HNRPC_RABIT
ID HNRPC_RABIT Reviewed; 306 AA.
AC O77768;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein C;
DE Short=hnRNP C;
GN Name=HNRNPC;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New England white;
RX PubMed=9765602; DOI=10.1016/s0167-4781(98)00114-6;
RA Jiang W., Guo X., Bhavanandan V.P.;
RT "Four distinct regions in the auxiliary domain of heterogeneous nuclear
RT ribonucleoprotein C-related proteins.";
RL Biochim. Biophys. Acta 1399:229-233(1998).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF061582; AAC61695.1; -; mRNA.
DR RefSeq; NP_001075507.1; NM_001082038.1.
DR RefSeq; XP_008251254.1; XM_008253032.2.
DR RefSeq; XP_008267007.1; XM_008268785.2.
DR RefSeq; XP_008267008.1; XM_008268786.2.
DR RefSeq; XP_008267009.1; XM_008268787.2.
DR AlphaFoldDB; O77768; -.
DR BMRB; O77768; -.
DR SMR; O77768; -.
DR STRING; 9986.ENSOCUP00000000300; -.
DR Ensembl; ENSOCUT00000000339; ENSOCUP00000000300; ENSOCUG00000000339.
DR Ensembl; ENSOCUT00000015027; ENSOCUP00000012913; ENSOCUG00000015029.
DR GeneID; 100008686; -.
DR GeneID; 100354921; -.
DR KEGG; ocu:100008686; -.
DR KEGG; ocu:100354921; -.
DR CTD; 3183; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000153402; -.
DR HOGENOM; CLU_079090_0_0_1; -.
DR InParanoid; O77768; -.
DR OMA; RPAGDMY; -.
DR OrthoDB; 1211602at2759; -.
DR TreeFam; TF330974; -.
DR Proteomes; UP000001811; Chromosome 17.
DR Bgee; ENSOCUG00000000339; Expressed in autopod skin and 11 other tissues.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
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_0000239446"
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 220..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 190..224
FT /evidence="ECO:0000255"
FT MOTIF 155..161
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 158..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..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 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 175
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 175
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; 33684 MW; DE39742085744673 CRC64;
MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK GFAFVQYVNE
RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS AAEMYGSVPE HPSPSPLLSS
SFDLDYDFQR DYYDRMYSYP ARVPPPPPIA RAVVPSKRQR VSGNTSRRGK SFNSKSGQRG
SSSKSGKLKG DDLQAIKKEL TQIKQKVDSL LESLEKIEKE QSKQGVEMKN DKSEEEQSSS
SQKKDETNVK MESEGGADDS AEEGDLLDDD DNEDRGDDQL ELIKDDEKEA EEGEDDRDSA
NGEDDS
