CAPR1_BOVIN
ID CAPR1_BOVIN Reviewed; 708 AA.
AC Q1LZB6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Caprin-1;
DE AltName: Full=Cytoplasmic activation- and proliferation-associated protein 1;
DE AltName: Full=RNA granule protein 105;
GN Name=CAPRIN1; Synonyms=RNG105;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q14444}.
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:0000250|UniProtKB:Q5M9G3}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q14444}. Note=Associated with RNA granules (By
CC similarity). At the leading edge of migrating fibroblasts, colocalizes
CC with DDX3X (By similarity). {ECO:0000250|UniProtKB:Q14444}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the caprin family. {ECO:0000305}.
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DR EMBL; BC116102; AAI16103.1; -; mRNA.
DR RefSeq; NP_001069530.1; NM_001076062.1.
DR AlphaFoldDB; Q1LZB6; -.
DR SMR; Q1LZB6; -.
DR BioGRID; 192146; 1.
DR STRING; 9913.ENSBTAP00000022266; -.
DR PaxDb; Q1LZB6; -.
DR PeptideAtlas; Q1LZB6; -.
DR PRIDE; Q1LZB6; -.
DR Ensembl; ENSBTAT00000022266; ENSBTAP00000022266; ENSBTAG00000016744.
DR GeneID; 535571; -.
DR KEGG; bta:535571; -.
DR CTD; 4076; -.
DR VEuPathDB; HostDB:ENSBTAG00000016744; -.
DR VGNC; VGNC:26751; CAPRIN1.
DR eggNOG; ENOG502QUGC; Eukaryota.
DR GeneTree; ENSGT00940000153438; -.
DR InParanoid; Q1LZB6; -.
DR OMA; VEQNYFK; -.
DR OrthoDB; 382856at2759; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000016744; Expressed in oviduct epithelium and 107 other tissues.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; ISS: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 2: Evidence at transcript 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..708
FT /note="Caprin-1"
FT /id="PRO_0000327208"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..379
FT /note="G3BP1-binding"
FT /evidence="ECO:0000250"
FT REGION 415..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..708
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 272..286
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..678
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 697
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
FT MOD_RES 697
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14444"
SQ SEQUENCE 708 AA; 78328 MW; 166A1F93783EE5F7 CRC64;
MPSATSHSGS GSKSSGPPPP SGSSGNEAGA GAAAPASQHP MTGTGAVQTE AMKQILGVID
KKLRNLEKKK GKLDDYQERM NKGERLNQDQ LDAVSKYQEV TNNLEFAKEL QRSFMALSQD
IQKTIKKTAR REQLMREEAE QKRLKTVLEL QYVLDKLGDD EVRTDLKQGL NGVPILSEEE
LSLLDEFYKL ADPERDMSLR LNEQYEHASI HLWDLLEGKE KPVCGTTYKA LKEIVERVFQ
SNYFDSTHNH QNGLCEEEEA ASAPTVEDQA AEAEPEPVEE YTEQNEVEST EYVNRQFMAE
TQFSSGEKEQ VDDWTVETVE VVNSLQQQPQ AASPSVPEPH SLTPVAQADP LVRRQRVQDL
MAQMQGPYNF IQDSMLDFEN QTLDPAIVSA QPMNPAQNMD IPQLVCPPVH SESRLAQPNQ
VSVQPEATQV PLVSSTSEGY TASQPLYQPS HATDQRPQKE PIDQIQATIS LNTDQTTASS
SLPAASQPQV FQAGTSKPLH SSGINVNAAP FQSMQTVFNM NAPVPPVNEP ETLKQQNQYQ
ASYNQSFSSQ PHQVEQTELQ QEQLQTVVGT YHGSQDQPHQ VTGNHQQPPQ QNTGFPRSNQ
PYYNSRGVSR GGSRGARGLM NGYRGPANGF RGGYDGYRPS FSTNTPNSGY TQSQFSAPRD
YSGYQRDGYQ QNFKRGSGQS GPRGAPRGRG GPPRPNRGMP QMNTQQVN
