ANR31_MOUSE
ID ANR31_MOUSE Reviewed; 1857 AA.
AC A0A140LI88; A0A140LIB3;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 2.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Ankyrin repeat domain-containing protein 31 {ECO:0000305};
GN Name=Ankrd31 {ECO:0000312|MGI:MGI:5006716};
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 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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP INTERACTION WITH REC114, X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF
RP 1716-1765 IN COMPLEX WITH REC114, AND MUTAGENESIS OF 1818-TYR-LEU-1819;
RP GLU-1831 AND TRP-1842.
RX PubMed=31003867; DOI=10.1016/j.molcel.2019.03.023;
RA Boekhout M., Karasu M.E., Wang J., Acquaviva L., Pratto F., Brick K.,
RA Eng D.Y., Xu J., Camerini-Otero R.D., Patel D.J., Keeney S.;
RT "REC114 partner ANKRD31 controls number, timing, and location of meiotic
RT DNA breaks.";
RL Mol. Cell 0:0-0(2019).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH REC114 AND IHO1, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=31000436; DOI=10.1016/j.molcel.2019.03.022;
RA Papanikos F., Clement J.A.J., Testa E., Ravindranathan R., Grey C.,
RA Dereli I., Bondarieva A., Valerio-Cabrera S., Stanzione M., Schleiffer A.,
RA Jansa P., Lustyk D., Fei J.F., Adams I.R., Forejt J., Barchi M.,
RA de Massy B., Toth A.;
RT "Mouse ANKRD31 regulates spatiotemporal patterning of meiotic recombination
RT initiation and ensures recombination between X and Y sex chromosomes.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: Required for DNA double-strand breaks (DSBs) formation during
CC meiotic recombination (PubMed:31003867, PubMed:31000436). Regulates the
CC spatial and temporal patterns of pre-DSB recombinosome assembly and
CC recombination activity by acting as a scaffold that anchors REC114 and
CC other factors to specific genomic locations, thereby regulating DSB
CC formation (PubMed:31003867, PubMed:31000436). Plays a key role in
CC recombination in the pseudoautosomal regions of sex chromosomes
CC (PubMed:31000436). {ECO:0000269|PubMed:31000436,
CC ECO:0000269|PubMed:31003867}.
CC -!- SUBUNIT: Interacts with REC114; the interaction is direct
CC (PubMed:31003867, PubMed:31000436). Interacts with IHO1
CC (PubMed:31000436). {ECO:0000269|PubMed:31000436,
CC ECO:0000269|PubMed:31003867}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31000436}. Chromosome
CC {ECO:0000269|PubMed:31000436, ECO:0000269|PubMed:31003867}.
CC Note=Localizes on chromatin between preleptotene and early pachytene
CC (PubMed:31000436). Associates with the chromosome axes, but disappears
CC from axes upon synaptonemal complex formation (PubMed:31000436).
CC {ECO:0000269|PubMed:31000436}.
CC -!- TISSUE SPECIFICITY: Present in meiotic cells (at protein level).
CC {ECO:0000269|PubMed:31000436, ECO:0000269|PubMed:31003867}.
CC -!- DISRUPTION PHENOTYPE: Fertility defects (PubMed:31003867,
CC PubMed:31000436). Although female mice are fertile, they display
CC fertility defects faster than wild type in advanced age
CC (PubMed:31000436). Male mice are infertile (PubMed:31003867,
CC PubMed:31000436). Defects are caused by delayed recombination
CC initiation (PubMed:31000436). DNA double-strand breaks (DSBs)
CC distribution during meiosis is altered because of reduced selectivity
CC for sites that normally attract DSBs (PubMed:31000436). Spermatocytes
CC have altered DSB locations and fail to target DSBs to the
CC pseudoautosomal regions of sex chromosomes (PubMed:31003867,
CC PubMed:31000436). {ECO:0000269|PubMed:31000436,
CC ECO:0000269|PubMed:31003867}.
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DR EMBL; AC154851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC174082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006517860.1; XM_006517797.1.
DR PDB; 6NXF; X-ray; 2.79 A; U/V=1716-1765.
DR PDBsum; 6NXF; -.
DR AlphaFoldDB; A0A140LI88; -.
DR SMR; A0A140LI88; -.
DR PhosphoSitePlus; A0A140LI88; -.
DR ProteomicsDB; 318693; -.
DR ProteomicsDB; 361257; -.
DR MGI; MGI:5006716; Ankrd31.
DR ChiTaRS; Ankrd31; mouse.
DR PRO; PR:A0A140LI88; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; A0A140LI88; protein.
DR GO; GO:0000785; C:chromatin; IMP:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:UniProtKB.
DR GO; GO:0010780; P:meiotic DNA double-strand break formation involved in reciprocal meiotic recombination; IMP:UniProtKB.
DR GO; GO:1903343; P:positive regulation of meiotic DNA double-strand break formation; IMP:UniProtKB.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR042334; ANKRD31.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR040843; RAMA.
DR PANTHER; PTHR24176; PTHR24176; 2.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF18755; RAMA; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 5.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Chromosome; DNA recombination; Meiosis; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..1857
FT /note="Ankyrin repeat domain-containing protein 31"
FT /id="PRO_0000447624"
FT REPEAT 475..504
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 508..537
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 541..570
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 1162..1191
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 1195..1224
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 1228..1257
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT DOMAIN 1687..1782
FT /note="RAMA"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1457..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1552..1570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1665..1690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1818..1819
FT /note="YL->AA: Abolished interaction with REC114."
