ID   NPL1B_XENLA             Reviewed;         393 AA.
AC   Q7ZY81; Q4U0Y5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Nucleosome assembly protein 1-like 1-B {ECO:0000250|UniProtKB:P55209, ECO:0000303|PubMed:7622566};
DE            Short=xNAP1L-B;
DE   AltName: Full=Nucleosome assembly protein 1 {ECO:0000303|PubMed:15928086};
DE            Short=NAP1 {ECO:0000303|PubMed:7622566};
DE            Short=xNAP-1 {ECO:0000303|PubMed:15928086, ECO:0000303|PubMed:7622566};
GN   Name=nap1l1-b; Synonyms=nap1-b;
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, ECO:0000312|EMBL:AAY43227.1}
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   [2] {ECO:0000305, ECO:0000312|EMBL:AAH43903.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH43903.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {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).
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:0000250|UniProtKB:Q4U0Y4, ECO:0000269|PubMed:15928086}.
CC   -!- SUBUNIT: Forms homomultimers (By similarity). Interacts with histone
CC       b4. Interacts with the B-type cyclins ccnb1 and ccnb2.
CC       {ECO:0000250|UniProtKB:Q4U0Y4, ECO:0000269|PubMed:15928086,
CC       ECO:0000269|PubMed:7622566}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q4U0Y4}. Nucleus
CC       {ECO:0000250|UniProtKB:Q4U0Y4}. Note=Cytoplasmic prior to the
CC       midblastula transition, becoming predominantly nuclear subsequently.
CC       {ECO:0000250|UniProtKB:Q4U0Y4}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:15928086}; Synonyms=p60B
CC       {ECO:0000312|EMBL:AAY43227.1};
CC         IsoId=Q7ZY81-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:15928086}; Synonyms=p56B
CC       {ECO:0000312|EMBL:AAY43228.1};
CC         IsoId=Q7ZY81-2; Sequence=VSP_052857;
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:7622566}.
CC   -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC       {ECO:0000255}.
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DR   EMBL; DQ020266; AAY43227.1; -; mRNA.
DR   EMBL; DQ020267; AAY43228.1; -; mRNA.
DR   EMBL; BC043903; AAH43903.1; -; mRNA.
DR   RefSeq; NP_001080547.1; NM_001087078.1. [Q7ZY81-1]
DR   RefSeq; XP_018106203.1; XM_018250714.1. [Q7ZY81-2]
DR   AlphaFoldDB; Q7ZY81; -.
DR   SMR; Q7ZY81; -.
DR   BioGRID; 98481; 1.
DR   IntAct; Q7ZY81; 2.
DR   DNASU; 380239; -.
DR   GeneID; 380239; -.
DR   KEGG; xla:380239; -.
DR   CTD; 380239; -.
DR   Xenbase; XB-GENE-6256560; nap1l1.L.
DR   OMA; NSAYNDE; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 380239; Expressed in spleen and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS: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; ISS: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; ISS:UniProtKB.
DR   GO; GO:0060215; P:primitive hemopoiesis; ISS: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   Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..393
FT                   /note="Nucleosome assembly protein 1-like 1-B"
FT                   /id="PRO_0000345635"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           274..280
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        12..29
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..375
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         383..393
FT                   /note="KAQNPAECKQQ -> V (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15928086"
FT                   /id="VSP_052857"
SQ   SEQUENCE   393 AA;  45516 MW;  E0EBC9D50FBADF44 CRC64;
     MANIDNKEQT ELDQQDMEDV EDVEEEETGE EANSKARQLT AQMMQNPQVL AALQERLDDL
     VGTPTGYIES LPKVVKRRVN ALKNLQVKCA QIEAKFYEEV HELERKYAAL YQPFFEKRSD
     IINASYEPTE EECEWKVDEE EDIAEDLKEK AKLEEEKKDE EKEDPKGIPE FWLTVFKNVD
     LLSDMVQEHD EPILKHLKDI KVKFSEAGQP MNFMLEFHFE PNEFFTNELL TKTYKMRSEP
     DESDPFSFDG PEIMGCTGCL IDWKKGKNVT LKTIKKKQKH KGRGTVRTVT KTVPNDSFFN
     FFSPPEVPEN GELDDDAEAI LTADFEIGHF LRERIIPRSV LYFTGEAIED DDDDYDEEGE
     EADDEEGEEE ADEDHDPDFD PKKAQNPAEC KQQ