ANO39_PATPE
ID ANO39_PATPE Reviewed; 346 AA.
AC Q9NLA3; Q8WSV9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Nucleoplasmin-like protein ANO39;
DE AltName: Full=39 kDa oocyte-expressed nucleolar protein;
DE AltName: Full=Nucleic acid-associated protein 36 {ECO:0000312|EMBL:BAA90827.1};
DE AltName: Full=Nucleic acid-binding nuclear protein {ECO:0000303|PubMed:10828953};
DE Short=NAAP {ECO:0000303|PubMed:10828953};
DE Short=NAAP1 {ECO:0000303|PubMed:10828953};
DE Short=NAAP2 {ECO:0000303|PubMed:10828953};
OS Patiria pectinifera (Starfish) (Asterina pectinifera).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC Valvatacea; Valvatida; Asterinidae; Patiria.
OX NCBI_TaxID=7594;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB82492.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-15; 20-81; 155-166;
RP 294-301; 304-312 AND 319-346, FUNCTION, SUBCELLULAR LOCATION, ACETYLATION
RP AT SER-2, PHOSPHORYLATION AT SER-145, VARIANT THR-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Ovary {ECO:0000269|PubMed:10828953};
RX PubMed=10828953; DOI=10.1021/bi992759x;
RA Matoba K., Matsumoto Y., Hongo T., Nagamatsu Y., Sugino H., Shimizu T.,
RA Takao T., Shimonishi Y., Ikegami S.;
RT "Chemical structure of nuclear proteins which are phosphorylated during
RT meiotic maturation of starfish oocytes.";
RL Biochemistry 39:6390-6400(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA90827.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-15; 55-81 AND 155-166,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP PHOSPHORYLATION AT SER-145, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovary {ECO:0000269|PubMed:10632699};
RX PubMed=10632699; DOI=10.1046/j.1432-1327.2000.00931.x;
RA Nakajima H., Matoba K., Matsumoto Y., Hongo T., Kiritaka K., Sugino H.,
RA Nagamatsu Y., Hamaguchi Y., Ikegami S.;
RT "Molecular characterization of a novel nucleolar protein in starfish
RT oocytes which is phosphorylated before and during oocyte maturation.";
RL Eur. J. Biochem. 267:295-304(2000).
CC -!- FUNCTION: Binds double-stranded RNA and both single-stranded and
CC double-stranded DNA. {ECO:0000269|PubMed:10828953}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10632699,
CC ECO:0000269|PubMed:10828953}. Cytoplasm {ECO:0000269|PubMed:10632699,
CC ECO:0000269|PubMed:10828953}. Note=In oocytes, expression is limited to
CC the germinal vesicle with highest levels in the nucleolus although a
CC considerable portion is present in other regions of the germinal
CC vesicle. In oocytes that progress to the first meiotic metaphase,
CC diffuse expression is observed throughout the egg cytoplasm.
CC {ECO:0000269|PubMed:10632699, ECO:0000269|PubMed:10828953}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the oocytes of the
CC ovaries. {ECO:0000269|PubMed:10632699}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally in immature oocytes at high
CC levels but is scarcely detectable in mature oocytes or in embryos at
CC the morula and blastula stages. {ECO:0000269|PubMed:10632699}.
CC -!- PTM: Phosphorylation occurs in oocytes during the progression of the
CC first meiotic M phase. No phosphorylation is observed in immature
CC oocytes. {ECO:0000269|PubMed:10632699, ECO:0000269|PubMed:10828953}.
CC -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000255}.
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DR EMBL; AB037176; BAB82492.1; -; mRNA.
DR EMBL; AB003034; BAA90827.1; -; mRNA.
DR AlphaFoldDB; Q9NLA3; -.
DR SMR; Q9NLA3; -.
DR iPTMnet; Q9NLA3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; NAS:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IEP:UniProtKB.
DR InterPro; IPR032569; NPM1_C.
DR InterPro; IPR004301; Nucleoplasmin.
DR InterPro; IPR024057; Nucleoplasmin_core_dom.
DR InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
DR PANTHER; PTHR22747; PTHR22747; 1.
DR Pfam; PF16276; NPM1-C; 1.
DR Pfam; PF03066; Nucleoplasmin; 1.
DR SUPFAM; SSF69203; SSF69203; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Glycoprotein; Nucleus; Phosphoprotein; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10828953"
FT CHAIN 2..346
FT /note="Nucleoplasmin-like protein ANO39"
FT /id="PRO_0000396520"
FT REGION 123..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..143
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..247
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10828953"
FT MOD_RES 145
FT /note="Phosphoserine; by CDC2"
FT /evidence="ECO:0000269|PubMed:10632699,
FT ECO:0000269|PubMed:10828953"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 52
FT /note="N -> T"
FT /evidence="ECO:0000269|PubMed:10828953"
SQ SEQUENCE 346 AA; 39005 MW; BA88FC06167E2FDC CRC64;
MSKEFFWGDS LTGTKKEVKW NPSLDDEDDF DNLDSDGIQH FLFLKQAVLG ANAKEGERNV
VEIETENFDG DNVKQPLFSL KLGLNESSPL DIGIQPPVTF ILTAGSGPVF LSGQHMIEIS
ADDEEELEED DEEEEEEDEV EVNASPDLPV AKSKKRPLST SDGTAKKTKM AKLDKDADKK
EDDDEEEDDE EEDEVMAMMD DDEDDEDDED FEGGEDDEEE DEEESDEDED DEDDNEEEEE
EDEDEESPEK PLKTTAKGKK GQMNGTTTAK GDNKPKAKAK TDTKLVKGKA KKKVLALDEI
KGKLQESSNV PKKEEKFKNY VRSAFHISEA KKLQDLWGWF RASLQK
