NPL1A_XENLA
ID NPL1A_XENLA Reviewed; 392 AA.
AC Q4U0Y4; Q4U0Y3; Q6NUD1; Q9I8H9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Nucleosome assembly protein 1-like 1-A {ECO:0000250|UniProtKB:P55209, ECO:0000303|PubMed:16982648};
DE Short=xNAP1L-A;
DE AltName: Full=Nucleosome assembly protein 1 {ECO:0000312|EMBL:AAF86278.1};
DE Short=NAP-1 {ECO:0000312|EMBL:AAF86278.1};
DE Short=NAP1 {ECO:0000303|PubMed:7622566};
DE Short=xNAP-1 {ECO:0000303|PubMed:15928086, ECO:0000303|PubMed:16982648};
DE Short=xNAP1 {ECO:0000303|PubMed:16982648};
GN Name=nap1l1-a; Synonyms=nap1-a;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RC TISSUE=Gastrula {ECO:0000269|PubMed:14550533};
RX PubMed=14550533; DOI=10.1016/s0925-4773(03)00176-x;
RA Steer W.M., Abu-Daya A., Brickwood S.J., Mumford K.L., Jordanaires N.,
RA Mitchell J., Robinson C., Thorne A.W., Guille M.J.;
RT "Xenopus nucleosome assembly protein becomes tissue-restricted during
RT development and can alter the expression of specific genes.";
RL Mech. Dev. 120:1045-1057(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAY43229.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND INTERACTION
RP WITH B4.
RC TISSUE=Egg {ECO:0000269|PubMed:15928086};
RX PubMed=15928086; DOI=10.1073/pnas.0500822102;
RA Shintomi K., Iwabuchi M., Saeki H., Ura K., Kishimoto T., Ohsumi K.;
RT "Nucleosome assembly protein-1 is a linker histone chaperone in Xenopus
RT eggs.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8210-8215(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH68664.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary {ECO:0000312|EMBL:AAH68664.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH68664.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-392.
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAF86278.1};
RA Oliver C.J., Shenolikar S.;
RT "Identification of protein phosphatase-1 binding proteins in a Xenopus
RT laevis gastrula stage embryo library.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP PROTEIN SEQUENCE OF 38-43 AND 52-29, FUNCTION, MULTIMERIZATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16982648; DOI=10.1093/nar/gkl434;
RA Friedeberg C.E., Scarlett G., McGeehan J., Abu-Daya A., Guille M.J.,
RA Kneale G.;
RT "Identification of a structural and functional domain in xNAP1 involved in
RT protein-protein interactions.";
RL Nucleic Acids Res. 34:4893-4899(2006).
RN [6] {ECO:0000305}
RP INTERACTION WITH CCNB1 AND CCNB2, AND PHOSPHORYLATION.
RX PubMed=7622566; DOI=10.1083/jcb.130.3.661;
RA Kellogg D.R., Kikuchi A., Fujii-Nakata T., Turck C.W., Murray A.W.;
RT "Members of the NAP/SET family of proteins interact specifically with B-
RT type cyclins.";
RL J. Cell Biol. 130:661-673(1995).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=15811954; DOI=10.1182/blood-2005-02-0598;
RA Abu-Daya A., Steer W.M., Trollope A.F., Friedeberg C.E., Patient R.K.,
RA Thorne A.W., Guille M.J.;
RT "Zygotic nucleosome assembly protein-like 1 has a specific, non-cell
RT autonomous role in hematopoiesis.";
RL Blood 106:514-520(2005).
CC -!- FUNCTION: Acts as a chaperone for the linker histone to facilitate
CC deposition of histone B4 onto linker DNA. Required for both remodeling
CC of sperm chromatin into nucleosomes, and linker histone binding to
CC nucleosome core dimers. Plays a role in tissue-specific gene
CC regulation. Required for primitive hemopoiesis, acting upstream of
CC tal1/scl. {ECO:0000269|PubMed:14550533, ECO:0000269|PubMed:15811954,
CC ECO:0000269|PubMed:15928086, ECO:0000269|PubMed:16982648}.
CC -!- SUBUNIT: Forms homomultimers. Interacts with histone B4. Interacts with
CC the B-type cyclins ccnb1 and ccnb2. {ECO:0000269|PubMed:15928086,
CC ECO:0000269|PubMed:16982648, ECO:0000269|PubMed:7622566}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14550533}. Nucleus
CC {ECO:0000269|PubMed:14550533}. Note=Cytoplasmic prior to the
CC midblastula transition, becoming predominantly nuclear subsequently.
