ABAP1_ARATH
ID ABAP1_ARATH Reviewed; 737 AA.
AC B7U179; Q8RY88; Q9FYA4;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=ARMADILLO BTB ARABIDOPSIS PROTEIN 1;
DE Short=ABAP1;
GN Name=ABAP1; OrderedLocusNames=At5g13060; ORFNames=T19L5.20;
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], FUNCTION, IDENTIFICATION IN ABAP1-TCP24
RP COMPLEX, INTERACTION WITH ORC1A; ORC1B; CDT1A; CDT1B, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=18818695; DOI=10.1038/emboj.2008.191;
RA Masuda H.P., Cabral L.M., De Veylder L., Tanurdzic M.,
RA de Almeida Engler J., Geelen D., Inze D., Martienssen R.A., Ferreira P.C.,
RA Hemerly A.S.;
RT "ABAP1 is a novel plant Armadillo BTB protein involved in DNA replication
RT and transcription.";
RL EMBO J. 27:2746-2756(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-737.
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 [5]
RP DOMAIN BTB.
RX PubMed=15749712; DOI=10.1074/jbc.m413247200;
RA Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L.,
RA Vierstra R.D.;
RT "Cullins 3a and 3b assemble with members of the broad
RT complex/tramtrack/bric-a-brac (BTB) protein family to form essential
RT ubiquitin-protein ligases (E3s) in Arabidopsis.";
RL J. Biol. Chem. 280:18810-18821(2005).
RN [6]
RP INTERACTION WITH DUF7/AIP1.
RX PubMed=26538092; DOI=10.1186/s12870-015-0641-z;
RA Brasil J.N., Cabral L.M., Eloy N.B., Primo L.M., Barroso-Neto I.L.,
RA Grangeiro L.P., Gonzalez N., Inze D., Ferreira P.C., Hemerly A.S.;
RT "AIP1 is a novel Agenet/Tudor domain protein from Arabidopsis that
RT interacts with regulators of DNA replication, transcription and chromatin
RT remodeling.";
RL BMC Plant Biol. 15:270-270(2015).
CC -!- FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex (CUL3-RBX1-BTB) which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins (By similarity). In association with TCP24, exerts a negative
CC role in cell proliferation in leaves, possibly by inhibiting mitotic
CC DNA replication. {ECO:0000250, ECO:0000269|PubMed:18818695}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Forms a heterodimeric complex with TCP24 (PubMed:18818695).
CC Interacts with the origin recognition complex (preRC) components ORC1A,
CC ORC1B, CDT1A and CDT1B (PubMed:18818695). Interacts with DUF7/AIP1
CC (PubMed:26538092). {ECO:0000269|PubMed:18818695,
CC ECO:0000269|PubMed:26538092}.
CC -!- INTERACTION:
CC B7U179; Q9SJW9: CDT1A; NbExp=3; IntAct=EBI-541722, EBI-8079732;
CC B7U179; Q9M1S9: CDT1B; NbExp=2; IntAct=EBI-541722, EBI-8079764;
CC B7U179; Q710E8: ORC1A; NbExp=9; IntAct=EBI-541722, EBI-2651718;
CC B7U179; Q9SU24: ORC1B; NbExp=2; IntAct=EBI-541722, EBI-2114228;
CC B7U179; Q9C758: TCP24; NbExp=4; IntAct=EBI-541722, EBI-8079833;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18818695}.
CC -!- TISSUE SPECIFICITY: Weakly expressed in the emerging lateral roots and
CC mainly expressed in the shoot apex, young leaves and flower buds.
CC {ECO:0000269|PubMed:18818695}.
CC -!- DEVELOPMENTAL STAGE: Detected in developing leaves during proliferation
CC stage (9-day-old plants) and expression rapidly declines in leaves of
CC 13 till 21-day-old plants. Also expressed during stomatal cell
CC differentiation. {ECO:0000269|PubMed:18818695}.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC05434.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; FJ422582; ACJ46331.1; -; mRNA.
DR EMBL; AL391711; CAC05434.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91846.1; -; Genomic_DNA.
