ID   CAPR1_HUMAN             Reviewed;         709 AA.
AC   Q14444; A6NMY7; Q15074; Q6IMN4; Q6IMN7; Q9BV09;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   05-OCT-2010, entry version 81.
DE   RecName: Full=Caprin-1;
DE   AltName: Full=Cell cycle-associated protein 1;
DE   AltName: Full=Cytoplasmic activation- and proliferation-associated protein 1;
DE   AltName: Full=GPI-anchored membrane protein 1;
DE   AltName: Full=GPI-anchored protein p137;
DE            Short=GPI-p137;
DE            Short=p137GPI;
DE   AltName: Full=Membrane component chromosome 11 surface marker 1;
GN   Name=CAPRIN1; Synonyms=GPIAP1, GPIP137, M11S1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-263.
RC   TISSUE=Colon;
RX   MEDLINE=95386525; PubMed=7657653; DOI=10.1074/jbc.270.35.20717;
RA   Ellis J.A., Luzio J.P.;
RT   "Identification and characterization of a novel protein (p137) which
RT   transcytoses bidirectionally in Caco-2 cells.";
RL   J. Biol. Chem. 270:20717-20723(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-72.
RX   MEDLINE=96230346; PubMed=8786113; DOI=10.1006/geno.1996.0099;
RA   Gessler M., Klant B., Tsaoussidou S., Ellis J.A., Luzio J.P.;
RT   "The gene encoding the GPI-anchored membrane protein p137GPI (M11S1)
RT   maps to human chromosome 11p13 and is highly conserved in the mouse.";
RL   Genomics 32:169-170(1996).
RN   [6]
RP   PROTEIN SEQUENCE OF 56-63; 88-110; 115-125; 148-158; 298-310 AND
RP   634-660, AND MASS SPECTROMETRY.
RC   TISSUE=Colon carcinoma;
RA   Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [7]
RP   IDENTIFICATION (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP   MULTIMERIZATION.
RX   PubMed=14764709;
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
RT   of a new family of proteins.";
RL   J. Immunol. 172:2389-2400(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611 AND SER-615, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17924679; DOI=10.1021/pr070152u;
RA   Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT   "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT   cells and high confident phosphopeptide identification by cross-
RT   validation of MS/MS and MS/MS/MS spectra.";
RL   J. Proteome Res. 6:4150-4162(2007).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH G3BP1, MRNA-BINDING,
RP   AND MUTAGENESIS OF ARG-612; ARG-633 AND ARG-690.
RX   PubMed=17210633; DOI=10.1128/MCB.02300-06;
RA   Solomon S., Xu Y., Wang B., David M.D., Schubert P., Kennedy D.,
RA   Schrader J.W.;
RT   "Distinct structural features of caprin-1 mediate its interaction with
RT   G3BP-1 and its induction of phosphorylation of eukaryotic translation
RT   initiation factor 2alpha, entry to cytoplasmic stress granules, and
RT   selective interaction with a subset of mRNAs.";
RL   Mol. Cell. Biol. 27:2324-2342(2007).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: May regulate the transport and translation of mRNAs of
CC       proteins involved in synaptic plasticity in neurons and cell
CC       proliferation and migration in multiple cell types (By
CC       similarity).
CC   -!- SUBUNIT: May form homomultimers. Directly interacts with G3BP1 in
CC       cytoplasmic RNA granules. Binds directly and selectively to MYC
CC       and CCND2 RNAs. In neuronal cells, directly binds to several mRNAs
CC       associated with RNA granules, including BDNF, CAMK2A, CREB1, MAP2,
CC       NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not to rRNAs
CC       (By similarity).
CC   -!- INTERACTION:
CC       Q96BK5:PINX1; NbExp=1; IntAct=EBI-1047080, EBI-721782;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection,
CC       dendrite. Note=Associated with RNA granules (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q14444-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14444-2; Sequence=VSP_032687;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- MISCELLANEOUS: Overexpression induces the formation of cytoplasmic
CC       stress granules and EIF2A phosphorylation through a mechanism that
CC       depends on its ability to bind mRNA.
CC   -!- SIMILARITY: Belongs to the caprin family.
CC   -!- CAUTION: Was originally thought to be a GPI-anchored membrane
CC       protein (PubMed:7657653).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA61751.1; Type=Erroneous gene model prediction;
CC       Sequence=CAA88096.1; Type=Frameshift; Positions=11, 629;
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DR   EMBL; Z48042; CAA88096.1; ALT_FRAME; mRNA.
DR   EMBL; AC090469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471064; EAW68177.1; -; Genomic_DNA.
DR   EMBL; CH471064; EAW68178.1; -; Genomic_DNA.
DR   EMBL; BC001731; AAH01731.2; -; mRNA.
DR   EMBL; X89572; CAA61751.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BK001101; DAA01118.1; -; mRNA.
DR   EMBL; BK001104; DAA01121.1; -; mRNA.
DR   IPI; IPI00783872; -.
DR   IPI; IPI00873926; -.
DR   PIR; A57352; A57352.