CC {ECO:0000269|PubMed:14550533}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:14550533, ECO:0000269|PubMed:15928086};
CC Synonyms=p60A {ECO:0000312|EMBL:AAY43229.1};
CC IsoId=Q4U0Y4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15928086}; Synonyms=p56A
CC {ECO:0000312|EMBL:AAY43230.1};
CC IsoId=Q4U0Y4-2; Sequence=VSP_052856;
CC -!- TISSUE SPECIFICITY: Initially expressed throughout the embryo with
CC expression higher at the animal pole. Becomes localized to presumptive
CC ectoderm by gastrula stages. By stage 18 (neurula), expressed in the
CC neural plate and posterior to the cement gland. In late neurula/early
CC tailbud stages, expressed in the neural crest, neural tube, eyes,
CC tailbud and ventral blood islands. Adult expression is predominantly in
CC ovaries. {ECO:0000269|PubMed:14550533}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expression levels remain constant during embryonic development,
CC increasing at the swimming tadpole stage.
CC {ECO:0000269|PubMed:14550533}.
CC -!- DOMAIN: The acidic domains are probably involved in the interaction
CC with histones. {ECO:0000250|UniProtKB:P55209}.
CC -!- PTM: Phosphorylated by cyclin B-cdc2 kinase complexes.
CC {ECO:0000269|PubMed:14550533, ECO:0000269|PubMed:7622566}.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF86278.1; Type=Miscellaneous discrepancy; Note=C-terminus does not match that of displayed sequence.; Evidence={ECO:0000305};
CC Sequence=AAH68664.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ020268; AAY43229.1; -; mRNA.
DR EMBL; DQ020269; AAY43230.1; -; mRNA.
DR EMBL; BC068664; AAH68664.1; ALT_FRAME; mRNA.
DR EMBL; AF278538; AAF86278.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001082010.1; NM_001088541.1.
DR AlphaFoldDB; Q4U0Y4; -.
DR SMR; Q4U0Y4; -.
DR BioGRID; 99511; 1.
DR PRIDE; Q4U0Y4; -.
DR DNASU; 398176; -.
DR GeneID; 398176; -.
DR KEGG; xla:398176; -.
DR CTD; 398176; -.
DR Xenbase; XB-GENE-484201; nap1l1.S.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 398176; Expressed in lung and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
DR GO; GO:0042393; F:histone binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0060215; P:primitive hemopoiesis; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR037231; NAP-like_sf.
DR InterPro; IPR002164; NAP_family.
DR PANTHER; PTHR11875; PTHR11875; 1.
DR Pfam; PF00956; NAP; 1.
DR SUPFAM; SSF143113; SSF143113; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Spermatogenesis; Transcription; Transcription regulation.
FT CHAIN 1..392
FT /note="Nucleosome assembly protein 1-like 1-A"
FT /id="PRO_0000345634"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 273..279
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 15..29
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..375
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 382..392
FT /note="KGQNPAECKQQ -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15928086"
FT /id="VSP_052856"
FT CONFLICT 3
FT /note="N -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="G -> E (in Ref. 1 and 3; AAH68664)"
FT /evidence="ECO:0000305"
FT CONFLICT 27..29
FT /note="ETG -> GTR (in Ref. 4; AAF86278)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="R -> G (in Ref. 3; AAH68664)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> N (in Ref. 1 and 4; AAF86278)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="E -> Q (in Ref. 1 and 4; AAF86278)"
FT /evidence="ECO:0000305"
FT CONFLICT 365..368
FT /note="EGEE -> FESR (in Ref. 1 and 4; AAF86278)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 45187 MW; 74960F50F2BA0E78 CRC64;
MANIDNKGQT ELDQQDMEDV EDVEEEETGE DANSKARQLT AQMMQNPQVL AALQERLDDL
VGTPTGYIES LPKVVKRRVN ALKNLQVKCA QIEAKFYEEV HELERKYAAL YQPLFDKRSD
IINATYEPTE EECEWKVEEE DISGDLKEKA KLEEEKKDEE KEDPKGIPEF WLTVFKNVDL
LSDMLQEHDE PILKHLKDIK VKFSDAGQPM SFTLEFYFEP NEFFTNEVLT KTYKMRSEPD
ESDPFSFDGP EIMGCTGCLI DWKKGKNVTL KTIKKKQKHK GRGTVRTVTK TVPNDSFFNF
FTPPEVPENG ELDDDAEAIL TADFEIGHFL RERIIPRSVL YFTGEAIEDD DDDYDEEGEE
ADDEEGEEEA DEDNDPDYEP KKGQNPAECK QQ
