NAP1_CANAL
ID NAP1_CANAL Reviewed; 435 AA.
AC Q5AAI8; A0A1D8PRQ7;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Nucleosome assembly protein 1 {ECO:0000305};
GN Name=NAP1; OrderedLocusNames=CAALFM_CR00320CA; ORFNames=orf19.7501;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17588813; DOI=10.1016/j.ijmm.2007.03.020;
RA Kusch H., Engelmann S., Bode R., Albrecht D., Morschhauser J., Hecker M.;
RT "A proteomic view of Candida albicans yeast cell metabolism in exponential
RT and stationary growth phases.";
RL Int. J. Med. Microbiol. 298:291-318(2008).
RN [5]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION, AND PHOSPHORYLATION
RP AT SER-16; THR-20; THR-24; SER-27; THR-29; SER-31; SER-35; THR-42; SER-46
RP AND THR-52.
RX PubMed=24496790; DOI=10.1128/mbio.00915-13;
RA Huang Z.X., Zhao P., Zeng G.S., Wang Y.M., Sudbery I., Wang Y.;
RT "Phosphoregulation of Nap1 plays a role in septin ring dynamics and
RT morphogenesis in Candida albicans.";
RL MBio 5:E00915-E00915(2014).
CC -!- FUNCTION: Acidic protein, which assembles histones into an octamer (By
CC similarity). Involved in the regulation of the localization and the
CC function of the septins during mitosis. {ECO:0000250|UniProtKB:P25293,
CC ECO:0000269|PubMed:24496790}.
CC -!- SUBUNIT: Component of the GIN4 complex which forms a ring at the bud
CC neck. {ECO:0000250|UniProtKB:P25293}.
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:24496790}. Bud tip
CC {ECO:0000269|PubMed:24496790}. Note=Has not been detected in the
CC nucleus. {ECO:0000269|PubMed:24496790}.
CC -!- PTM: Phosphorylation is cell cycle dependent and is important for its
CC bud neck localization. Phosphorylation is highest in newly collected G1
CC cells, declines when the cells are traversing through the G1 phase, and
CC reaches the lowest level around the time of bud emergence.
CC Phosphorylation increases and remains high through the rest of the cell
CC cycle until the beginning of the next one, when it decreases again.
CC Phosphorylation involves two septin ring-associated kinases, CLA4 and
CC GIN4, and its dephosphorylation occurs at the septin ring in a manner
CC dependent on the phosphatases PP2A and CDC14.
CC {ECO:0000269|PubMed:24496790}.
CC -!- DISRUPTION PHENOTYPE: Leads to constitutive filamentous growth and
CC abnormalities in both septin localization and organization. Exhibits
CC greatly reduced virulence in a mouse model of systemic candidiasis.
CC {ECO:0000269|PubMed:24496790}.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
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DR EMBL; CP017630; AOW30803.1; -; Genomic_DNA.
DR RefSeq; XP_718658.1; XM_713565.1.
DR AlphaFoldDB; Q5AAI8; -.
DR SMR; Q5AAI8; -.
DR STRING; 237561.Q5AAI8; -.
DR iPTMnet; Q5AAI8; -.
DR PRIDE; Q5AAI8; -.
DR GeneID; 3639714; -.
DR KEGG; cal:CAALFM_CR00320CA; -.
DR CGD; CAL0000200763; NAP1.
DR VEuPathDB; FungiDB:CR_00320C_A; -.
DR eggNOG; KOG1507; Eukaryota.
DR HOGENOM; CLU_038841_1_0_1; -.
DR InParanoid; Q5AAI8; -.
DR OMA; VSPITWK; -.
DR OrthoDB; 1216172at2759; -.
DR PHI-base; PHI:4045; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0005934; C:cellular bud tip; IEA:UniProtKB-SubCell.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0032168; C:hyphal septin ring; IDA:CGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
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 Phosphoprotein; Reference proteome.
FT CHAIN 1..435
FT /note="Nucleosome assembly protein 1"
FT /id="PRO_0000431680"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..358
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..421
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24496790"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24496790"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24496790"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24496790"
FT MOD_RES 29
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24496790"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24496790"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24496790"
FT MOD_RES 42
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24496790"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24496790"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24496790"
SQ SEQUENCE 435 AA; 49517 MW; 8DEBC86F18EF6573 CRC64;
MTEQPINTKK KNGDISKAPT PQNTPASVTN SYMRSKPPTV STIQESNNED GTGAAAAAGG
LANNPVLLSM IQGKLGDLVG KQSGYIDNLS KPVKNRVYGL KSLQLNQMKL EAQFQKELLE
LEKKFFAKYQ PLYVKRKQII NGELEPTVEE IEEGQQLEEE EKGIDKEDGE EEEEEEEDDE
EEDEQGIPGF WLTALENLST VSETITDRDS EVLSNLIDIR MEYLSTPGFQ LIFEFKPNDF
FENQTLTKTY HYQAELGYSG DFVYDHADGC EIRWKSKENN VTITIERRKQ RNKTTKQTRT
IEKLTPTESF FNFFDPPKPP KIKSEDDDND DKLQDKEEAN DDDEGEEGDE EDEELEARLE
LDYQLGEEIK DRLIPRAIDW FTGDAVDFDY PELEGEGDED EYSDEDGEGD SDDDDDDDDE
AAGSQKQPPP ECKQQ
