ASY1_ARATH
ID ASY1_ARATH Reviewed; 596 AA.
AC F4HRV8; Q9FYF5; Q9FYF6; Q9M6R5;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Meiosis-specific protein ASY1 {ECO:0000305};
DE AltName: Full=Protein ASYNAPTIC 1 {ECO:0000303|PubMed:10855496};
DE Short=AtASY1 {ECO:0000303|PubMed:22319460};
GN Name=ASY1 {ECO:0000303|PubMed:10855496};
GN OrderedLocusNames=At1g67370/At1g67380 {ECO:0000312|Araport:AT1G67370};
GN ORFNames=F1N21.19/F1N21.20 {ECO:0000312|EMBL:AAG00246.1,
GN ECO:0000312|EMBL:AAG00247.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=10855496; DOI=10.1007/s004120050413;
RA Caryl A.P., Armstrong S.J., Jones G.H., Franklin F.C.H.;
RT "A homologue of the yeast HOP1 gene is inactivated in the Arabidopsis
RT meiotic mutant asy1.";
RL Chromosoma 109:62-71(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=12186950; DOI=10.1242/jcs.00048;
RA Armstrong S.J., Caryl A.P., Jones G.H., Franklin F.C.;
RT "Asy1, a protein required for meiotic chromosome synapsis, localizes to
RT axis-associated chromatin in Arabidopsis and Brassica.";
RL J. Cell Sci. 115:3645-3655(2002).
RN [5]
RP FUNCTION.
RX PubMed=17785529; DOI=10.1101/gad.439007;
RA Sanchez-Moran E., Santos J.-L., Jones G.H., Franklin F.C.;
RT "ASY1 mediates AtDMC1-dependent interhomolog recombination during meiosis
RT in Arabidopsis.";
RL Genes Dev. 21:2220-2233(2007).
RN [6]
RP FUNCTION.
RX PubMed=18504359; DOI=10.1159/000121079;
RA Sanchez-Moran E., Osman K., Higgins J.D., Pradillo M., Cunado N.,
RA Jones G.H., Franklin F.C.;
RT "ASY1 coordinates early events in the plant meiotic recombination
RT pathway.";
RL Cytogenet. Genome Res. 120:302-312(2008).
RN [7]
RP INTERACTION WITH ASY3.
RX PubMed=22319460; DOI=10.1371/journal.pgen.1002507;
RA Ferdous M., Higgins J.D., Osman K., Lambing C., Roitinger E., Mechtler K.,
RA Armstrong S.J., Perry R., Pradillo M., Cunado N., Franklin F.C.;
RT "Inter-homolog crossing-over and synapsis in Arabidopsis meiosis are
RT dependent on the chromosome axis protein AtASY3.";
RL PLoS Genet. 8:E1002507-E1002507(2012).
CC -!- FUNCTION: Required for normal meiosis in male and female gametophytes.
CC Plays a crucial role in coordinating the activity of DMC1, a key member
CC of the homologous recombination machinery (PubMed:18504359). Acts at
CC the interface between the developing chromosome axes and the
CC recombination machinery to ensure DMC1-mediated interhomolog
CC recombination (PubMed:17785529). {ECO:0000269|PubMed:17785529,
CC ECO:0000269|PubMed:18504359}.
CC -!- SUBUNIT: Interacts with ASY3. {ECO:0000269|PubMed:22319460}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:12186950}. Nucleus
CC {ECO:0000269|PubMed:12186950}. Note=During interphase-early leptotene,
CC distributed as numerous punctuate foci throughout the chromatin. At
CC zygotene and pachytene, shows a continuous localization along
CC chromosomal axes. {ECO:0000269|PubMed:12186950}.
CC -!- DISRUPTION PHENOTYPE: Failure of the pairing of homologous chromosomes
CC during meiosis (asynapsis or non-homologous synapsis) in both male and
CC female gametophytes. {ECO:0000269|PubMed:10855496}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG00246.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At1g67370 and At1g67380.; Evidence={ECO:0000305};
CC Sequence=AAG00247.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At1g67370 and At1g67380.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF157556; AAF70826.1; -; mRNA.
