SUV2_ARATH
ID SUV2_ARATH Reviewed; 646 AA.
AC C8KI33; A0A1P8BEL4; Q9FK80;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Protein SENSITIVE TO UV 2 {ECO:0000303|PubMed:19619159, ECO:0000303|PubMed:28556304};
DE AltName: Full=ATR interacting protein {ECO:0000303|PubMed:19619158, ECO:0000303|PubMed:19619159};
DE Short=AtATRIP {ECO:0000303|PubMed:19619158, ECO:0000303|PubMed:19619159};
DE AltName: Full=Protein HYDROXYUREA-SENSITIVE 2 {ECO:0000303|PubMed:19619158};
GN Name=SUV2 {ECO:0000303|PubMed:19619159, ECO:0000303|PubMed:28556304};
GN Synonyms=ATRIP {ECO:0000303|PubMed:19619158, ECO:0000303|PubMed:19619159},
GN HUS2 {ECO:0000303|PubMed:19619158};
GN OrderedLocusNames=At5g45610 {ECO:0000312|Araport:AT5G45610};
GN ORFNames=MRA19.1 {ECO:0000312|EMBL:BAB09204.1};
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] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE, AND
RP SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=19619159; DOI=10.1111/j.1365-313x.2009.03974.x;
RA Sakamoto A.N., Lan V.T.T., Puripunyavanich V., Hase Y., Yokota Y.,
RA Shikazono N., Nakagawa M., Narumi I., Tanaka A.;
RT "A UVB-hypersensitive mutant in Arabidopsis thaliana is defective in the
RT DNA damage response.";
RL Plant J. 60:509-517(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19619158; DOI=10.1111/j.1365-313x.2009.03975.x;
RA Sweeney P.R., Britt A.B., Culligan K.M.;
RT "The Arabidopsis ATRIP ortholog is required for a programmed response to
RT replication inhibitors.";
RL Plant J. 60:518-526(2009).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=28556304; DOI=10.1111/pce.12992;
RA Sjogren C.A., Larsen P.B.;
RT "SUV2, which encodes an ATR-related cell cycle checkpoint and putative
RT plant ATRIP, is required for aluminium-dependent root growth inhibition in
RT Arabidopsis.";
RL Plant Cell Environ. 40:1849-1860(2017).
CC -!- FUNCTION: Required for tolerance to DNA-damaging and cross-linking
CC agents such as UVB irradiation, gamma-radiation, aphidicolin, ionizing
CC radiation and hydroxyurea (HU), cisplatin (CDDP) and mitomycin C (MMC)
CC (PubMed:19619159, PubMed:19619158, PubMed:28556304). Involved in cell-
CC cycle G2/M arrest in response to DNA damage (PubMed:19619159,
CC PubMed:19619158). Required for aluminum-dependent gene regulation and
CC root growth inhibition in an ATR-dependent manner by halting cell cycle
CC progression and triggering loss of the quiescent center (QC)
CC (PubMed:28556304). {ECO:0000269|PubMed:19619158,
CC ECO:0000269|PubMed:19619159, ECO:0000269|PubMed:28556304}.
CC -!- SUBUNIT: Forms multimers through the coiled-coil domain.
CC {ECO:0000269|PubMed:19619159}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:28556304}. Cytoplasm {ECO:0000269|PubMed:28556304}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=C8KI33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=C8KI33-2; Sequence=VSP_060239;
CC -!- TISSUE SPECIFICITY: Accumulates throughout the root tip.
CC {ECO:0000269|PubMed:28556304}.
CC -!- INDUCTION: Becomes more restricted to the distal region of the root tip
CC upon addition of aluminum (Al). {ECO:0000269|PubMed:28556304}.
CC -!- PTM: Probably phosphorylated by ATR. {ECO:0000269|PubMed:28556304}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to DNA-damaging agents including
CC UVB, gamma-radiation, aphidicolin, ionizing radiation and hydroxyurea
CC (HU) (PubMed:19619159, PubMed:19619158). Defective in cell-cycle G2/M
CC arrest in response to DNA damage (PubMed:19619159, PubMed:19619158).
CC Reversed extreme hypersensitivity to aluminum (Al) of the mutant als3-
CC 1, including Al-dependent terminal differentiation of the root tip and
CC transition to endoreduplication. Increased tolerance to Al
CC (PubMed:28556304). {ECO:0000269|PubMed:19619158,
CC ECO:0000269|PubMed:19619159, ECO:0000269|PubMed:28556304}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09204.1; Type=Erroneous gene model prediction; 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; AB492859; BAI43377.1; -; mRNA.