FT /evidence="ECO:0000269|PubMed:31003867"
FT MUTAGEN 1831
FT /note="E->A: Reduced interaction with REC114."
FT /evidence="ECO:0000269|PubMed:31003867"
FT MUTAGEN 1842
FT /note="W->A: Abolished interaction with REC114."
FT /evidence="ECO:0000269|PubMed:31003867"
FT STRAND 1813..1816
FT /evidence="ECO:0007829|PDB:6NXF"
FT HELIX 1817..1819
FT /evidence="ECO:0007829|PDB:6NXF"
FT STRAND 1823..1825
FT /evidence="ECO:0007829|PDB:6NXF"
FT HELIX 1829..1831
FT /evidence="ECO:0007829|PDB:6NXF"
FT HELIX 1835..1846
FT /evidence="ECO:0007829|PDB:6NXF"
FT HELIX 1848..1850
FT /evidence="ECO:0007829|PDB:6NXF"
FT TURN 1851..1854
FT /evidence="ECO:0007829|PDB:6NXF"
SQ SEQUENCE 1857 AA; 206173 MW; 2270A300D481A737 CRC64;
MENGAEASDC DSDETVIEGS VTENEPEDEE LPWRRLLLNQ DTTCRSEFCF HSGVDGMQKG
IHSPEIQLGL KLRKDSQEQN NKNKLLLALS EDLVLQDPQD KTAQNQVLLQ TTKEFPVFTV
SFPHPEVSWS HQNTGGHEAE NCENLPHSKK ELRENSDSPE VSLLSGTSPV APDLVALKER
LTEPVKTLAV PNTLSEPGEE VTQTMTSKET KDEESSLETF VSTLEKLLES SECTQEERLL
EVMDDFNPQE LFSTLSNSLG SVSVPLNAWA AQGRDELENK ADAALPAKLL AAVNTGADVG
PSCQGQEKSS SVSGGNGCLA VQPIMSQVDE DCTQIAQNIE DPKPFRLQTL THENAISYEQ
INKKKNSDPI KNTSTQETPR VLRRSSRLEK LKASRDVVHT EAVLKKPERI LSNTLSFKDQ
INSIFTTDSF SKRKNMHSSG FKNEQIRKSE QLRKKNGTGE MKKMCLCTIN RRNVFGENLL
YKAALHNDVD LVRCCIKNGE NVNQPSYDGW TALHEASIGG YYQAVSELLK GGADVNVKGK
YQITPLHDAV MNRHYKVAEL LLMSGADPLF RSDHGTCALD EAKDSSMETL LMKYIPQQKK
CHLSAQRNST DPAHVEDMFQ NKKPKLSSNN YTEFICDENF DRQEPGHLEI NKGSNNLLMS
KEYVCEHCQK DSNTTKFGKS NLNSVKNSRT NVSKRKGQKN RQQKKTQVDD RDCNLSQKIG
TSSFRRTNKL LTQQQHAVQT LSDLPEESFE LSTTTLSSLE NGIGYNEACL VSKKSDTHVL
DSSDGQELES VDQTEAASVS ELSSYKEIKL LPVTTHQQPH TNQEQYSSPY KSLGNNSSNE
KGKATNKWED SFFSFIKGRS ADSDSDCHTL DKSIASPKEG MSHDHHEEIM TGQEVDSQQR
LSSENYFSQE NDLKVHPLTT HPQEEAVNFC DSNLISVQHT PDYKNCLHEI SFGNSYAKTE
QSSTSCTRPP STQKVSPLTV EVELLKGLQD SLAHRDSSPL VNQAGIHSLE RKQDTDKNYT
KKGPNTSSSS RPLPTVVHSQ VIEITKAEKR REDLPGNEPI NNTDFYSTDI NKELANSSQL
NQRKEKENVR KSDAELTHND SEAERTLKSC EEKKKNMDSE THSPCDIQEH RKDQNFRKRK
CSLKAPCSQG VNTTGIGKRN KKGESQLHVA ARGGNLSRVK VLIEARADVN LRDNAGWTPL
HKAASGGFDD VIIELLQAGA NVNCENIDGI VPLHGASAGN HLKAAEILLE HGANPNQKDQ
KQRTALDEAD DEKMKELLKS YGAIESTNGE KRNSTDLVKI PTVQPKRYKQ FICDNDKAIG
SPVPSHKAKK SESLPVHQTI SAILQDIEEK QENLLKLEIR NSEDEEQYIG KMLEIKEVMD
NILAQQKTER DDLAKKYRVS MESFKHGALR EQLANLATRQ KSLLVVAKKQ KKIRLKIQNY
KNATAVSGVG LRKLPCNSDI SSDKKSQEPP TMGDSAHAQP GLLAPVSLAY GSMQEIPLSP
EIESESQKIN ICLNAEAIRR EEFSGNDINS KQNVQDCTLG GLLRSKPTDD AEKIASSSQP
AALTPHAENS QAEATVKGCG FDSSALTGTI NISEDKSIFS PNGACLAADP HSQKLSRCNP
KRRNKKTASQ QPSAGAAEPL PQAPAVLDTY TVHQTLPCLR DSAAAASHTD STQSSLSSAS
AHQHPTKTVP HRNTTPRKKA VQLKDLILRG RINPGNNILE FKTQETTHRA SVLPSGKLKG
ENGQIYQNPV TWLKELLGGG SYVTWNYAWN TVTYLGRELV KCVSEEAPMS AELNPPQLHQ
PHLSAGTSRE SMQTIPHYLQ IKEILQISKQ ELLPCHVMEQ HWKFYVGRSH SEALLSW