DR EMBL; AC002130; AAG00246.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC002130; AAG00247.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34638.1; -; Genomic_DNA.
DR PIR; B96697; B96697.
DR RefSeq; NP_564896.1; NM_105405.1.
DR AlphaFoldDB; F4HRV8; -.
DR SMR; F4HRV8; -.
DR IntAct; F4HRV8; 5.
DR STRING; 3702.AT1G67370.1; -.
DR iPTMnet; F4HRV8; -.
DR PaxDb; F4HRV8; -.
DR PRIDE; F4HRV8; -.
DR ProteomicsDB; 246714; -.
DR EnsemblPlants; AT1G67370.1; AT1G67370.1; AT1G67370.
DR GeneID; 843058; -.
DR Gramene; AT1G67370.1; AT1G67370.1; AT1G67370.
DR KEGG; ath:AT1G67370; -.
DR Araport; AT1G67370; -.
DR TAIR; locus:2019569; AT1G67370.
DR eggNOG; KOG4652; Eukaryota.
DR HOGENOM; CLU_015787_0_0_1; -.
DR InParanoid; F4HRV8; -.
DR OMA; GDLMYMK; -.
DR OrthoDB; 1038689at2759; -.
DR PRO; PR:F4HRV8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HRV8; baseline and differential.
DR GO; GO:0000785; C:chromatin; IDA:TAIR.
DR GO; GO:0005694; C:chromosome; IDA:TAIR.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:TAIR.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:TAIR.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051026; P:chiasma assembly; IMP:TAIR.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IDA:TAIR.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0007130; P:synaptonemal complex assembly; ISS:TAIR.
DR Gene3D; 3.30.900.10; -; 1.
DR InterPro; IPR003511; HORMA_dom.
DR InterPro; IPR036570; HORMA_dom_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF02301; HORMA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF56019; SSF56019; 1.
DR PROSITE; PS50815; HORMA; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 1: Evidence at protein level;
KW Chromosome; Meiosis; Nucleus; Reference proteome.
FT CHAIN 1..596
FT /note="Meiosis-specific protein ASY1"
FT /id="PRO_0000438696"
FT DOMAIN 15..228
FT /note="HORMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
FT DOMAIN 351..449
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT REGION 235..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..298
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 386
FT /note="S -> P (in Ref. 1; AAF70826)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="Q -> H (in Ref. 1; AAF70826)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 67211 MW; 3D4E8D1B48D2E6D2 CRC64;
MVMAQKLKEA EITEQDSLLL TRNLLRIAIF NISYIRGLFP EKYFNDKSVP ALDMKIKKLM
PMDAESRRLI DWMEKGVYDA LQRKYLKTLM FSICETVDGP MIEEYSFSFS YSDSDSQDVM
MNINRTGNKK NGGIFNSTAD ITPNQMRSSA CKMVRTLVQL MRTLDKMPDE RTIVMKLLYY
DDVTPPDYEP PFFRGCTEDE AQYVWTKNPL RMEIGNVNSK HLVLTLKVKS VLDPCEDEND
DMQDDGKSIG PDSVHDDQPS DSDSEISQTQ ENQFIVAPVE KQDDDDGEVD EDDNTQDPAE
NEQQLARVKD WINSRHLDTL ELTDILANFP DISIVLSEEI MDQLVTEGVL SKTGKDMYIK
KRDKTPESEF TFVKEEADGQ ISPGKSVAPE DYLYMKALYH SLPMKYVTIT KLHNMLDGEA
NQTAVRKLMD RMTQEGYVEA SSNRRLGKRV IHSSLTEKKL NEVRKVLATD DMDVDVTETI
NKTNGPDAKV TADVSTCGGI HSIGSDFTRT KGRSGGMQQN GSVLSEQTIS KAGNTPISNK
AQPAASRESF AVHGGAVKEA ETVNCSQASQ DRRGRKTSMV REPILQYSKR QKSQAN