; PF12287; Caprin-1_C; 1.
PRINTS; PR00007; COMPLEMNTC1Q.
SMART; SM00110; C1Q; 1.
SUPFAM; SSF49842; SSF49842; 1.
PROSITE; PS50871; C1Q; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell membrane;
Coiled coil; Complete proteome; Cytoplasm; Differentiation;
Growth regulation; Membrane; Metal-binding; Mitochondrion;
Phosphoprotein; Polymorphism; Protein synthesis inhibitor;
Reference proteome; RNA-binding.
CHAIN 1 1127 Caprin-2.
/FTId=PRO_0000302082.
DOMAIN 993 1127 C1q. {ECO:0000255|PROSITE-
ProRule:PRU00368}.
COILED 129 156 {ECO:0000255}.
COILED 194 216 {ECO:0000255}.
METAL 1078 1078 Calcium 1; shared with neighboring
subunits. {ECO:0000244|PDB:4OUL,
ECO:0000269|PubMed:25331957}.
METAL 1084 1084 Calcium 2; shared with neighboring
subunits. {ECO:0000244|PDB:4OUL,
ECO:0000269|PubMed:25331957}.
MOD_RES 948 948 Phosphoserine.
{ECO:0000250|UniProtKB:Q05A80}.
MOD_RES 949 949 Phosphoserine.
{ECO:0000250|UniProtKB:Q05A80}.
VAR_SEQ 1 333 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_052531.
VAR_SEQ 270 278 SVEDQMEQS -> RQTLEGSTV (in isoform 5).
{ECO:0000303|PubMed:14593112}.
/FTId=VSP_052532.
VAR_SEQ 279 1127 Missing (in isoform 5).
{ECO:0000303|PubMed:14593112}.
/FTId=VSP_052533.
VAR_SEQ 596 596 P -> S (in isoform 6).
{ECO:0000303|Ref.5}.
/FTId=VSP_052534.
VAR_SEQ 597 1127 Missing (in isoform 6).
{ECO:0000303|Ref.5}.
/FTId=VSP_052535.
VAR_SEQ 682 716 Missing (in isoform 10).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043293.
VAR_SEQ 717 765 Missing (in isoform 2).
{ECO:0000303|PubMed:14593112}.
/FTId=VSP_052536.
VAR_SEQ 823 843 Missing (in isoform 7 and isoform 10).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_052537.
VAR_SEQ 823 823 Missing (in isoform 2, isoform 3 and
isoform 9). {ECO:0000303|PubMed:14593112,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_027920.
VAR_SEQ 940 961 GWSDSSQVSSPERDNETFNSGD -> NCFIMRNSLLLIKQQ
GGVILLR (in isoform 3, isoform 7 and
isoform 10).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_052538.
VAR_SEQ 962 1127 Missing (in isoform 3, isoform 7 and
isoform 10).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_052539.
VARIANT 114 114 P -> S (in dbSNP:rs17688567).
/FTId=VAR_048445.
VARIANT 237 237 K -> R (in dbSNP:rs12146709).
/FTId=VAR_048446.
VARIANT 519 519 M -> V (in dbSNP:rs2304630).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_034939.
VARIANT 655 655 S -> L (in dbSNP:rs2304628).
/FTId=VAR_048447.
MUTAGEN 1048 1048 I->R: Impaired homotrimer formation. No
effect on LRP6 binding although LRP6
phosphorylation is significantly reduced.
{ECO:0000269|PubMed:25331957}.
MUTAGEN 1078 1078 D->A: Loss of calcium binding and
increased homotrimer stability; when
associated with Ala-1084.
{ECO:0000269|PubMed:25331957}.
MUTAGEN 1084 1084 E->A: Loss of calcium binding and
increased homotrimer stability; when
associated with Ala-1078.
{ECO:0000269|PubMed:25331957}.
MUTAGEN 1091 1091 I->S: Impaired homotrimer formation. No
effect on LRP6 binding although LRP6
phosphorylation is significantly reduced.
{ECO:0000269|PubMed:25331957}.
MUTAGEN 1114 1114 W->S: No effect on homotrimer formation.
{ECO:0000269|PubMed:25331957}.
MUTAGEN 1122 1122 Y->S: No effect on homotrimer formation.
{ECO:0000269|PubMed:25331957}.
CONFLICT 298 298 Y -> D (in Ref. 4; BAB13830).
{ECO:0000305}.
CONFLICT 320 320 P -> S (in Ref. 5; AAK83153).
{ECO:0000305}.
CONFLICT 595 595 V -> A (in Ref. 4; BAB13830).
{ECO:0000305}.
STRAND 999 1004 {ECO:0000244|PDB:4OUM}.
STRAND 1011 1016 {ECO:0000244|PDB:4OUM}.
STRAND 1020 1026 {ECO:0000244|PDB:4OUM}.
TURN 1032 1035 {ECO:0000244|PDB:4OUM}.
STRAND 1036 1038 {ECO:0000244|PDB:4OUM}.
STRAND 1041 1053 {ECO:0000244|PDB:4OUM}.
STRAND 1055 1058 {ECO:0000244|PDB:4OUM}.
STRAND 1060 1066 {ECO:0000244|PDB:4OUM}.
STRAND 1069 1076 {ECO:0000244|PDB:4OUM}.
STRAND 1079 1082 {ECO:0000244|PDB:4OUM}.
STRAND 1085 1094 {ECO:0000244|PDB:4OUM}.
STRAND 1099 1107 {ECO:0000244|PDB:4OUM}.
STRAND 1117 1126 {ECO:0000244|PDB:4OUM}.
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


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