ZFAN3_MOUSE
ID ZFAN3_MOUSE Reviewed; 227 AA.
AC Q497H0; Q8K230; Q8R2V7; Q8R3V1;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=AN1-type zinc finger protein 3;
DE AltName: Full=Testis-expressed protein 27;
GN Name=Zfand3; Synonyms=Tex27;
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 FVB/N; TISSUE=Embryo, Mammary gland, and Thymus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 5-227 (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RX PubMed=10366431; DOI=10.1006/excr.1999.4482;
RA de Luis O., Lopez-Fernandez L.A., del Mazo J.;
RT "Tex27, a gene containing a zinc-finger domain, is up-regulated during the
RT haploid stages of spermatogenesis.";
RL Exp. Cell Res. 249:320-326(1999).
RN [3]
RP PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=8703127; DOI=10.1007/s003359900210;
RA Lopez-Fernandez L.A., del Mazo J.;
RT "Characterization of genes expressed early in mouse spermatogenesis,
RT isolated from a subtractive cDNA library.";
RL Mamm. Genome 7:698-700(1996).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q497H0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q497H0-2; Sequence=VSP_017154;
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:8703127}.
CC -!- DEVELOPMENTAL STAGE: Preferentially expressed during the haploid stages
CC of spermatogenesis. {ECO:0000269|PubMed:10366431}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27161.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC024483; AAH24483.1; -; mRNA.
DR EMBL; BC027161; AAH27161.1; ALT_INIT; mRNA.
DR EMBL; BC034396; AAH34396.1; -; mRNA.
DR EMBL; BC083124; AAH83124.1; -; mRNA.
DR EMBL; BC100559; AAI00560.1; -; mRNA.
DR EMBL; X80437; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS28598.1; -. [Q497H0-2]
DR CCDS; CCDS89053.1; -. [Q497H0-1]
DR RefSeq; NP_683728.1; NM_148926.2. [Q497H0-2]
DR RefSeq; XP_006524090.1; XM_006524027.1.
DR AlphaFoldDB; Q497H0; -.
DR SMR; Q497H0; -.
DR iPTMnet; Q497H0; -.
DR PhosphoSitePlus; Q497H0; -.
DR EPD; Q497H0; -.
DR MaxQB; Q497H0; -.
DR PeptideAtlas; Q497H0; -.
DR PRIDE; Q497H0; -.
DR ProteomicsDB; 298515; -. [Q497H0-1]
DR ProteomicsDB; 298516; -. [Q497H0-2]
DR Antibodypedia; 15614; 194 antibodies from 23 providers.
DR DNASU; 21769; -.
DR Ensembl; ENSMUST00000057897; ENSMUSP00000063158; ENSMUSG00000044477. [Q497H0-2]
DR Ensembl; ENSMUST00000226208; ENSMUSP00000154782; ENSMUSG00000044477. [Q497H0-1]
DR GeneID; 21769; -.
DR KEGG; mmu:21769; -.
DR UCSC; uc008btp.1; mouse. [Q497H0-2]
DR UCSC; uc008btq.1; mouse. [Q497H0-1]
DR CTD; 60685; -.
DR MGI; MGI:1096572; Zfand3.
DR VEuPathDB; HostDB:ENSMUSG00000044477; -.
DR GeneTree; ENSGT00390000014679; -.
DR HOGENOM; CLU_102579_0_0_1; -.
DR InParanoid; Q497H0; -.
DR OMA; HDCEIDF; -.
DR OrthoDB; 1440530at2759; -.
DR PhylomeDB; Q497H0; -.
DR TreeFam; TF354281; -.
DR BioGRID-ORCS; 21769; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Zfand3; mouse.
DR PRO; PR:Q497H0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q497H0; protein.
DR Bgee; ENSMUSG00000044477; Expressed in seminiferous tubule of testis and 243 other tissues.
DR ExpressionAtlas; Q497H0; baseline and differential.
DR Genevisible; Q497H0; MM.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 4.10.1110.10; -; 1.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR002653; Znf_A20.
DR InterPro; IPR000058; Znf_AN1.
DR Pfam; PF01754; zf-A20; 1.
DR Pfam; PF01428; zf-AN1; 1.
DR SMART; SM00259; ZnF_A20; 1.
DR SMART; SM00154; ZnF_AN1; 1.
DR SUPFAM; SSF118310; SSF118310; 1.
DR PROSITE; PS51036; ZF_A20; 1.
DR PROSITE; PS51039; ZF_AN1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..227
FT /note="AN1-type zinc finger protein 3"
FT /id="PRO_0000076371"
FT ZN_FING 12..44
FT /note="A20-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT ZN_FING 151..200
FT /note="AN1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 41..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT VAR_SEQ 99..121
FT /note="CGPCTDTAHVSLITPTKRSCGAD -> Y (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017154"
SQ SEQUENCE 227 AA; 25081 MW; 98B3015F50D83E12 CRC64;
MGDAGSERSK APSLPPRCPC GFWGSSKTMN LCSKCFADFQ KKQPDDDSTP STSNSQSDLF
SEETTSDNNN TSVTTPTLSP SQQSLPTELN VTSPSTEECG PCTDTAHVSL ITPTKRSCGA
DSQSENEASP VKRPRLVENP ERPEESGRSK QKSRRRCFQC QTKLELVQQE LGSCRCGYVF
CMLHRLPEQH DCTFDHMGRG REEAIMKMVK LDRKVGRSCQ RIGEGCS
