ZN365_MOUSE
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 03-AUG-2022, entry version 123.
DE RecName: Full=Protein ZNF365;
DE AltName: Full=DISC1-binding zinc-finger protein {ECO:0000303|PubMed:23912123};
DE AltName: Full=Su48;
GN Name=Znf365; 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; Q8BG89; -.
DR PRIDE; Q8BG89; -.
DR ProteomicsDB; 275285; -. [Q8BG89-1]
DR ProteomicsDB; 275286; -. [Q8BG89-2]
DR Antibodypedia; 28272; 428 antibodies from 20 providers.
DR DNASU; 216049; -.
DR Ensembl; ENSMUST00000064656; ENSMUSP00000067197; ENSMUSG00000037855. [Q8BG89-1]
DR GeneID; 216049; -.
DR KEGG; mmu:216049; -.
DR UCSC; uc007fmb.1; mouse. [Q8BG89-1]
DR UCSC; uc007fmc.1; mouse. [Q8BG89-2]
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; AKPHSFQ; -.
DR OrthoDB; 918236at2759; -.
DR PhylomeDB; Q8BG89; -.
DR TreeFam; TF329439; -.
DR BioGRID-ORCS; 216049; 2 hits in 73 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 137 other tissues.
DR Genevisible; Q8BG89; MM.
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.
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