DR EMBL; AB012245; BAB09204.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95275.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70036.1; -; Genomic_DNA.
DR RefSeq; NP_001331674.1; NM_001344635.1. [C8KI33-2]
DR RefSeq; NP_199374.4; NM_123929.6. [C8KI33-1]
DR AlphaFoldDB; C8KI33; -.
DR STRING; 3702.AT5G45610.1; -.
DR iPTMnet; C8KI33; -.
DR PaxDb; C8KI33; -.
DR PRIDE; C8KI33; -.
DR ProteomicsDB; 185590; -. [C8KI33-1]
DR EnsemblPlants; AT5G45610.1; AT5G45610.1; AT5G45610. [C8KI33-1]
DR EnsemblPlants; AT5G45610.2; AT5G45610.2; AT5G45610. [C8KI33-2]
DR GeneID; 834601; -.
DR Gramene; AT5G45610.1; AT5G45610.1; AT5G45610. [C8KI33-1]
DR Gramene; AT5G45610.2; AT5G45610.2; AT5G45610. [C8KI33-2]
DR KEGG; ath:AT5G45610; -.
DR Araport; AT5G45610; -.
DR TAIR; locus:2171993; AT5G45610.
DR eggNOG; ENOG502QR7S; Eukaryota.
DR HOGENOM; CLU_020186_0_0_1; -.
DR InParanoid; C8KI33; -.
DR OMA; HMERNSH; -.
DR OrthoDB; 794775at2759; -.
DR PhylomeDB; C8KI33; -.
DR PRO; PR:C8KI33; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C8KI33; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IPI:TAIR.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IMP:TAIR.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0010044; P:response to aluminum ion; IMP:UniProtKB.
DR GO; GO:0072718; P:response to cisplatin; IMP:UniProtKB.
DR GO; GO:0010332; P:response to gamma radiation; IMP:UniProtKB.
DR GO; GO:0072710; P:response to hydroxyurea; IMP:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR GO; GO:0010224; P:response to UV-B; IMP:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR044952; SUV2.
DR PANTHER; PTHR35761; PTHR35761; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; DNA damage; Hydrolase;
KW Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..646
FT /note="Protein SENSITIVE TO UV 2"
FT /id="PRO_0000447698"
FT DOMAIN 376..646
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT REGION 42..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 123..157
FT /evidence="ECO:0000255"
FT MOTIF 119..126
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 46..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 579..580
FT /note="Reactive bond"
FT /evidence="ECO:0000305"
FT VAR_SEQ 560..645
FT /note="TLLMREILILLNRLVSGLSSSATILKELTTSRDMASLTVDAATRLSRKRNLL
FT GKPESSVERMRNTEIMDLARIFKKRVFAFLGDNT -> FILHRGDLQIENL (in
FT isoform 2)"
FT /id="VSP_060239"
SQ SEQUENCE 646 AA; 72806 MW; 63F468041513D83A CRC64;
MSGNDEEFND EFLLAIDSIE TTLKKADMYR PLPPPYLPTF LPAPPPSTKI SSSLSHPMQL
QSSAGQQRKQ IQVPDPFLSY SPPRELSQRV VSGFNDALMD YSNSTVVTAA KPISPTTSNR
RCDSEKDLEI DRLKKELERV SKQLLDVEQE CSQLKKGKSK ETESRNLCAD DNRGQCSTVH
ASKRIDLEPD VATSSVNHRE NDSRMALDDK RSFKTTGVQA DVANHSDLSK KLLDIWRTSN
YQDPRKNLIS ELLLACSTDL QILFSFMKIS TPPQELNKQE AKTSSDRQSS KALESEKVYQ
LYSAVTKISY GFVNLKTLVE PLLDLCKAET AVLVHRSLRV LHVLLEHICG DEKRFEASWD
ANWHSLFKLM NQIASKRTEQ DVKQEALSIM NIIVMSTDAY TARESFVSKE VFESISLLLR
KEGGLHVRKE AIHLFYLLLN CPKLYDTFDS LHEEKNSSDT ENDSEGNFFA LEAFGKIFEG
LADCLTSPRK TSEDLELCRN VIMILALAAS SGNSGYELLS SHKLPQDSSF LMLILHLLVA
EIDSESTEFH PKAEIFKART LLMREILILL NRLVSGLSSS ATILKELTTS RDMASLTVDA
ATRLSRKRNL LGKPESSVER MRNTEIMDLA RIFKKRVFAF LGDNTI
