PUB44_ARATH
ID PUB44_ARATH Reviewed; 801 AA.
AC Q9LM76; Q93YT4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=U-box domain-containing protein 44;
DE EC=2.3.2.27;
DE AltName: Full=Plant U-box protein 44;
DE AltName: Full=Protein SENESCENCE-ASSOCIATED E3 UBIQUITIN LIGASE 1;
DE AltName: Full=RING-type E3 ubiquitin transferase PUB44 {ECO:0000305};
GN Name=PUB44; Synonyms=SAUL1; OrderedLocusNames=At1g20780; ORFNames=F2D10.27;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY ORGANIZATION.
RX PubMed=14657406; DOI=10.1104/pp.103.029553;
RA Mudgil Y., Shiu S.-H., Stone S.L., Salt J.N., Goring D.R.;
RT "A large complement of the predicted Arabidopsis ARM repeat proteins are
RT members of the U-box E3 ubiquitin ligase family.";
RL Plant Physiol. 134:59-66(2004).
RN [5]
RP INTERACTION WITH SD129.
RX PubMed=18552232; DOI=10.1104/pp.108.123380;
RA Samuel M.A., Mudgil Y., Salt J.N., Delmas F., Ramachandran S., Chilelli A.,
RA Goring D.R.;
RT "Interactions between the S-domain receptor kinases and AtPUB-ARM E3
RT ubiquitin ligases suggest a conserved signaling pathway in Arabidopsis.";
RL Plant Physiol. 147:2084-2095(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP AAO3.
RX PubMed=19309463; DOI=10.1111/j.1365-313x.2009.03846.x;
RA Raab S., Drechsel G., Zarepour M., Hartung W., Koshiba T., Bittner F.,
RA Hoth S.;
RT "Identification of a novel E3 ubiquitin ligase that is required for
RT suppression of premature senescence in Arabidopsis.";
RL Plant J. 59:39-51(2009).
CC -!- FUNCTION: Functions as an E3 ubiquitin-protein ligase. Prevents
CC premature senescence probably by targeting proteins involved in this
CC process for degradation. Promotes the degradation of AAO3 and thus
CC represses abscisic acid (ABA) biosynthesis.
CC {ECO:0000269|PubMed:19309463}.
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 -!- SUBUNIT: Interacts with AAO3. Binds to SD129.
CC {ECO:0000269|PubMed:18552232, ECO:0000269|PubMed:19309463}.
CC -!- INTERACTION:
CC Q9LM76; Q8GY72: At5g03050/F15A17_80; NbExp=4; IntAct=EBI-4466572, EBI-4430930;
CC Q9LM76; Q9SL70: TCX6; NbExp=3; IntAct=EBI-4466572, EBI-1238421;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LM76-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LM76-2; Sequence=VSP_031883, VSP_031884;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, root vasculature and guard
CC cells. {ECO:0000269|PubMed:19309463}.
CC -!- DISRUPTION PHENOTYPE: Premature senescence under low light conditions
CC accompanied by enhanced ABA biosynthesis, accumulation of AAO3, and
CC reduced photosynthetic capacity. {ECO:0000269|PubMed:19309463}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
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DR EMBL; AC069251; AAF80621.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30021.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60921.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60922.1; -; Genomic_DNA.
DR EMBL; AY059775; AAL24123.1; -; mRNA.
DR EMBL; AY096753; AAM20387.1; -; mRNA.
DR RefSeq; NP_001323169.1; NM_001332466.1. [Q9LM76-1]
DR RefSeq; NP_001323170.1; NM_001332465.1. [Q9LM76-1]
DR RefSeq; NP_564125.2; NM_101930.4. [Q9LM76-1]
DR AlphaFoldDB; Q9LM76; -.
DR SASBDB; Q9LM76; -.
DR BioGRID; 23907; 3.
DR IntAct; Q9LM76; 2.
DR STRING; 3702.AT1G20780.1; -.
DR iPTMnet; Q9LM76; -.
DR PaxDb; Q9LM76; -.
DR PRIDE; Q9LM76; -.
