ID   HNRPC_XENLA             Reviewed;         282 AA.
AC   P19600; Q6GR47;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein C;
DE            Short=hnRNP C;
DE   AltName: Full=hnRNP core protein C;
GN   Name=hnrnpc; Synonyms=hnrpc;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2904678; DOI=10.1073/pnas.85.24.9669;
RA   Preugschat F., Wold B.;
RT   "Isolation and characterization of a Xenopus laevis C protein cDNA:
RT   structure and expression of a heterogeneous nuclear ribonucleoprotein core
RT   protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:9669-9673(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-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. {ECO:0000250|UniProtKB:P07910}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {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; J03831; AAA60937.1; -; mRNA.
DR   EMBL; BC071084; AAH71084.1; -; mRNA.
DR   PIR; A31765; A31765.
DR   RefSeq; NP_001081360.1; NM_001087891.1.
DR   RefSeq; XP_018086485.1; XM_018230996.1.
DR   RefSeq; XP_018086563.1; XM_018231074.1.
DR   AlphaFoldDB; P19600; -.
DR   SMR; P19600; -.
DR   BioGRID; 99132; 1.
DR   PRIDE; P19600; -.
DR   DNASU; 397793; -.
DR   GeneID; 397793; -.
DR   KEGG; xla:397793; -.
DR   CTD; 397793; -.
DR   Xenbase; XB-GENE-489145; hnrnpc.L.
DR   OMA; RPAGDMY; -.
DR   OrthoDB; 1211602at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 397793; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IPR036305; RGS_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; SSF48097; SSF48097; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding.
FT   CHAIN           1..282
FT                   /note="Heterogeneous nuclear ribonucleoprotein C"
FT                   /id="PRO_0000081847"
FT   DOMAIN          17..88
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          131..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          177..217
FT                   /evidence="ECO:0000255"
FT   MOTIF           141..147
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        145..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..282
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   282 AA;  30950 MW;  7373FA46F8C85413 CRC64;
     MMASNVTNKT DPRSMNSRVF IGNLNTLVVK KTDVEAIFSK YGKIVGCSVH KGFAFVQFSN
     ERTARTAVAG EDGRMIAGQV LDINLAAEPK ANRSKTGVKR SAADMYGSSF DLEYDFPRDY
     YDSYSATRVP APPPLARAVV PSKRQRVSGN ASRRGKSGFN SKSGQRGGSS KSSRLKGDDL
     QAIKKELSQI KQRVDSLLEN LERIERDQSK QDTKLDDDQS SVSLKKEETG VKLIEETGDS
     AEEGDLLDDD EQGEDTLEEI KDGDKETEEG EDEGDSANEE DS