ID   ZN365_PONAB             Reviewed;         407 AA.
AC   Q5R9L2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Protein ZNF365;
GN   Name=ZNF365;
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: Involved in the regulation of neurogenesis. Negatively
CC       regulates neurite outgrowth (By similarity). Involved in the
CC       morphogenesis of basket cells in the somatosensory cortex during
CC       embryogenesis. Involved in the positive regulation of oligodendrocyte
CC       differentiation during postnatal growth. Involved in dendritic
CC       arborization, morphogenesis of spine density dendrite, and
CC       establishment of postsynaptic dendrite density in cortical pyramidal
CC       neurons (By similarity). Involved in homologous recombination (HR)
CC       repair pathway. Required for proper resolution of DNA double-strand
CC       breaks (DSBs) by HR. Is required for recovery of stalled replication
CC       forks, and directly contributes to genomic stability. Interacts with
CC       PARP1 and mediates MRE11-dependent DNA end resection during replication
CC       fork recovery. Contributes to genomic stability by preventing telomere
CC       dysfunction (By similarity). {ECO:0000250|UniProtKB:Q70YC5,
CC       ECO:0000250|UniProtKB:Q8BG89}.
CC   -!- SUBUNIT: Homodimers. Interacts with NDE1 and NDEL1 (By similarity).
CC       Interacts with DISC1. Interacts with PARP1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q70YC5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250|UniProtKB:Q70YC5}.
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DR   EMBL; CR859375; CAH91548.1; -; mRNA.
DR   RefSeq; NP_001125908.1; NM_001132436.1.
DR   AlphaFoldDB; Q5R9L2; -.
DR   SMR; Q5R9L2; -.
DR   STRING; 9601.ENSPPYP00000002800; -.
DR   GeneID; 100172841; -.
DR   KEGG; pon:100172841; -.
DR   CTD; 22891; -.
DR   eggNOG; ENOG502QT88; Eukaryota.
DR   InParanoid; Q5R9L2; -.
DR   OrthoDB; 918236at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0021687; P:cerebellar molecular layer morphogenesis; ISS:UniProtKB.
DR   GO; GO:0140059; P:dendrite arborization; ISS:UniProtKB.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0110026; P:regulation of DNA strand resection involved in replication fork processing; ISS:UniProtKB.
DR   GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Metal-binding; Neurogenesis;
KW   Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..407
FT                   /note="Protein ZNF365"
FT                   /id="PRO_0000076376"
FT   ZN_FING         26..51
FT                   /note="C2H2-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          347..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          169..296
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        347..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BG89"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BG89"
FT   MOD_RES         175
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BG89"
FT   MOD_RES         369
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PQS2"
SQ   SEQUENCE   407 AA;  46506 MW;  99EF84DC0CD8B09F CRC64;
     MQQKAFEESR YPWQESFENV AVCLPFRCPR CGDHTRFRSL SSLRAHLEFS HSYEERTLLT
     KCSLFPSLKD TDLVTSSELL KPGKLQSSGN VVKQKPSYVN LYSISHEHSK DRKPFEVVAE
     RPVSYVQTYT AMDLRADSLD GPRSGPGLPT SDTKASFEAH VREKFNRMVE AVDRTIEKRI
     DKLTKELAQK TAELLEVRAA FVQLTQKKQE VQRRERALNR QVDVAVEMIA VLRQRLTESE
     EELLRKEEEV VTFNHFLEAA AEKEVQGKAR LQDFIENLVQ RVELAEKQLE YYQSQQASGF
     GHDLSGHVLT DISSNRKPKC LSRGHPHSVC NHSDLKAHFH PKGRNHLKKA KDDRASMQPA
     KAIHEQAESS RDLCRPPKKG ELLGFGRKGN IRPKMAKKKP TAIVNII