DR ProteomicsDB; 226250; -. [Q9LM76-1]
DR EnsemblPlants; AT1G20780.1; AT1G20780.1; AT1G20780. [Q9LM76-1]
DR EnsemblPlants; AT1G20780.2; AT1G20780.2; AT1G20780. [Q9LM76-1]
DR EnsemblPlants; AT1G20780.3; AT1G20780.3; AT1G20780. [Q9LM76-1]
DR GeneID; 838668; -.
DR Gramene; AT1G20780.1; AT1G20780.1; AT1G20780. [Q9LM76-1]
DR Gramene; AT1G20780.2; AT1G20780.2; AT1G20780. [Q9LM76-1]
DR Gramene; AT1G20780.3; AT1G20780.3; AT1G20780. [Q9LM76-1]
DR KEGG; ath:AT1G20780; -.
DR Araport; AT1G20780; -.
DR TAIR; locus:2030462; AT1G20780.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_004912_0_0_1; -.
DR InParanoid; Q9LM76; -.
DR OMA; TGLCRLH; -.
DR PhylomeDB; Q9LM76; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LM76; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LM76; baseline and differential.
DR Genevisible; Q9LM76; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0070696; F:transmembrane receptor protein serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0090359; P:negative regulation of abscisic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010115; P:regulation of abscisic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0010380; P:regulation of chlorophyll biosynthetic process; IMP:TAIR.
DR GO; GO:0010271; P:regulation of chlorophyll catabolic process; IMP:TAIR.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.25.10.10; -; 3.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 8.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50176; ARM_REPEAT; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..801
FT /note="U-box domain-containing protein 44"
FT /id="PRO_0000322184"
FT DOMAIN 22..101
FT /note="U-box"
FT REPEAT 134..173
FT /note="ARM 1"
FT REPEAT 176..215
FT /note="ARM 2"
FT REPEAT 218..259
FT /note="ARM 3"
FT REPEAT 261..300
FT /note="ARM 4"
FT REPEAT 301..340
FT /note="ARM 5"
FT REPEAT 342..386
FT /note="ARM 6"
FT REPEAT 390..429
FT /note="ARM 7"
FT REPEAT 435..475
FT /note="ARM 8"
FT REPEAT 480..521
FT /note="ARM 9"
FT VAR_SEQ 376..383
FT /note="VSATILAN -> SGESAPSN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_031883"
FT VAR_SEQ 384..801
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_031884"
SQ SEQUENCE 801 AA; 88380 MW; 7288E943EEF50D96 CRC64;
MVGSSDGDQS DDSSHFERGV DHIYEAFICP LTKEVMHDPV TLENGRTFER EAIEKWFKEC
RDSGRPPSCP LTSQELTSTD VSASIALRNT IEEWRSRNDA AKLDIARQSL FLGNAETDIL
QALMHVRQIC RTIRSNRHGV RNSQLIHMII DMLKSTSHRV RYKALQTLQV VVEGDDESKA
IVAEGDTVRT LVKFLSHEPS KGREAAVSLL FELSKSEALC EKIGSIHGAL ILLVGLTSSN
SENVSIVEKA DRTLENMERS EEIVRQMASY GRLQPLLGKL LEGSPETKLS MASFLGELPL
NNDVKVLVAQ TVGSSLVDLM RSGDMPQREA ALKALNKISS FEGSAKVLIS KGILPPLIKD
LFYVGPNNLP IRLKEVSATI LANIVNIGYD FDKATLVSEN RVENLLHLIS NTGPAIQCKL
LEVLVGLTSC PKTVPKVVYA IKTSGAIISL VQFIEVREND DLRLASIKLL HNLSPFMSEE
LAKALCGTAG QLGSLVAIIS EKTPITEEQA AAAGLLAELP DRDLGLTQEM LEVGAFEKII
SKVFGIRQGD IKGMRFVNPF LEGLVRILAR ITFVFNKEAR AINFCREHDV ASLFLHLLQS
NGQDNIQMVS AMALENLSLE SIKLTRMPDP PPVNYCGSIF SCVRKPHVVN GLCKIHQGIC
SLRETFCLVE GGAVEKLVAL LDHENVKVVE AALAALSSLL EDGLDVEKGV KILDEADGIR
HILNVLRENR TERLTRRAVW MVERILRIED IAREVAEEQS LSAALVDAFQ NADFRTRQIA
ENALKHIDKI PNFSSIFPNI A
