ID   ZN365_MOUSE             Reviewed;         408 AA.
AC   Q8BG89; Q80TQ4; Q8BK39; Q8BXT2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Protein ZNF365;
DE   AltName: Full=DISC1-binding zinc-finger protein {ECO:0000303|PubMed:23912123};
DE   AltName: Full=Su48;
GN   Name=Znf365;
GN   Synonyms=Dbz {ECO:0000303|PubMed:23912123}, Kiaa0844, Zfp365;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=15363853; DOI=10.1016/j.gene.2004.06.030;
RA   Gianfrancesco F., Esposito T., Casu G., Maninchedda G., Roberto R.,
RA   Parastu M.;
RT   "Emergence of talanin protein associated with human uric acid
RT   nephrolithiasis in the hominidae lineage.";
RL   Gene 339:131-138(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=16617106; DOI=10.1073/pnas.0601682103;
RA   Wang Q., Du X., Meinkoth J., Hirohashi Y., Zhang H., Liu Q., Richter M.,
RA   Greene M.I.;
RT   "Characterization of Su48, a centrosome protein essential for cell
RT   division.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6512-6517(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-139; SER-146 AND
RP   THR-176, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   FUNCTION.
RX   PubMed=23776040; DOI=10.1158/2159-8290.cd-12-0536;
RA   Zhang Y., Shin S.J., Liu D., Ivanova E., Foerster F., Ying H., Zheng H.,
RA   Xiao Y., Chen Z., Protopopov A., Depinho R.A., Paik J.H.;
RT   "ZNF365 promotes stability of fragile sites and telomeres.";
RL   Cancer Discov. 3:798-811(2013).
RN   [8]
RP   INDUCTION BY GAMMA IRRADIATION.
RX   PubMed=23966166; DOI=10.4161/cc.25882;
RA   Zhang Y., Park E., Kim C.S., Paik J.H.;
RT   "ZNF365 promotes stalled replication forks recovery to maintain genome
RT   stability.";
RL   Cell Cycle 12:2817-2828(2013).
RN   [9]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=23912123; DOI=10.1016/j.jchemneu.2013.07.002;
RA   Koyama Y., Hattori T., Shimizu S., Taniguchi M., Yamada K., Takamura H.,
RA   Kumamoto N., Matsuzaki S., Ito A., Katayama T., Tohyama M.;
RT   "DBZ (DISC1-binding zinc finger protein)-deficient mice display
RT   abnormalities in basket cells in the somatosensory cortices.";
RL   J. Chem. Neuroanat. 53:1-10(2013).
RN   [10]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25983680; DOI=10.3389/fnana.2015.00052;
RA   Koyama Y., Hattori T., Nishida T., Hori O., Tohyama M.;
RT   "Alterations in dendrite and spine morphology of cortical pyramidal neurons
RT   in DISC1-binding zinc finger protein (DBZ) knockout mice.";
RL   Front. Neuroanat. 9:52-52(2015).
CC   -!- FUNCTION: Contributes to genomic stability by preventing telomere
CC       dysfunction (PubMed:23776040). Involved in the morphogenesis of basket
CC       cells in the somatosensory cortex during embryogenesis
CC       (PubMed:23912123). Involved in the positive regulation of
CC       oligodendrocyte differentiation during postnatal growth
CC       (PubMed:24481677). Involved in dendritic arborization, morphogenesis of
CC       spine density dendrite, and establishment of postsynaptic dendrite
CC       density in cortical pyramidal neurons (PubMed:25983680). Involved in
CC       the 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 (By similarity).
CC       {ECO:0000250|UniProtKB:Q70YC5, ECO:0000269|PubMed:23776040,
CC       ECO:0000269|PubMed:23912123, ECO:0000269|PubMed:24481677,
CC       ECO:0000269|PubMed:25983680}.
CC   -!- SUBUNIT: Homodimer. 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}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=ZNF365a;
CC         IsoId=Q8BG89-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BG89-2; Sequence=VSP_016601, VSP_016602;
CC   -!- TISSUE SPECIFICITY: Detected in several tissues, with highest levels in
CC       brain. Also expressed during embryonic development. Expressed in
CC       cerebral cortex, hippocampus, striatum, inferior colliculus and
CC       thalamus (PubMed:23912123). {ECO:0000269|PubMed:15363853,
CC       ECO:0000269|PubMed:16617106, ECO:0000269|PubMed:23912123}.
CC   -!- DEVELOPMENTAL STAGE: In the embryo at day 14.5 post-coitum, expressed
CC       in the basal, medial and lateral ganglionic eminences of the cerebral
CC       cortex, but not in the caudal ganglionic eminence (PubMed:23912123).
CC       Expressed in the corpus callosum from postnatal day 7 (PD7) to PD56
CC       with a peak at PD14 (PubMed:24481677). {ECO:0000269|PubMed:23912123,
CC       ECO:0000269|PubMed:24481677}.
CC   -!- INDUCTION: Induced by gamma irradiation. {ECO:0000269|PubMed:23966166}.
CC   -!- DISRUPTION PHENOTYPE: Basket cells with reduced branches and short
CC       processes in the somatosensory cortex of adult knockout (KO) mice.
CC       Reduced expression of the gamma-aminobutyric acid-synthesizing enzymes
CC       Gad1 in the somatosensory cortex of KO mice (PubMed:23912123). Delayed
CC       myelination in the corpus callosum of KO mice during the postnatal
CC       period, but recovery by adulthood (PubMed:24481677). Decreased
CC       dendritic arborization and increased spine density dendrites in
CC       cortical pyramidal neurons of adult KO mice (PubMed:25983680).
