NUCL_CHICK
ID NUCL_CHICK Reviewed; 694 AA.
AC P15771;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Nucleolin;
DE AltName: Full=Protein C23;
GN Name=NCL;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2320420; DOI=10.1093/nar/18.5.1286;
RA Maridor G., Nigg E.A.;
RT "cDNA sequences of chicken nucleolin/C23 and NO38/B23, two major nucleolar
RT proteins.";
RL Nucleic Acids Res. 18:1286-1286(1990).
RN [2]
RP DISCUSSION OF SEQUENCE.
RX PubMed=2114180; DOI=10.1016/0167-4781(90)90032-w;
RA Maridor G., Krek W., Nigg E.A.;
RT "Structure and developmental expression of chicken nucleolin and NO38:
RT coordinate expression of two abundant non-ribosomal nucleolar proteins.";
RL Biochim. Biophys. Acta 1049:126-133(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 407-694.
RX PubMed=2914325; DOI=10.1016/0092-8674(89)90241-9;
RA Borer R.A., Lehner C.F., Eppenberger H.M., Nigg E.A.;
RT "Major nucleolar proteins shuttle between nucleus and cytoplasm.";
RL Cell 56:379-390(1989).
RN [4]
RP PHOSPHORYLATION.
RX PubMed=2178776; DOI=10.1016/0092-8674(90)90093-t;
RA Peter M., Nakagawa J., Doree M., Labbe J.C., Nigg E.A.;
RT "Identification of major nucleolar proteins as candidate mitotic substrates
RT of cdc2 kinase.";
RL Cell 60:791-801(1990).
CC -!- FUNCTION: Nucleolin is the major nucleolar protein of growing
CC eukaryotic cells. It is found associated with intranucleolar chromatin
CC and pre-ribosomal particles. It induces chromatin decondensation by
CC binding to histone H1. It is thought to play a role in pre-rRNA
CC transcription and ribosome assembly.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC -!- PTM: Highly phosphorylated during mitosis.
CC {ECO:0000269|PubMed:2178776}.
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DR EMBL; X17199; CAA35060.1; -; mRNA.
DR EMBL; M21791; AAA48983.1; -; mRNA.
DR PIR; S08414; DNCHNL.
DR RefSeq; NP_990596.1; NM_205265.1.
DR AlphaFoldDB; P15771; -.
DR SMR; P15771; -.
DR BioGRID; 676461; 1.
DR STRING; 9031.ENSGALP00000032625; -.
DR PaxDb; P15771; -.
DR GeneID; 396201; -.
DR KEGG; gga:396201; -.
DR CTD; 4691; -.
DR VEuPathDB; HostDB:geneid_396201; -.
DR eggNOG; KOG0123; Eukaryota.
DR InParanoid; P15771; -.
DR OrthoDB; 1174365at2759; -.
DR PhylomeDB; P15771; -.
DR PRO; PR:P15771; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd12403; RRM1_NCL; 1.
DR CDD; cd12405; RRM3_NCL; 1.
DR CDD; cd12406; RRM4_NCL; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR034230; Nucleolin_RRM1.
DR InterPro; IPR034234; Nucleolin_RRM3.
DR InterPro; IPR034235; Nucleolin_RRM4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 3.
DR SUPFAM; SSF54928; SSF54928; 4.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding.
FT CHAIN 1..694
FT /note="Nucleolin"
FT /id="PRO_0000081695"
FT REPEAT 55..61
FT /note="1"
FT REPEAT 62..68
FT /note="2"
FT REPEAT 69..75
FT /note="3"
FT REPEAT 76..82
FT /note="4"
FT REPEAT 84..90
FT /note="5"
FT DOMAIN 281..357
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 371..445
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 461..535
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 553..628
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..90
FT /note="5 X 7 AA tandem repeats of X-T-P-X-K-K-X"
FT REGION 631..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..141
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..247
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CONFLICT 419
FT /note="A -> R (in Ref. 3; AAA48983)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="N -> T (in Ref. 3; AAA48983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 694 AA; 75640 MW; 7996C504BE9459A1 CRC64;
MVKLAKTPKN QMKQKKMAPP PKKVEESEEE ESSDLEESSG EEVMVPPKKQ QKAAVTPAKK
AATPAKKAAT PAKKAVTPAK KAVATPAKKA VAPSPKKAAV VGKGAKNGKN AKKEESEEED
EDDEDDEEDE DEEEESDEEE EPAVPVKPAA KKSAAAVPAK KPAVVPAKQE SEEEEEEDDE
EEDEEDDESE DEAMDTTPAP VKKPTPAKAT PAKAKAESED EEDEEDEDED EEDEDDEEED
EEESEDEKPV KEAPGKRKKE MANKSAPEAK KKKTETPASA FSLFVKNLTP TKDYEELRTA
IKEFFGKKNL QVSEVRIGSS KRFGYVDFLS AEDMDKALQL NGKKLMGLEI KLEKAKSKES
LKENKKERDA RTLFVKNLPY RVTEDEMKNV FENALEVRLV LNKEGSSKGM AYIEFKTEAE
AEKALEEKQG TEVDGRAMVI DYTGEKSQQE SQKGGGERES KTLIVNNLSY AASEETLQEL
FKKATSIKMP QNNQGRPKGY AFVEFPTAED AKEALNSCNN TEIEGRAIRL EFSSPSWQKG
NMNARGGFNQ QSKTLFVRGL SEDTTEETLR ESFEGSISAR IVTDRDTGSS KGFGFVDFSS
PEDAKAAKEA MEDGEIDGNK VTLDFAKPKG EFQRGGGFGG GFGGRGGRGG RGGGRGGFGG
RGGGRGFGGR GGGFRGGRGG GGDHKPQGKK IKFE
