ZN365_RAT
ID ZN365_RAT Reviewed; 408 AA.
AC Q5PQS2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protein ZNF365;
DE AltName: Full=DISC1-binding zinc-finger protein {ECO:0000303|PubMed:17389905};
GN Name=Znf365; Synonyms=DBZ {ECO:0000303|PubMed:17389905}, Zfp365;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP INTERACTION WITH DISC1, AND TISSUE SPECIFICITY.
RX PubMed=17389905; DOI=10.1038/sj.mp.4001945;
RA Hattori T., Baba K., Matsuzaki S., Honda A., Miyoshi K., Inoue K.,
RA Taniguchi M., Hashimoto H., Shintani N., Baba A., Shimizu S., Yukioka F.,
RA Kumamoto N., Yamaguchi A., Tohyama M., Katayama T.;
RT "A novel DISC1-interacting partner DISC1-binding zinc-finger protein:
RT implication in the modulation of DISC1-dependent neurite outgrowth.";
RL Mol. Psychiatry 12:398-407(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-176 AND SER-370, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP FUNCTION.
RX PubMed=24481677; DOI=10.1002/glia.22636;
RA Shimizu S., Koyama Y., Hattori T., Tachibana T., Yoshimi T., Emoto H.,
RA Matsumoto Y., Miyata S., Katayama T., Ito A., Tohyama M.;
RT "DBZ, a CNS-specific DISC1 binding protein, positively regulates
RT oligodendrocyte differentiation.";
RL Glia 62:709-724(2014).
CC -!- FUNCTION: Involved in the positive regulation of oligodendrocyte
CC differentiation during postnatal growth (PubMed:24481677). Involved in
CC the morphogenesis of basket cells in the somatosensory cortex during
CC embryogenesis. Involved in dendritic arborization, morphogenesis of
CC spine density dendrite, and establishment of postsynaptic dendrite
CC density in cortical pyramidal neurons (By similarity). Involved in the
CC regulation of neurogenesis. Negatively regulates neurite outgrowth.
CC Involved in homologous recombination (HR) repair pathway. Required for
CC proper resolution of DNA double-strand breaks (DSBs) by HR. Is required
CC for recovery of stalled replication forks, and directly contributes to
CC genomic stability. Interacts with PARP1 and mediates MRE11-dependent
CC DNA end resection during replication fork recovery. Contributes to
CC genomic stability by preventing telomere dysfunction (By similarity).
CC {ECO:0000250|UniProtKB:Q70YC5, ECO:0000250|UniProtKB:Q8BG89,
CC ECO:0000269|PubMed:24481677}.
CC -!- SUBUNIT: Homodimers. Interacts with NDE1 and NDEL1 (By similarity).
CC Interacts with DISC1 (PubMed:17389905). Interacts with PARP1 (By
CC similarity). {ECO:0000250|UniProtKB:Q70YC5,
CC ECO:0000269|PubMed:17389905}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q70YC5}.
CC -!- TISSUE SPECIFICITY: Expressed in cerebral cortex, hippocampus,
CC olfactory tubercle and striatum. {ECO:0000269|PubMed:17389905}.
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DR EMBL; BC087056; AAH87056.1; -; mRNA.
DR RefSeq; NP_001020316.1; NM_001025145.1.
DR AlphaFoldDB; Q5PQS2; -.
DR SMR; Q5PQS2; -.
DR STRING; 10116.ENSRNOP00000054802; -.
DR iPTMnet; Q5PQS2; -.
DR PhosphoSitePlus; Q5PQS2; -.
DR PaxDb; Q5PQS2; -.
DR PRIDE; Q5PQS2; -.
DR GeneID; 499425; -.
DR KEGG; rno:499425; -.
DR UCSC; RGD:1565986; rat.
DR CTD; 216049; -.
DR RGD; 1565986; Zfp365.
DR VEuPathDB; HostDB:ENSRNOG00000000638; -.
DR eggNOG; ENOG502QT88; Eukaryota.
DR HOGENOM; CLU_049609_0_0_1; -.
DR InParanoid; Q5PQS2; -.
DR OMA; AKPHSFQ; -.
DR OrthoDB; 918236at2759; -.
DR PhylomeDB; Q5PQS2; -.
DR PRO; PR:Q5PQS2; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000638; Expressed in frontal cortex and 17 other tissues.
DR Genevisible; Q5PQS2; RN.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
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:0033566; P:gamma-tubulin complex localization; ISO:RGD.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP: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:0010975; P:regulation of neuron projection development; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Metal-binding; Neurogenesis;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..408
FT /note="Protein ZNF365"
FT /id="PRO_0000076377"
FT ZN_FING 26..51
FT /note="C2H2-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT COILED 170..298
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG89"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG89"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BG89"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 408 AA; 46968 MW; 6756159816AE504D CRC64;
MQQTTFEESR YRWQDSLENV AVCLPFRCPR CGDHTRFRSL SSLRAHLEFS HSYEERTLLT
KCSLLPSLKD TDLLRSSELP KQGKLLRGHA KVTKQKPSYV NLYSISHGHS KDPKPFEMVA
ERPVSYVQTY TAVDIRADSL DAPRSSSGLP TQDTKAAFEA HVREKFNRMV EAVDRTIEKR
IDKLTKELAQ KTAELLEVRA AFVQLTQKKQ EVQRRERALH KQVDVAVEMI AVLKQRLTES
EEELLRKEEE VVTFNHFLEA AAEKEVQGKA RLQDFIENLL QRVELAEKQL EYYQSQQASG
FSHDTSEHML TDISSSRKSR CLSRGHQHSV CNHPELKAHF HLKGRSYLKK AKDERAGMQP
AKAIHEQAES PREFFRPAKK GEHLGLSRKG NFRPKMAKKK PTAIVNII