CC       {ECO:0000269|PubMed:23912123, ECO:0000269|PubMed:24481677,
CC       ECO:0000269|PubMed:25983680}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65669.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ516033; CAD56774.1; -; mRNA.
DR   EMBL; AF543761; AAQ11828.1; -; mRNA.
DR   EMBL; AK122387; BAC65669.1; ALT_INIT; mRNA.
DR   EMBL; AK031846; BAC27578.1; -; mRNA.
DR   EMBL; AK033892; BAC28505.1; -; mRNA.
DR   EMBL; AK044322; BAC31866.1; -; mRNA.
DR   EMBL; AK077316; BAC36745.1; -; mRNA.
DR   EMBL; BC080272; AAH80272.1; -; mRNA.
DR   CCDS; CCDS23903.1; -. [Q8BG89-1]
DR   RefSeq; NP_848794.1; NM_178679.2. [Q8BG89-1]
DR   AlphaFoldDB; Q8BG89; -.
DR   SMR; Q8BG89; -.
DR   IntAct; Q8BG89; 2.
DR   STRING; 10090.ENSMUSP00000067197; -.
DR   iPTMnet; Q8BG89; -.
DR   PhosphoSitePlus; Q8BG89; -.
DR   PaxDb; 10090-ENSMUSP00000067197; -.
DR   ProteomicsDB; 275285; -. [Q8BG89-1]
DR   ProteomicsDB; 275286; -. [Q8BG89-2]
DR   Antibodypedia; 28272; 446 antibodies from 20 providers.
DR   DNASU; 216049; -.
DR   Ensembl; ENSMUST00000064656.8; ENSMUSP00000067197.8; ENSMUSG00000037855.16. [Q8BG89-1]
DR   GeneID; 216049; -.
DR   KEGG; mmu:216049; -.
DR   UCSC; uc007fmb.1; mouse. [Q8BG89-1]
DR   UCSC; uc007fmc.1; mouse. [Q8BG89-2]
DR   AGR; MGI:2143676; -.
DR   CTD; 216049; -.
DR   MGI; MGI:2143676; Zfp365.
DR   VEuPathDB; HostDB:ENSMUSG00000037855; -.
DR   eggNOG; ENOG502QT88; Eukaryota.
DR   GeneTree; ENSGT00530000063713; -.
DR   HOGENOM; CLU_049609_0_0_1; -.
DR   InParanoid; Q8BG89; -.
DR   OMA; CGDRTRF; -.
DR   OrthoDB; 4513996at2759; -.
DR   PhylomeDB; Q8BG89; -.
DR   TreeFam; TF329439; -.
DR   BioGRID-ORCS; 216049; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Zfp365; mouse.
DR   PRO; PR:Q8BG89; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q8BG89; Protein.
DR   Bgee; ENSMUSG00000037855; Expressed in retrosplenial region and 139 other cell types or tissues.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0021687; P:cerebellar molecular layer morphogenesis; IMP:UniProtKB.
DR   GO; GO:0140059; P:dendrite arborization; IMP:UniProtKB.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; IMP:UniProtKB.
DR   GO; GO:0033566; P:gamma-tubulin complex localization; ISO:MGI.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISO:MGI.
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; IMP:UniProtKB.
DR   PANTHER; PTHR15739:SF2; PROTEIN ZNF365; 1.
DR   PANTHER; PTHR15739; ZINC FINGER PROTEIN; 1.
DR   Genevisible; Q8BG89; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Metal-binding;
KW   Neurogenesis; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..408
FT                   /note="Protein ZNF365"
FT                   /id="PRO_0000076375"
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:0007744|PubMed:21183079"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         176
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         370
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PQS2"
FT   VAR_SEQ         310..332
FT                   /note="LTDIPSNRKPRCLSRGHQHSVCN -> VSPLPVSHPMAPPEYSQNEPRQS
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_016601"
FT   VAR_SEQ         333..408
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_016602"
FT   CONFLICT        97
FT                   /note="S -> P (in Ref. 2; AAQ11828, 3; BAC65669 and 4;
FT                   BAC31866)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        309
FT                   /note="Missing (in Ref. 3; BAC65669)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        336
FT                   /note="M -> L (in Ref. 2; AAQ11828, 3; BAC65669 and 4;
FT                   BAC31866)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   408 AA;  46860 MW;  B4E18F21EC340E26 CRC64;
     MQQTTFEESR YHWQDSLENV AVCLPFRCPR CGDHTRFRSL SSLRAHLEFS HSYEERTLLT
     KCSLLPSLKD TELLRSSELP KQGKVLRGHA KVTKQKSSYV NLYSISHGHS KDTKPFEMVA
     ERPVSYVQTY TAVDIRADSL DAPCASPGLP TQDTKAAFEA HVREKFNRMV EAVDRTIEKR
     IDKLTKELAQ KTAELLEVRA AFAQLTQKKQ EVQRRERALN KQVDVAVEMI AVLKQRLTES
     EEELLRKEEE VVTFNHFLEA AAEKEVQGKA RLQDFIENLL QRVELAEKQL EYYQSQQASG
     FSCDTSEHML TDIPSNRKPR CLSRGHQHSV CNHPEMRAHF HLKGRSYLKK AKDERAGMQP
     AKAIHEPAES PREFFRPAKK GEHLGLSRKG NFRPKMAKKK PTAIVNII
//