ID   NUCL_XENLA              Reviewed;         651 AA.
AC   P20397;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Nucleolin;
DE   AltName: Full=Protein C23;
GN   Name=ncl;
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].
RC   TISSUE=Ovary;
RX   PubMed=8441611; DOI=10.1093/nar/21.1.169;
RA   Rankin M.L., Heine M.A., Xiao S., Leblanc M.D., Nelson J.W., Dimario P.J.;
RT   "A complete nucleolin cDNA sequence from Xenopus laevis.";
RL   Nucleic Acids Res. 21:169-169(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 126-651.
RX   PubMed=2656405; DOI=10.1101/gad.3.3.324;
RA   Caizergues-Ferrer M., Mariottini P., Curie C., Lapeyre B., Gas N.,
RA   Amalric F., Amaldi F.;
RT   "Nucleolin from Xenopus laevis: cDNA cloning and expression during
RT   development.";
RL   Genes Dev. 3:324-333(1989).
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.
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DR   EMBL; X63091; CAA44805.1; -; mRNA.
DR   PIR; S30250; S18874.
DR   AlphaFoldDB; P20397; -.
DR   SMR; P20397; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   CDD; cd12405; RRM3_NCL; 1.
DR   Gene3D; 3.30.70.330; -; 4.
DR   InterPro; IPR034234; Nucleolin_RRM3.
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; 4.
DR   SMART; SM00360; RRM; 4.
DR   SUPFAM; SSF54928; SSF54928; 4.
DR   PROSITE; PS50102; RRM; 4.
PE   2: Evidence at transcript level;
KW   DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; RNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..651
FT                   /note="Nucleolin"
FT                   /id="PRO_0000081696"
FT   DOMAIN          233..309
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          325..399
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          415..488
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          503..578
FT                   /note="RRM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..42
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..203
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         155
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        215
FT                   /note="P -> Q (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        219..220
FT                   /note="PE -> LR (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        411
FT                   /note="E -> Q (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        581
FT                   /note="D -> E (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   651 AA;  70196 MW;  4F0E972B7F0244ED CRC64;
     MVKLAKGAKT QAKPKKAAPP PPKDMEDSEE EEDMEEDDSS DEEVEVPVKK TPAKKTATPA
     KATPGKAATP GKKGATPAKN GKQAKKQESE EEEDDSDEEA EDQKPIKNKP VAKKAVAKKE
     ESEEDDDDED ESEEEKAVAK KPTPAKKPAG KKQESEEEDD EESEDEPMEV APALKGKKTA
     QAAEEDDEEE DDDDEEDDDD EEEQQGSAKR KKEMPKTIPE AKKTKTDTAS EGLSIFIGNL
     NSTKEFDELK DALREFFSKK NLTIQDIRIG NSKKFGYVDF SSEEEVEKAL KLTGKKILGT
     EVKIEKAMAF DKNKTAENKK ERDSRTLFVK NIPYSTTVEE LQEIFENAKD IRIPTGKDGS
     NKGIAYVEFS NEDEANKALE EKQGAEIEGR SIFVDFTGEK SQNSGNKKGP EGDSKVLVVN
     NLSYSATEDS LREVFEKATS IRIPQNQGRA KGFAFIEFSS AEDAKDAMDS CNNTEIEGRS
     IRLEFSQGGG PQGGGRGGSA QSKTLFVRGL SEDTTEETLK EAFDGSVNAR IVTDRDTGAS
     KGFGFVDFST AEDAKAAKEA MEDGEIDGNK VTLDFAKPKG DSQRGGRGGF GRGGGFRGGR
     GGRGGGGGRG FGGRGGGRGR GGFGGRGGGG FRGGQGGGFR GGQGKKMRFD D