CAPR1_RAT
ID CAPR1_RAT Reviewed; 707 AA.
AC Q5M9G3; A9ZSZ9; Q6YF16;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Caprin-1;
DE AltName: Full=Cytoplasmic activation- and proliferation-associated protein 1;
DE AltName: Full=GPI-anchored protein p137;
DE Short=GPI-p137;
DE Short=p137GPI;
DE AltName: Full=RNA granule protein 105;
GN Name=Caprin1; Synonyms=Gpiap1, Rng105;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, MRNA-BINDING,
RP AND TISSUE SPECIFICITY.
RX PubMed=15858068; DOI=10.1523/jneurosci.0382-05.2005;
RA Shiina N., Shinkura K., Tokunaga M.;
RT "A novel RNA-binding protein in neuronal RNA granules: regulatory machinery
RT for local translation.";
RL J. Neurosci. 25:4420-4434(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-70; 121-430 AND 518-686.
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-707.
RC TISSUE=Kidney;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-707, AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Fetal heart;
RX PubMed=14565619; DOI=10.1002/bdra.10073;
RA Collier J.M., Selmin O., Johnson P.D., Runyan R.B.;
RT "Trichloroethylene effects on gene expression during cardiac development.";
RL Birth Defects Res. A Clin. Mol. Teratol. 67:488-495(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND RNA-BINDING.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Binds directly and
CC selectively to MYC and CCND2 RNAs. In neuronal cells, directly binds to
CC several mRNAs associated with RNA granules, including BDNF, CAMK2A,
CC CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not
CC to rRNAs. {ECO:0000269|PubMed:15858068, ECO:0000269|PubMed:20516077}.
CC -!- SUBUNIT: May form homomultimers (By similarity). Interacts with G3BP1;
CC interaction is direct and takes place in cytoplasmic RNA granules (By
CC similarity). Interacts with PQBP1 (By similarity). Interacts with DDX3X
CC (By similarity). {ECO:0000250|UniProtKB:Q14444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q14444}. Cell projection, dendrite
CC {ECO:0000269|PubMed:15858068, ECO:0000269|PubMed:20516077}. Cell
CC projection, lamellipodium {ECO:0000250|UniProtKB:Q14444}.
CC Note=Associated with RNA granules (By similarity). At the leading edge
CC of migrating fibroblasts, colocalizes with DDX3X (By similarity).
CC {ECO:0000250|UniProtKB:Q14444}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampal and neocortical pyramidal
CC neurons, but not in Purkinje cells. {ECO:0000269|PubMed:15858068}.
CC -!- INDUCTION: Down-regulated by exposure to trichloroethylene (TCE) and
CC dichloroethylene (DCE) in fetal heart. {ECO:0000269|PubMed:14565619}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the caprin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a GPI-anchored membrane protein.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO21306.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB373991; BAF98181.1; -; mRNA.
DR EMBL; AABR03028010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03028081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03029653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC087123; AAH87123.1; -; mRNA.
DR EMBL; AY155572; AAO21306.1; ALT_INIT; mRNA.
DR RefSeq; NP_001012185.2; NM_001012185.2.
DR AlphaFoldDB; Q5M9G3; -.
DR SMR; Q5M9G3; -.
DR BioGRID; 263241; 2.
DR IntAct; Q5M9G3; 2.
DR MINT; Q5M9G3; -.
DR STRING; 10116.ENSRNOP00000012428; -.
DR jPOST; Q5M9G3; -.
DR PaxDb; Q5M9G3; -.
DR PRIDE; Q5M9G3; -.
DR GeneID; 362173; -.
DR KEGG; rno:362173; -.
DR UCSC; RGD:1305707; rat.
DR CTD; 4076; -.
DR RGD; 1305707; Caprin1.
DR VEuPathDB; HostDB:ENSRNOG00000009152; -.
DR eggNOG; ENOG502QUGC; Eukaryota.
DR InParanoid; Q5M9G3; -.
DR OrthoDB; 382856at2759; -.
DR PhylomeDB; Q5M9G3; -.
DR PRO; PR:Q5M9G3; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000009152; Expressed in spleen and 19 other tissues.
DR ExpressionAtlas; Q5M9G3; baseline and differential.
DR Genevisible; Q5M9G3; RN.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
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 InterPro; IPR028816; Caprin.
DR InterPro; IPR022070; Caprin-1_C.
DR InterPro; IPR041637; Caprin-1_dimer.
DR PANTHER; PTHR22922; PTHR22922; 1.
DR Pfam; PF12287; Caprin-1_C; 1.
DR Pfam; PF18293; Caprin-1_dimer; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Coiled coil; Cytoplasm; Differentiation;
KW Glycoprotein; Methylation; Phosphoprotein; Protein synthesis inhibitor;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT CHAIN 2..707
FT /note="Caprin-1"
FT /id="PRO_0000327209"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..379
FT /note="G3BP1-binding"
FT /evidence="ECO:0000250"
FT REGION 412..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 58..92
FT /evidence="ECO:0000255"
FT COILED 123..151
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 163
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q60865"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 624
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 631
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 638
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 696
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 696
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT CONFLICT 27
FT /note="E -> K (in Ref. 4; AAO21306)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="Q -> E (in Ref. 4; AAO21306)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="Q -> Y (in Ref. 4; AAO21306)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="T -> A (in Ref. 4; AAO21306)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="S -> N (in Ref. 4; AAO21306)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="T -> Q (in Ref. 4; AAO21306)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="Y -> F (in Ref. 4; AAO21306)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="P -> L (in Ref. 4; AAO21306)"
FT /evidence="ECO:0000305"
FT CONFLICT 587..588
FT /note="QP -> AA (in Ref. 4; AAO21306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 78121 MW; 3F0859BC83403242 CRC64;
MPSATSHSGS GSKSSGPPPP SGSSGSEAAA GAAAPASQHP ATGTGAVQTE AMKQILGVID
KKLRNLEKKK GKLDDYQERM NKGERLNQDQ LDAVSKYQEV TNNLEFAKEL QRSFMALSQD
IQKTIKKTAR REQLMREEAE QKRLKTVLEL QYVLDKLGDD DVRTDLKQGL SGVPILSEEE
LSLLDEFYKL VDPERDMSLR LNEQYEHASI HLWDLLEGKE KPVCGTTYKA LKEIVERVFQ
SNYFDSTHNH QNGLCEEEEA ASAPIVEDQV AEAEPEPTEE YTEQSEVEST EYVNRQFMAE
TQFSSGEKEQ VDEWAVETVE VVNSLQQQPQ AASPSVPEPH SLTPVAQSDP LVRRQRVQDL
MAQMQGPYNF IQDSMLDFEN QTLDPAIVSA QPMNPTQNMD MPQLVCPQVH SESRLAQSNQ
VPVQPEATQV PLVSSTSEGY TASQPLYQPS HAAEQRPQKE PIDQIQATIS LNTEQTTASS
SLPAASQPQV FQAGASKPLH SSGINVNAAP FQSMQTVFNM NAPVPPVNEP ETLKQQSQYQ
ASYNQSFSSQ PHQVEQTELQ QDQLQTVVGT YHGSQDQPHQ VPGNHQQPPQ QSTGFPRSSQ
PYYNSRGVSR GGSRGARGLM NGYRGPANGF RGGYDGYRSS FSNTPNSGYT QSQFNAPRDY
SGYQRDGYQQ NFKRGSGQSG PRGAPRGRGG PPRPNRGMPQ MNTQQVN
