HEI10_ARATH
ID HEI10_ARATH Reviewed; 304 AA.
AC F4HRI2; Q9C8L1; Q9LPG5;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=E3 ubiquitin-protein ligase CCNB1IP1 homolog;
DE EC=2.3.2.27;
DE AltName: Full=RING finger-containing protein HEI10;
DE AltName: Full=RING-type E3 ubiquitin transferase HEI10 {ECO:0000305};
GN Name=HEI10; OrderedLocusNames=At1g53490; ORFNames=F22G10.16, T3F20.19;
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 [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 [2]
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 [3]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Wassilewskija-4;
RX PubMed=22844245; DOI=10.1371/journal.pgen.1002799;
RA Chelysheva L., Vezon D., Chambon A., Gendrot G., Pereira L., Lemhemdi A.,
RA Vrielynck N., Le Guin S., Novatchkova M., Grelon M.;
RT "The Arabidopsis HEI10 is a new ZMM protein related to Zip3.";
RL PLoS Genet. 8:E1002799-E1002799(2012).
CC -!- FUNCTION: Ubiquitin E3 ligase required for class I crossover (CO)
CC formation during meiosis. {ECO:0000269|PubMed:22844245}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22844245}. Chromosome
CC {ECO:0000269|PubMed:22844245}. Note=Dynamic localization on the meiotic
CC chromosomes. Present as numerous foci on the chromosome axes and the
CC synaptonemal complex central element until pachytene. From pachytene to
CC diakinesis, restricted to a limited number of sites that correspond to
CC class I crossovers.
CC -!- TISSUE SPECIFICITY: Expressed mostly in flower buds and roots.
CC {ECO:0000269|PubMed:22844245}.
CC -!- DISRUPTION PHENOTYPE: Normal vegetative growth but fertility defects
CC leading to reduced seed number per silique, due to abortion of male and
CC female gametophytes characterized by abnormal tetrahedral structure
CC becoming either asymmetric tetrads or polyads containing more than four
CC products, because of impaired class I crossover (CO) formation during
CC meiosis. {ECO:0000269|PubMed:22844245}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF78440.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51983.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC018748; AAF78440.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC024260; AAG51983.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32948.1; -; Genomic_DNA.
DR PIR; A96575; A96575.
DR RefSeq; NP_175754.2; NM_104227.2.
DR AlphaFoldDB; F4HRI2; -.
DR SMR; F4HRI2; -.
DR BioGRID; 27009; 2.
DR STRING; 3702.AT1G53490.1; -.
DR PaxDb; F4HRI2; -.
DR PRIDE; F4HRI2; -.
DR EnsemblPlants; AT1G53490.1; AT1G53490.1; AT1G53490.
DR GeneID; 841784; -.
DR Gramene; AT1G53490.1; AT1G53490.1; AT1G53490.
DR KEGG; ath:AT1G53490; -.
DR Araport; AT1G53490; -.
DR TAIR; locus:2024917; AT1G53490.
DR eggNOG; ENOG502RMFV; Eukaryota.
DR HOGENOM; CLU_052740_0_0_1; -.
DR InParanoid; F4HRI2; -.
DR OrthoDB; 1383870at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:F4HRI2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HRI2; baseline and differential.
DR Genevisible; F4HRI2; AT.
DR GO; GO:0005712; C:chiasma; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0051026; P:chiasma assembly; IMP:TAIR.
DR GO; GO:0035825; P:homologous recombination; IMP:TAIR.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF14634; zf-RING_5; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Coiled coil; DNA recombination; Meiosis; Metal-binding;
KW Nucleus; Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..304
FT /note="E3 ubiquitin-protein ligase CCNB1IP1 homolog"
FT /id="PRO_0000425730"
FT ZN_FING 3..42
FT /note="RING-type; degenerate"
FT REGION 218..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 124..184
FT /evidence="ECO:0000255"
FT COMPBIAS 233..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 304 AA; 34765 MW; 2595AC1B4B56E9D2 CRC64;
MRCNACWRDL EGRAISTTCG HLLCTEDASK ILSNDGACPI CDQVLSKSLM KPVDINPNEE
WINMAMAGIS PQILMKSAYR SVMFYIAQRD LEMQYKMNRV VAQCRQKCEG MQAKFSEKME
QVHTAYQKMG KRCQMMEQEV ENLTKDKQEL QEKFSEKSRQ KRKLDEMYDQ LRSEYESVKR
TAIQPANNFY PRHQEPDFFS NPAVNMMENR ETIRKDRSFF SPATPGPKDE IWPARQNSSN
SGPFDISTDS PAIPSDLGNR RAGRGHPVYG GGGTANPQST LRNLILSPIK RSQLSRSRPQ
LFTL