ID   NP1L1_PONAB             Reviewed;         391 AA.
AC   Q5R4D4;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Nucleosome assembly protein 1-like 1;
DE   Flags: Precursor;
GN   Name=NAP1L1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone chaperone that plays a role in the nuclear import of
CC       H2A-H2B and nucleosome assembly. Participates also in several important
CC       DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin
CC       remodeling which is essential for transcription-coupled nucleotide
CC       excision DNA repair. Stimulates also homologous recombination (HR) by
CC       RAD51 and RAD54 which is essential in mitotic DNA double strand break
CC       (DSB) repair (By similarity). Plays a key role in the regulation of
CC       embryonic neurogenesis (By similarity). Promotes the proliferation of
CC       neural progenitors and inhibits neuronal differentiation during
CC       cortical development (By similarity). Regulates neurogenesis via the
CC       modulation of RASSF10; regulates RASSF10 expression by promoting
CC       SETD1A-mediated H3K4 methylation at the RASSF10 promoter (By
CC       similarity). {ECO:0000250|UniProtKB:P28656,
CC       ECO:0000250|UniProtKB:P55209}.
CC   -!- SUBUNIT: Homodimer. The dimer binds strongly and sequentially to single
CC       and double H2A-H2B heterodimers. Interacts with ERCC6; this interaction
CC       increases ERCC6 processivity. Interacts with RAD54 (By similarity).
CC       Interacts with SETD1A (By similarity). {ECO:0000250|UniProtKB:P28656,
CC       ECO:0000250|UniProtKB:P55209}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P28656}.
CC       Melanosome {ECO:0000250|UniProtKB:P55209}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P28656}.
CC   -!- DOMAIN: The acidic domains are probably involved in the interaction
CC       with histones. {ECO:0000250}.
CC   -!- PTM: Polyglycylated by TTLL10 on glutamate residues, resulting in
CC       polyglycine chains on the gamma-carboxyl group. Both polyglutamylation
CC       and polyglycylation modifications can coexist on the same protein on
CC       adjacent residues, and lowering polyglycylation levels increases
CC       polyglutamylation, and reciprocally. {ECO:0000250|UniProtKB:P28656}.
CC   -!- PTM: Polyglutamylated by TTLL4 on glutamate residues, resulting in
CC       polyglutamate chains on the gamma-carboxyl group. Both
CC       polyglutamylation and polyglycylation modifications can coexist on the
CC       same protein on adjacent residues, and lowering polyglycylation levels
CC       increases polyglutamylation, and reciprocally.
CC       {ECO:0000250|UniProtKB:P28656}.
CC   -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC       {ECO:0000305}.
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DR   EMBL; CR861317; CAH93382.1; -; mRNA.
DR   RefSeq; NP_001126986.1; NM_001133514.1.
DR   AlphaFoldDB; Q5R4D4; -.
DR   SMR; Q5R4D4; -.
DR   STRING; 9601.ENSPPYP00000005453; -.
DR   GeneID; 100174009; -.
DR   KEGG; pon:100174009; -.
DR   CTD; 4673; -.
DR   eggNOG; KOG1507; Eukaryota.
DR   InParanoid; Q5R4D4; -.
DR   OrthoDB; 1216172at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
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   Acetylation; Cytoplasm; Isopeptide bond; Lipoprotein; Methylation;
KW   Neurogenesis; Nucleus; Phosphoprotein; Prenylation; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P55209"
FT   CHAIN           2..388
FT                   /note="Nucleosome assembly protein 1-like 1"
FT                   /id="PRO_0000236210"
FT   PROPEP          389..391
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P55209"
FT                   /id="PRO_0000396687"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..391
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        10..27
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..163
FT                   /note="Basic and 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   COMPBIAS        376..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P55209"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55209"
FT   MOD_RES         62
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P55209"
FT   MOD_RES         64
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P28656"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55209"
FT   MOD_RES         116
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P55209"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55209"
FT   MOD_RES         359
FT                   /note="5-glutamyl polyglycine"
FT                   /evidence="ECO:0000250|UniProtKB:P28656"
FT   MOD_RES         360
FT                   /note="5-glutamyl polyglycine"
FT                   /evidence="ECO:0000250|UniProtKB:P28656"
FT   MOD_RES         388
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000305"
FT   LIPID           388
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P55209"
SQ   SEQUENCE   391 AA;  45316 MW;  BBC9DDF9D00F6344 CRC64;
     MADIDNKEQS ELDQDLDDVE EVEEEETGEE TKIKARQLTV QMMQNPQILA ALQERLDGLV
     ETPTGYIESL PRVVKRRVNA LKNLQVKCAQ IEAKFYEEVH DLERKYAVLY QPLFDKRFEI
     INAIYEPTEE ECEWKPDEED EISEELKEKA KIEDEKKDEE KEDPKGIPEF WLTVFKNVDL
     LSDMVQEHDE PILKHLKDIK VKFSGAGQPM SFVLEFHFEP NEYFTNEVLT KTYRMRSEPD
     DSDPFSFDGP EIMGCTGCQI DWKKGKNVTL KTIKKKQKHK GRGTVRTVTK TVSNDSFFNF
     FAPPEVPESG DLDDDAEAIL AADFEIGHFL RERIIPRSVL YFTGEAIEDD DDDYDEEGEE
     ADEEGEEEGD EENDPDYDPK KDQNPAECKQ Q