HNRPC_RAT
ID HNRPC_RAT Reviewed; 298 AA.
AC G3V9R8; D4ACR0; Q4V8K6;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein C {ECO:0000305};
DE Short=hnRNP C;
DE AltName: Full=hnRNP core protein C;
GN Name=Hnrnpc {ECO:0000312|RGD:1309982}; Synonyms=Hnrpc;
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 [LARGE SCALE GENOMIC DNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-217; SER-226;
RP SER-231; SER-246; SER-253 AND SER-291, AND IDENTIFICATION BY MASS
RP 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: 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-253 and Ser-291 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; AABR06080380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06080381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06080382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06080383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06080384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06082837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06082838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06082839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC097346; AAH97346.1; -; mRNA.
DR AlphaFoldDB; G3V9R8; -.
DR BMRB; G3V9R8; -.
DR SMR; G3V9R8; -.
DR IntAct; G3V9R8; 3.
DR MINT; G3V9R8; -.
DR STRING; 10116.ENSRNOP00000057256; -.
DR iPTMnet; G3V9R8; -.
DR PhosphoSitePlus; G3V9R8; -.
DR jPOST; G3V9R8; -.
DR PaxDb; G3V9R8; -.
DR PeptideAtlas; G3V9R8; -.
DR PRIDE; G3V9R8; -.
DR RGD; 1309982; Hnrnpc.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_079090_0_0_1; -.
DR PhylomeDB; G3V9R8; -.
DR TreeFam; TF330974; -.
DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-RNO-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-RNO-9013422; RHOBTB1 GTPase cycle.
DR PRO; PR:G3V9R8; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; G3V9R8; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:1990826; C:nucleoplasmic periphery of the nuclear pore complex; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0045120; C:pronucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005681; C:spliceosomal complex; ISS:HGNC-UCL.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISO:RGD.
DR GO; GO:1990827; F:deaminase binding; IPI:RGD.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; IDA:RGD.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; ISS:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IPI:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:RGD.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISO:RGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0090367; P:negative regulation of mRNA modification; IDA:RGD.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:RGD.
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 1: Evidence at protein 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..298
FT /note="Heterogeneous nuclear ribonucleoprotein C"
FT /id="PRO_0000432125"
FT DOMAIN 16..87
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 204..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 176..211
FT /evidence="ECO:0000255"
FT MOTIF 142..148
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 221..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..298
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 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z204"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 163
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z204"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z204"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 298
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 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 236
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 243
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07910"
FT CROSSLNK 243
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07910"
SQ SEQUENCE 298 AA; 32857 MW; F4D2F4A6E3F85479 CRC64;
MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK GFAFVQYVNE
RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS AAEMYGSSFD LDYDFQRDYY
DRMYSYPARV PPPPPIARAV VPSKRQRVSG NTSRRGKSGF NSKSGQRGSS SKSVKGDDLQ
AIKKELTQIK QKVDSLLESL EKIEKEQSKQ ADLSFSSPVE MKNEKSEEEQ SSASVKKDET
NVKMESEAGA DDSAEEGDLL DDDDNEDRGD DQLELKDDEK EPEEGEDDRD SANGEDDS
