ZN541_MOUSE
ID ZN541_MOUSE Reviewed; 1363 AA.
AC Q0GGX2; B2RXS6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Zinc finger protein 541;
DE AltName: Full=Spermatogenic cell HDAC-interacting protein 1 {ECO:0000303|PubMed:18849567};
GN Name=Znf541; Synonyms=Ship1 {ECO:0000303|PubMed:17662146}, Zfp541;
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), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=ICR; TISSUE=Testis;
RX PubMed=17662146; DOI=10.1186/1471-2164-8-256;
RA Choi E., Lee J., Oh J., Park I., Han C., Yi C., Kim D.H., Cho B.-N.,
RA Eddy E.M., Cho C.;
RT "Integrative characterization of germ cell-specific genes from mouse
RT spermatocyte UniGene library.";
RL BMC Genomics 8:256-256(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC 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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DNTTIP1, IDENTIFICATION IN
RP A COMPLEX WITH KCDT19; HDAC1 AND HSPA2, AND TISSUE SPECIFICITY.
RX PubMed=18849567; DOI=10.1074/jbc.m805590200;
RA Choi E., Han C., Park I., Lee B., Jin S., Choi H., Kim do H., Park Z.Y.,
RA Eddy E.M., Cho C.;
RT "A novel germ cell-specific protein, SHIP1, forms a complex with chromatin
RT remodeling activity during spermatogenesis.";
RL J. Biol. Chem. 283:35283-35294(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Component of some chromatin remodeling multiprotein complex
CC that plays a role during spermatogenesis.
CC {ECO:0000269|PubMed:18849567}.
CC -!- SUBUNIT: Interacts with DNTTIP1 (PubMed:18849567). Identified in a
CC complex with KCDT19, HDAC1 and HSPA2 (PubMed:18849567). Component of a
CC histone deacetylase complex containing DNTTIP1, ZNF541, HDAC1 and HDAC2
CC (By similarity). {ECO:0000250|UniProtKB:Q9H0D2,
CC ECO:0000269|PubMed:18849567}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:17662146,
CC ECO:0000269|PubMed:18849567}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0GGX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0GGX2-2; Sequence=VSP_036221;
CC -!- TISSUE SPECIFICITY: Germ-cell-specific. Specifically present in
CC testicular spermatogenic cells, but not in testicular and mature sperm.
CC During spermatogenesis, it is present in spermatocytes and round
CC spermatids only (at protein level). {ECO:0000269|PubMed:17662146,
CC ECO:0000269|PubMed:18849567}.
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DR EMBL; DQ864732; ABI17929.1; -; mRNA.
DR EMBL; BC157962; AAI57963.1; -; mRNA.
DR CCDS; CCDS39781.1; -. [Q0GGX2-1]
DR CCDS; CCDS90162.1; -. [Q0GGX2-2]
DR RefSeq; NP_001092747.1; NM_001099277.1. [Q0GGX2-1]
DR RefSeq; NP_001334488.1; NM_001347559.1. [Q0GGX2-2]
DR RefSeq; XP_006540359.1; XM_006540296.3. [Q0GGX2-2]
DR AlphaFoldDB; Q0GGX2; -.
DR SMR; Q0GGX2; -.
DR BioGRID; 578363; 3.
DR IntAct; Q0GGX2; 1.
DR MINT; Q0GGX2; -.
DR STRING; 10090.ENSMUSP00000104149; -.
DR iPTMnet; Q0GGX2; -.
DR PhosphoSitePlus; Q0GGX2; -.
DR PaxDb; Q0GGX2; -.
DR PRIDE; Q0GGX2; -.
DR ProteomicsDB; 299586; -. [Q0GGX2-1]
DR ProteomicsDB; 299587; -. [Q0GGX2-2]
DR Antibodypedia; 18215; 127 antibodies from 26 providers.
DR Ensembl; ENSMUST00000108509; ENSMUSP00000104149; ENSMUSG00000078796. [Q0GGX2-1]
DR Ensembl; ENSMUST00000209369; ENSMUSP00000147475; ENSMUSG00000078796. [Q0GGX2-1]
DR Ensembl; ENSMUST00000210805; ENSMUSP00000148143; ENSMUSG00000078796. [Q0GGX2-2]
DR GeneID; 666528; -.
DR KEGG; mmu:666528; -.
DR UCSC; uc009fgv.1; mouse. [Q0GGX2-1]
DR UCSC; uc012fab.1; mouse. [Q0GGX2-2]
DR CTD; 666528; -.
DR MGI; MGI:3647699; Zfp541.
DR VEuPathDB; HostDB:ENSMUSG00000078796; -.