DR   RefSeq; NP_005889.3; -.
DR   RefSeq; NP_976240.1; -.
DR   UniGene; Hs.471818; -.
DR   ProteinModelPortal; Q14444; -.
DR   IntAct; Q14444; 8.
DR   MINT; MINT-1624210; -.
DR   STRING; Q14444; -.
DR   PhosphoSite; Q14444; -.
DR   PRIDE; Q14444; -.
DR   Ensembl; ENST00000341394; ENSP00000340329; ENSG00000135387.
DR   GeneID; 4076; -.
DR   KEGG; hsa:4076; -.
DR   UCSC; uc001mvg.1; human.
DR   UCSC; uc001mvh.1; human.
DR   CTD; 4076; -.
DR   GeneCards; GC11P034031; -.
DR   HGNC; HGNC:6743; CAPRIN1.
DR   HPA; HPA018126; -.
DR   MIM; 601178; gene.
DR   eggNOG; prNOG17895; -.
DR   HOGENOM; HBG713539; -.
DR   HOVERGEN; HBG051781; -.
DR   InParanoid; Q14444; -.
DR   OMA; PFQSMQT; -.
DR   OrthoDB; EOG99PDJB; -.
DR   NextBio; 15972; -.
DR   ArrayExpress; Q14444; -.
DR   Bgee; Q14444; -.
DR   CleanEx; HS_CAPRIN1; -.
DR   Genevestigator; Q14444; -.
DR   GermOnline; ENSG00000135387; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR022070; Caprin-1_C.
DR   Pfam; PF12287; Caprin-1_C; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Coiled coil; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Phosphoprotein; Polymorphism.
FT   CHAIN         1    709       Caprin-1.
FT                                /FTId=PRO_0000087549.
FT   REGION      360    381       G3BP1-binding.
FT   COILED       60     94       Potential.
FT   COILED      125    153       Potential.
FT   MOD_RES     611    611       Phosphoserine.
FT   MOD_RES     615    615       Phosphoserine.
FT   VAR_SEQ     690    709       RGGPPRPNRGMPQMNTQQVN -> NILWW (in isoform
FT                                2).
FT                                /FTId=VSP_032687.
FT   VARIANT     263    263       A -> D (in dbSNP:rs1132973).
FT                                /FTId=VAR_042425.
FT   VARIANT     588    588       Q -> H (in dbSNP:rs12282627).
FT                                /FTId=VAR_042426.
FT   VARIANT     616    616       R -> H (in dbSNP:rs11552285).
FT                                /FTId=VAR_042427.
FT   MUTAGEN     612    612       R->A: Major reduction in MYC and CCND2
FT                                RNA-binding; when associated with A-633
FT                                and A-690.
FT   MUTAGEN     633    633       R->A: Major reduction in MYC and CCND2
FT                                RNA-binding; when associated with A-612
FT                                and A-690.
FT   MUTAGEN     690    690       R->A: Major reduction in MYC and CCND2
FT                                RNA-binding; when associated with A-612
FT                                and A-633.
FT   CONFLICT    370    370       Y -> D (in Ref. 1; CAA88096).
SQ   SEQUENCE   709 AA;  78366 MW;  56F5BC188CA3A2D4 CRC64;
     MPSATSHSGS GSKSSGPPPP SGSSGSEAAA GAGAAAPASQ HPATGTGAVQ TEAMKQILGV
     IDKKLRNLEK KKGKLDDYQE RMNKGERLNQ DQLDAVSKYQ EVTNNLEFAK ELQRSFMALS
     QDIQKTIKKT ARREQLMREE AEQKRLKTVL ELQYVLDKLG DDEVRTDLKQ GLNGVPILSE
     EELSLLDEFY KLVDPERDMS LRLNEQYEHA SIHLWDLLEG KEKPVCGTTY KVLKEIVERV
     FQSNYFDSTH NHQNGLCEEE EAASAPAVED QVPEAEPEPA EEYTEQSEVE STEYVNRQFM
     AETQFTSGEK EQVDEWTVET VEVVNSLQQQ PQAASPSVPE PHSLTPVAQA DPLVRRQRVQ
     DLMAQMQGPY NFIQDSMLDF ENQTLDPAIV SAQPMNPTQN MDMPQLVCPP VHSESRLAQP
     NQVPVQPEAT QVPLVSSTSE GYTASQPLYQ PSHATEQRPQ KEPIDQIQAT ISLNTDQTTA
     SSSLPAASQP QVFQAGTSKP LHSSGINVNA APFQSMQTVF NMNAPVPPVN EPETLKQQNQ
     YQASYNQSFS SQPHQVEQTE LQQEQLQTVV GTYHGSPDQS HQVTGNHQQP PQQNTGFPRS
     NQPYYNSRGV SRGGSRGARG LMNGYRGPAN GFRGGYDGYR PSFSNTPNSG YTQSQFSAPR
     DYSGYQRDGY QQNFKRGSGQ SGPRGAPRGR GGPPRPNRGM PQMNTQQVN
//