ZMY15_MOUSE
ID ZMY15_MOUSE Reviewed; 736 AA.
AC Q8C0R7; Q3TAD1;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Zinc finger MYND domain-containing protein 15;
GN Name=Zmynd15;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP FUNCTION, INTERACTION WITH HDAC1; HDAC3; HDAC6 AND HDAC7, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20675388; DOI=10.1074/jbc.m110.116418;
RA Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A.,
RA Saunders L., Verdin E., Charo I.F.;
RT "Zmynd15 encodes a histone deacetylase-dependent transcriptional repressor
RT essential for spermiogenesis and male fertility.";
RL J. Biol. Chem. 285:31418-31426(2010).
CC -!- FUNCTION: Acts as a transcriptional repressor through interaction with
CC histone deacetylases (HDACs). May regulate haploid genes important for
CC spermiogenesis. {ECO:0000269|PubMed:20675388}.
CC -!- SUBUNIT: Interacts with HDAC1, HDAC3, HDAC6 and, to a lesser extent,
CC with HDAC7. {ECO:0000269|PubMed:20675388}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20675388}. Cytoplasm
CC {ECO:0000269|PubMed:20675388}. Note=In step 9-11 spermatids, shifts
CC from nucleus to cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C0R7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0R7-2; Sequence=VSP_042145, VSP_042146;
CC -!- TISSUE SPECIFICITY: Testis-specific. Expressed in pachytene
CC spermatocytes and all developing spermatids, but not in Sertoli, nor
CC Leydig cells (at protein level). {ECO:0000269|PubMed:20675388}.
CC -!- DEVELOPMENTAL STAGE: At the mRNA level, first detected in early
CC pachytene spermatocytes. At the protein level, first detected in step 2
CC round spermatids. Expression continuously increases thereafter and
CC peaks in spermatids at steps 7-9 (at protein level). Levels start to
CC decrease after step 9 and in step 9-11 elongating spermatids (at
CC protein level).
CC -!- DISRUPTION PHENOTYPE: Since CXCL16 and ZMYND15 genes overlap in their
CC 5'UTRs, CXCL16 knockout also disrupts the ZMYND15 gene. The double
CC knockout mice display severe depletion of late spermatids and are thus
CC infertile. This phenotype is probably due to ZMYND15, rather than
CC CXCL16, deficiency. {ECO:0000269|PubMed:20675388}.
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DR EMBL; AK029988; BAC26719.1; -; mRNA.
DR EMBL; AK171931; BAE42737.1; -; mRNA.
DR EMBL; AL596096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151086; AAI51087.1; -; mRNA.
DR CCDS; CCDS24949.1; -. [Q8C0R7-1]
DR CCDS; CCDS88182.1; -. [Q8C0R7-2]
DR RefSeq; NP_001025100.1; NM_001029929.3. [Q8C0R7-1]
DR RefSeq; NP_001335266.1; NM_001348337.1. [Q8C0R7-2]
DR AlphaFoldDB; Q8C0R7; -.
DR STRING; 10090.ENSMUSP00000048816; -.
DR PhosphoSitePlus; Q8C0R7; -.
DR PaxDb; Q8C0R7; -.
DR PRIDE; Q8C0R7; -.
DR ProteomicsDB; 275066; -. [Q8C0R7-1]
DR ProteomicsDB; 275067; -. [Q8C0R7-2]
DR Antibodypedia; 11307; 16 antibodies from 9 providers.
DR DNASU; 574428; -.
DR Ensembl; ENSMUST00000039093; ENSMUSP00000048816; ENSMUSG00000040829. [Q8C0R7-1]
DR Ensembl; ENSMUST00000108563; ENSMUSP00000104203; ENSMUSG00000040829. [Q8C0R7-2]
DR GeneID; 574428; -.
DR KEGG; mmu:574428; -.
DR UCSC; uc007juy.1; mouse. [Q8C0R7-1]
DR UCSC; uc007juz.1; mouse. [Q8C0R7-2]
DR CTD; 84225; -.
DR MGI; MGI:3603821; Zmynd15.
DR VEuPathDB; HostDB:ENSMUSG00000040829; -.
DR eggNOG; KOG2084; Eukaryota.
DR GeneTree; ENSGT00390000000527; -.
DR HOGENOM; CLU_022430_0_0_1; -.
DR InParanoid; Q8C0R7; -.
DR OMA; GEGPALM; -.
DR PhylomeDB; Q8C0R7; -.
DR TreeFam; TF336410; -.
DR BioGRID-ORCS; 574428; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Cxcl16; mouse.
DR PRO; PR:Q8C0R7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C0R7; protein.
DR Bgee; ENSMUSG00000040829; Expressed in spermatid and 73 other tissues.
DR ExpressionAtlas; Q8C0R7; baseline and differential.
DR Genevisible; Q8C0R7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR InterPro; IPR042989; ZMY15.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR47085; PTHR47085; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Differentiation; Metal-binding; Nucleus;
KW Reference proteome; Spermatogenesis; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..736
FT /note="Zinc finger MYND domain-containing protein 15"
FT /id="PRO_0000414854"
FT ZN_FING 307..353
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 70..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..717
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT VAR_SEQ 1..129
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042145"
FT VAR_SEQ 191
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042146"
FT CONFLICT 200
FT /note="C -> S (in Ref. 1; BAE42737)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 736 AA; 81604 MW; A1EEF8505FFDEE37 CRC64;
MEFVSGYRDE FLDFAALLFG WFRKFVAERG TMGTSLEGRW RQLESQIRRL PQDPALWVLH
VLPNRSVGIS LGQGAEPGPG PGLGASRLLG DEPPLHLRDL SPYVSFVSLE DGEEGEEEEE
DEEHGERPGM EKVEPQEGGE PAPPSKRFPQ EAKPAPESEV TQQEASREEG SREERPEDER
APEKRKGQKN AEAAPLHLSC LLLVTDEHGT ILGIDLLMDG AQGSVGQNPG TENLAPRAYA
LLCHSMACPM GSGDPRKPRQ LTVGDAHLHR ELESLVPRLG VKLAKTPMRT WGPRPGFTFA
SLRARTCHVC HKHSFEVKLT PCPQCSAVLY CGEACLQADW RRCPDDVSHR FWCPRLSAFM
ERVGELASLP FTYTAEVTSE TFNKEAFLAS RGLTRGYWTQ LSMLIPGPGA PRYPWGSTSS
LSCLLNGDPY QLLQGDGPAL MPPVPLEPPR SLFGSWQDYY TWRGLSLDSP MAVLLTYPLT
VYYVITHLVP QSFPELNIQN KQSLKIHVVE AGKEFDLVMV FWELLVLLPH VALELQFVGD
SLPPESDQQH FTMQRDGPEV SLRPGSGVSA RFNSGTKEKG GRRDLQIRVS ARPYHLLQGP
KPDLVIGFNS GFGLKDTWLS SLPRLQSLRV PAFFTESSEY GCVMDDQTMA VATGGGTSSP
QPNPFRSPFR LRAADNCMPW YCNAFIFHLV YKPPQGGTVR SAPGPAPRPP TPAAPPVPAR
RRRGEKKAAR GPRRRR
