NP1L1_XENTR
ID NP1L1_XENTR Reviewed; 393 AA.
AC Q28EB4; Q6NVB1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Nucleosome assembly protein 1-like 1 {ECO:0000312|EMBL:AAH68215.1};
GN Name=nap1l1 {ECO:0000312|EMBL:AAH68215.1}; ORFNames=TNeu131c07.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAJ83249.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Neurula {ECO:0000312|EMBL:CAJ83249.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAJ83249.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=N6 {ECO:0000312|EMBL:AAI23976.1}, and
RC PopA {ECO:0000312|EMBL:AAI54890.1};
RC TISSUE=Spleen {ECO:0000312|EMBL:AAI23976.1}, and
RC Tail bud {ECO:0000312|EMBL:AAH68215.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:Q4U0Y4}.
CC -!- SUBUNIT: Forms homomultimers. Interacts with histone B4. Interacts with
CC the B-type cyclins ccnb1 and ccnb2 (By similarity).
CC {ECO:0000250|UniProtKB:Q4U0Y4}.
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;
CC IsoId=Q28EB4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q28EB4-2; Sequence=VSP_052858;
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:0000250|UniProtKB:Q4U0Y4}.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR848343; CAJ83249.1; -; mRNA.
DR EMBL; BC068215; AAH68215.1; -; mRNA.
DR EMBL; BC123975; AAI23976.1; -; mRNA.
DR EMBL; BC154889; AAI54890.1; -; mRNA.
DR RefSeq; NP_001001249.1; NM_001001249.2. [Q28EB4-2]
DR RefSeq; NP_001015984.1; NM_001015984.3. [Q28EB4-1]
DR AlphaFoldDB; Q28EB4; -.
DR SMR; Q28EB4; -.
DR STRING; 8364.ENSXETP00000054165; -.
DR PaxDb; Q28EB4; -.
DR DNASU; 407956; -.
DR GeneID; 407956; -.
DR KEGG; xtr:407956; -.
DR CTD; 4673; -.
DR Xenbase; XB-GENE-484197; nap1l1.
DR eggNOG; KOG1507; Eukaryota.
DR HOGENOM; CLU_038841_3_0_1; -.
DR InParanoid; Q28EB4; -.
DR OrthoDB; 1216172at2759; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000013323; Expressed in ovary and 31 other tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0030332; F:cyclin binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS: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; ISS: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:0001878; P:response to yeast; IEA:Ensembl.
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 2: Evidence at transcript 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"
FT /id="PRO_0000345636"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..165
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 141..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..377
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 6
FT /note="N -> KTKKKNAALS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_052858"
SQ SEQUENCE 393 AA; 45348 MW; D56E18CDA4B57749 CRC64;
MANIDNKEQT ELDQQDMEDV EDIEEEEAGE DANSKARQLT AQMMQNPQVL AALQERLDDL
VGTPTGYIES LPKVVKRRVN ALKNLQVKCA QIEAKFYEEV HELERKYAAL YQPLFDKRSD
IINATYEPTE EECEWKVDEE EDISGDLKDK AKLEEEKKDE EKEDPKGIPE FWLTVFKNVD
LLSDMVQEHD EPILKHLKDI KVKFSEAGQP MSFTLEFHFE PNDFFTNEVL TKTYKMRSEP
DESDPFSFDG PEIMGCTGCL IDWKKGKNVT LKTIKKKQKH KGRGTVRTVT KTVPNDSFFN
FFSPPEVPEN GELDDDAEAI LTADFEIGHF LRERIIPRSV LYFTGEAIED DDDDYDEEGE
EADDEEGEEE ADEDNDPDYE PKKDQNPAEC KQQ