DR EMBL; AY074524; AAL69492.1; -; mRNA.
DR RefSeq; NP_196810.5; NM_121309.6.
DR AlphaFoldDB; B7U179; -.
DR SMR; B7U179; -.
DR BioGRID; 16423; 9.
DR IntAct; B7U179; 8.
DR MINT; B7U179; -.
DR STRING; 3702.AT5G13060.1; -.
DR PaxDb; B7U179; -.
DR PRIDE; B7U179; -.
DR ProteomicsDB; 244613; -.
DR EnsemblPlants; AT5G13060.1; AT5G13060.1; AT5G13060.
DR GeneID; 831145; -.
DR Gramene; AT5G13060.1; AT5G13060.1; AT5G13060.
DR KEGG; ath:AT5G13060; -.
DR Araport; AT5G13060; -.
DR TAIR; locus:2179842; AT5G13060.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_392026_0_0_1; -.
DR InParanoid; B7U179; -.
DR OMA; MYELADT; -.
DR OrthoDB; 237086at2759; -.
DR PhylomeDB; B7U179; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:B7U179; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B7U179; baseline and differential.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0006261; P:DNA-templated DNA replication; TAS:TAIR.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:2000104; P:negative regulation of DNA-templated DNA replication; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:TAIR.
DR Gene3D; 1.25.10.10; -; 4.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR044282; ABAP1/ARIA.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR46710; PTHR46710; 1.
DR Pfam; PF00514; Arm; 3.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00185; ARM; 8.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50176; ARM_REPEAT; 4.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..737
FT /note="ARMADILLO BTB ARABIDOPSIS PROTEIN 1"
FT /id="PRO_0000405807"
FT REPEAT 112..154
FT /note="ARM 1"
FT REPEAT 165..212
FT /note="ARM 2"
FT REPEAT 215..254
FT /note="ARM 3"
FT REPEAT 257..296
FT /note="ARM 4"
FT REPEAT 299..338
FT /note="ARM 5"
FT REPEAT 341..380
FT /note="ARM 6"
FT REPEAT 382..421
FT /note="ARM 7"
FT REPEAT 456..495
FT /note="ARM 8"
FT REPEAT 497..536
FT /note="ARM 9"
FT DOMAIN 568..635
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
SQ SEQUENCE 737 AA; 81361 MW; 1B2454D5CBBCBA71 CRC64;
MIISKSFKAP LKFSVKSSTA PVISNHPPME NHPKRQRTTR LAARNLKRKL SHNTDGAPIV
TQLIDIDDEP IDLVVAIRRH VEVLNSSFSD PDFDHEAVKE AAADIADLAK IDENVEIIVE
NGAIPALVRY LESPLVVCGN VPKSCEHKLE KDCALALGLI AAIQPGYQQL IVDAGAIVPT
VKLLKRRGEC GECMFANAVI RRAADIITNI AHDNPRIKTN IRVEGGIAPL VELLNFPDVK
VQRAAAGALR TVSFRNDENK SQIVELNALP TLVLMLQSQD STVHGEAIGA IGNLVHSSPD
IKKEVIRAGA LQPVIGLLSS TCLETQREAA LLIGQFAAPD SDCKVHIAQR GAITPLIKML
ESSDEQVVEM SAFALGRLAQ DAHNQAGIAH RGGIISLLNL LDVKTGSVQH NAAFALYGLA
DNEENVADFI KAGGIQKLQD DNFTVQPTRD CVVRTLKRLQ NKIHGPVLNQ LLYLMRTAEK
TVQIRIALAL AHLCDPKDGK LIFIDNNGVE FLLELLYFSS NKQQRYSSSA LYELAKKATS
FAPEDSAPCS PTQQVFLGEK FVNNPTMSDV TFLIDGKQFY AHKIGLVASS DIFRAMFDGL
YKERNAQNVE IPNIRWEVFE LMMKFIYSGR INIAKHLAKD LLVAADQYLL EGLKRQCEYT
IAQEICLDNI PEMYELADTF NASALRRACT LFVLEHFTKL SSQLWFAKFV KQIIPEIRSY
MTDILTRPVE ASPPTVV