HNRPF_MACFA
ID HNRPF_MACFA Reviewed; 415 AA.
AC Q60HC3; Q4R950;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 87.
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; ORFNames=QflA-17741, QtsA-10715;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RA Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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; AB125204; BAD51992.1; -; mRNA.
DR EMBL; AB168246; BAE00371.1; -; mRNA.
DR RefSeq; NP_001270670.1; NM_001283741.1.
DR RefSeq; XP_005565111.1; XM_005565054.2.
DR RefSeq; XP_005565112.1; XM_005565055.2.
DR RefSeq; XP_005565114.1; XM_005565057.2.
DR RefSeq; XP_005565115.1; XM_005565058.2.
DR RefSeq; XP_005565116.1; XM_005565059.2.
DR RefSeq; XP_005565117.1; XM_005565060.2.
DR RefSeq; XP_005565118.1; XM_005565061.2.
DR RefSeq; XP_005565119.1; XM_005565062.2.
DR RefSeq; XP_005565120.1; XM_005565063.2.
DR RefSeq; XP_005565121.1; XM_005565064.2.
DR AlphaFoldDB; Q60HC3; -.
DR SMR; Q60HC3; -.
DR STRING; 9541.XP_005565111.1; -.
DR GeneID; 101867097; -.
DR KEGG; mcf:101867097; -.
DR CTD; 3185; -.
DR eggNOG; KOG4211; Eukaryota.
DR OrthoDB; 603679at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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; 2.
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..415
FT /note="Heterogeneous nuclear ribonucleoprotein F"
FT /id="PRO_0000081853"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52597"
FT CHAIN 2..415
FT /note="Heterogeneous nuclear ribonucleoprotein F, N-
FT terminally processed"
FT /id="PRO_0000367115"
FT DOMAIN 13..85
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 107
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"
FT CONFLICT 234
FT /note="S -> G (in Ref. 2; BAE00371)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="S -> A (in Ref. 2; BAE00371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 45718 MW; FB19A30625F469F6 CRC64;
MMLGPEGGEG FVVKLRGLPW SCSVEDVQNF LSDCTIHDGA AGVHFIYTRE GRQSGEAFVE
LGSEDDVKMA LKKDRESMGH RYIEVFKSHR TEMDWVLKHS GPNSADSAND GFVRLRGLPF
GCTKEEIVQF FSGLEIVPNG ITLPVDPEGK ITGEAFVQFA SQELAEKALG KHKERIGHRY
IEVFKSSQEE VRSYSDPPLK FMSVQRPGPY DRPGTARRYI GIVKQAGLER MRPSAYSTGY
GGYEEYSGLS DGYGFTTDLF GRDLSYCLSG MYDHRYGDSE FTVQSTTGHC VHMRGLPYKA
TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHEE AVAAMSKDRA NMQHRYIELF
LNSTTGASNG AYSSQVMQGM GVSSAQATYS GLESQSVSGC YGAGYSGQNS MGGYD
