HNRPC_PONAB
ID HNRPC_PONAB Reviewed; 306 AA.
AC Q5RA82;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein C;
DE Short=hnRNP C;
GN Name=HNRNPC; Synonyms=HNRPC;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds pre-mRNA and nucleates the assembly of 40S hnRNP
CC particles. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA
CC and modulates the stability and the level of translation of bound mRNA
CC molecules. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of
CC HNRNPC tetramers bind 700 nucleotides. May play a role in the early
CC steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine
CC (m6A) has been shown to alter the local structure in mRNAs and long
CC non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch',
CC facilitating binding of HNRNPC, leading to regulation of mRNA splicing.
CC {ECO:0000250|UniProtKB:P07910}.
CC -!- SUBUNIT: Tetramer composed of 3 copies of isoform C1 and 1 copy of
CC isoform C2. Assembly of 3 tetramers with bound pre-mRNA gives rise to a
CC 19S complex that interacts with HNRNPA2B1 tetramers. Component of the
CC 40S hnRNP particle. Identified in the spliceosome C complex. Interacts
CC with IGF2BP1 (By similarity). Interacts with PPIA/CYPA (By similarity).
CC {ECO:0000250|UniProtKB:P07910}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07910}.
CC Note=Component of ribonucleosomes. {ECO:0000250|UniProtKB:P07910}.
CC -!- PTM: Phosphorylated on Ser-260 and Ser-299 in resting cells.
CC {ECO:0000250|UniProtKB:P07910}.
CC -!- PTM: Sumoylated. Sumoylation reduces affinity for mRNA.
CC {ECO:0000250|UniProtKB:P07910}.
CC -!- SIMILARITY: Belongs to the RRM HNRPC family. RALY subfamily.
CC {ECO:0000305}.
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DR EMBL; CR859136; CAH91328.1; -; mRNA.
DR RefSeq; NP_001125784.1; NM_001132312.2.
DR AlphaFoldDB; Q5RA82; -.
DR BMRB; Q5RA82; -.
DR SMR; Q5RA82; -.
DR STRING; 9601.ENSPPYP00000006361; -.
DR Ensembl; ENSPPYT00000006616; ENSPPYP00000006361; ENSPPYG00000005593.
DR GeneID; 100172712; -.
DR KEGG; pon:100172712; -.
DR CTD; 3183; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000153402; -.
DR InParanoid; Q5RA82; -.
DR OMA; RTLISHC; -.
DR OrthoDB; 1211602at2759; -.
DR TreeFam; TF330974; -.
DR Proteomes; UP000001595; Chromosome 14.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; ISS:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; IEA:Ensembl.
DR GO; GO:0070034; F:telomerase RNA binding; IEA:Ensembl.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IEA:Ensembl.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR017347; hnRNP_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037992; hnRNP-C_Raly; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW RNA-binding; Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CHAIN 2..306
FT /note="Heterogeneous nuclear ribonucleoprotein C"
FT /id="PRO_0000239445"
FT DOMAIN 16..87
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 139..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 190..238
FT /evidence="ECO:0000255"
FT MOTIF 155..161
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 158..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..276
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..306
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z204"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 176
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z204"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 94
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 223
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 232
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 232
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 243
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07910"
SQ SEQUENCE 306 AA; 33670 MW; 17BBC78690C69C5C CRC64;
MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK GFAFVQYVNE
RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS AAEMYGSVTE HPSPSPLLSS
SFDLDYDFQR DYYDRMYSYP ARVPPPPPIA RAVVPSKRQR VSGNTSRRGK SGFNSKSGQR
GSSKSGKLKG DDLQAIKKEL TQIKQKVDSL LENLEKIEKE QSKQAVEMKN DKSEEEQSSS
SVKKDETNVK MESEGGADDS AEEGDLLDDD DNEDRGDDQL ELIKDDEKEA EEGEDDRDSA
NGEDDS
