HNRPF_BOVIN
ID HNRPF_BOVIN Reviewed; 414 AA.
AC Q5E9J1;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein F;
DE Short=hnRNP F;
DE Contains:
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein F, N-terminally processed;
GN Name=HNRNPF; Synonyms=HNRPF;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the heterogeneous nuclear ribonucleoprotein
CC (hnRNP) complexes which provide the substrate for the processing events
CC that pre-mRNAs undergo before becoming functional, translatable mRNAs
CC in the cytoplasm. Plays a role in the regulation of alternative
CC splicing events. Binds G-rich sequences in pre-mRNAs and keeps target
CC RNA in an unfolded state (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts with AGO1,
CC AGO2, TBP and TXNL4/DIM1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
CC -!- DOMAIN: The N-terminal RRM domains are responsible for recognizing the
CC G-tract of BCL-X RNA. {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
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DR EMBL; BT020929; AAX08946.1; -; mRNA.
DR EMBL; BC102955; AAI02956.1; -; mRNA.
DR RefSeq; NP_001014860.1; NM_001014860.3.
DR RefSeq; XP_005226302.1; XM_005226245.3.
DR RefSeq; XP_005226303.1; XM_005226246.3.
DR RefSeq; XP_005226304.1; XM_005226247.3.
DR RefSeq; XP_005226306.1; XM_005226249.3.
DR RefSeq; XP_005226307.1; XM_005226250.3.
DR RefSeq; XP_005226308.1; XM_005226251.3.
DR RefSeq; XP_005226309.1; XM_005226252.3.
DR RefSeq; XP_010818754.1; XM_010820452.2.
DR RefSeq; XP_010818755.1; XM_010820453.2.
DR RefSeq; XP_010818756.1; XM_010820454.2.
DR RefSeq; XP_010818757.1; XM_010820455.2.
DR RefSeq; XP_015316432.1; XM_015460946.1.
DR AlphaFoldDB; Q5E9J1; -.
DR SMR; Q5E9J1; -.
DR STRING; 9913.ENSBTAP00000011658; -.
DR PaxDb; Q5E9J1; -.
DR PeptideAtlas; Q5E9J1; -.
DR PRIDE; Q5E9J1; -.
DR Ensembl; ENSBTAT00000011658; ENSBTAP00000011658; ENSBTAG00000008853.
DR GeneID; 506917; -.
DR KEGG; bta:506917; -.
DR CTD; 3185; -.
DR VEuPathDB; HostDB:ENSBTAG00000008853; -.
DR eggNOG; KOG4211; Eukaryota.
DR GeneTree; ENSGT00940000157838; -.
DR HOGENOM; CLU_032003_1_0_1; -.
DR InParanoid; Q5E9J1; -.
DR OMA; GDACVIF; -.
DR OrthoDB; 603679at2759; -.
DR TreeFam; TF316157; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000008853; Expressed in blood and 104 other tissues.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR012996; Znf_CHHC.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF08080; zf-RNPHF; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Spliceosome; Ubl conjugation.
FT CHAIN 1..414
FT /note="Heterogeneous nuclear ribonucleoprotein F"
FT /id="PRO_0000253052"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT CHAIN 2..414
FT /note="Heterogeneous nuclear ribonucleoprotein F, N-
FT terminally processed"
FT /id="PRO_0000367113"
FT DOMAIN 11..90
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 111..188
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 289..366
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 81..86
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT REGION 179..184
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT REGION 355..360
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 16
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 20
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 52
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 75
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 116
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 120
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 150
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 173
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 294
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 298
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 326
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 349
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 2
FT /note="N-acetylmethionine; in Heterogeneous nuclear
FT ribonucleoprotein F, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q794E4"
FT MOD_RES 200
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2X1"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 224
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT CROSSLNK 72
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52597"
SQ SEQUENCE 414 AA; 45689 MW; 4B7466C5FA09F666 CRC64;
MMLGPEGGEG FVVKLRGLPW SCSVEDVQNF LSDCTIHDGV AGVHFIYTRE GRQSGEAFVE
LESEDDVKLA LKKDRESMGH RYIEVFKSHR TEMDWVLKHS GPNSADTAND GFVRLRGLPF
GCTKEEIIQF FSGLEIVPNG ITLPVDPEGK ITGEAFVQFA SQELAEKALG KHKERIGHRY
IEVFKSSQEE VRSYSDPPLK FMSVQRPGPY DRPGTARRYI GIVKQAGLER MRSGAYSAGY
GGYEEYSGLS DGYGFTTDLF GRDLSYCLSG MYDHRYGDGE FTVQSTTGHC VHMRGLPYKA
TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHEE AVAAMSKDRA NMQHRYIELF
LNSTTGASNG AYSSQMMQGM GVSTQSTYSG LESQSVSGCY GAGYGGQNSM GGYD