DR eggNOG; KOG1721; Eukaryota.
DR eggNOG; KOG4167; Eukaryota.
DR GeneTree; ENSGT00940000160330; -.
DR HOGENOM; CLU_006052_0_0_1; -.
DR InParanoid; Q0GGX2; -.
DR OMA; SHHPTPE; -.
DR OrthoDB; 165439at2759; -.
DR PhylomeDB; Q0GGX2; -.
DR TreeFam; TF106431; -.
DR BioGRID-ORCS; 666528; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp541; mouse.
DR PRO; PR:Q0GGX2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q0GGX2; protein.
DR Bgee; ENSMUSG00000078796; Expressed in seminiferous tubule of testis and 12 other tissues.
DR Genevisible; Q0GGX2; MM.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Spermatogenesis; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1363
FT /note="Zinc finger protein 541"
FT /id="PRO_0000361545"
FT DOMAIN 1063..1155
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 1170..1221
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 140..162
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 168..190
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 196..221
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 838..860
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1301..1323
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1243..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 874..934
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036221"
FT CONFLICT 26
FT /note="V -> G (in Ref. 2; AAI57963)"
FT /evidence="ECO:0000305"
FT CONFLICT 1200
FT /note="M -> T (in Ref. 2; AAI57963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1363 AA; 148297 MW; BAE2FD52F1E72934 CRC64;
MEPYSLGEEG ALPSEGHLPS FSESQVLNCS DTLNRDLGPS TRDLLYAGLS GLDLDPSLST
SDMPSEVLED NLDTLSLYSG KDSDSVKLLE EYADSESQTS LQDLGLGALK VPKEADEGGR
ATGSTRKGKR QHSSPQNPLL DCSLCGKVFS SASSLSKHYL THSQERKHVC KVCSKAFKRQ
DHLTGHMLTH QKTKPFVCIE QGCSKSYCDY RSLRRHYEVQ HGVCILKETP PEEEAYGDPT
HNHDVANQPP PSGLRSLGPP EARSPGSVLP NRDLLRCIVS SIVHQKIPSP GPAVGPSDTE
ARSSACACPT SLGSSSCTPA STPVALGTLG SEIPEETHPP RKEAATEVFT PVQSRAAENG
VPDPPESELE SESPRLQRPS SLEGWPEGSS LPACLPLFRG HSVPSGSQPS SHNFQWLRNL
PGCPKNKGSN VFMVHKPPAV ASREGSEGGG SGPSSTPTSV EPSPSLGTTQ EELLPFPPAL
LKAPGEASSE VRQAAGEDET WAPKKCKPDC ESFPWQSPTE LGLQDAQNPG GLPSDATPLF
RQLFMKSQES LVSHEQMQVL QMIAKSQRIF SHTQVATASA QRPGPEGKQS TLKPLQGPWP
PQTLPPAPTV DSFQIGPGHS EPEGSPVRRR KTMPAVSRET SPGGPRRDTK GGPKVASAPP
SLTGPGLLPS RNPDSSSLAK GTLDLGDIIP NAGSRQSQLG GDEPAGTQLV GKQGQGENGL
ASGAMRGEKG PACPRGGGYR LFSGHPRAQR FSGFRKEKVK MDVCCAASPS QVAMASFSSA
GPLADPPRDM KSKLTIFNRI QGGNIYRLPH PVKEESLAGG CHQPNGGPTD WMESKSTFVC
KNCSQMFYTE KGLSSHMCFH SDQWPSPRGK QEQQVKGQMV ASVKRKAGRE EGAVEDMKRH
YDCSSSEPQD VTILSMLVSS GSCGVTPVVL SSLLQGQEKD GEERDSKESC QYRKRKKRPQ
PKALFAPPAP SALGEPGPGG CHQSCLHSPV FLVDHLLKGL FQCSPYTPPP MLSPIREGSG
LYFNTLCSTS RAGPHLISPV LDQVDSSFGI CVVKDDTKIS IEPHINVGSR FQAEIPELQE
RLLARVDENV ASLVWKPWGD VMTNPETQDR VMELCNVACS SVMPGGGTNL ELALHCLHDA
QGSVQVALET LLLRGPQKPR THPLADYRYT GSDIWTPMEK RLFKKAFCAH KKDFYLIHKM
IQTKSVAQCV EYYYIWKKMV KFDCGRAPGL EKRGRRELDE VERTEDKVTC SPRERPTHRP
TPELKIKTKS YRRESILHSS PSAAPKRTPE PPGSVESQGV FPCRECERVF DKIKSRNAHM
KRHRLQEHVE PVRVKWPVKP YPLKEEEEEE EEELGADMGP LQW
