WAPL2_ARATH
ID WAPL2_ARATH Reviewed; 840 AA.
AC Q9C951; Q681R1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Wings apart-like protein 2 {ECO:0000303|PubMed:25033056};
DE Short=AtWAPL2 {ECO:0000303|PubMed:25033056};
GN Name=WAPL2 {ECO:0000303|PubMed:25033056};
GN OrderedLocusNames=At1g61030 {ECO:0000312|Araport:AT1G61030};
GN ORFNames=T7P1.16 {ECO:0000312|EMBL:AAG51640.1};
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 [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] OF 1-322.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25033056; DOI=10.1371/journal.pgen.1004497;
RA De K., Sterle L., Krueger L., Yang X., Makaroff C.A.;
RT "Arabidopsis thaliana WAPL is essential for the prophase removal of cohesin
RT during meiosis.";
RL PLoS Genet. 10:e1004497-e1004497(2014).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=26813623; DOI=10.1105/tpc.15.00781;
RA De K., Bolanos-Villegas P., Mitra S., Yang X., Homan G., Jauh G.-Y.,
RA Makaroff C.A.;
RT "The Opposing Actions of Arabidopsis CHROMOSOME TRANSMISSION FIDELITY7 and
RT WINGS APART-LIKE1 and 2 Differ in Mitotic and Meiotic Cells.";
RL Plant Cell 28:521-536(2016).
CC -!- FUNCTION: Regulator of sister chromatid cohesion in meiosis which
CC negatively regulates cohesin association with chromatin, acting as an
CC antagonist of CTF7 (PubMed:25033056, PubMed:26813623). Cohesion ensures
CC that chromosome partitioning is accurate in both meiotic and mitotic
CC cells and plays an important role in DNA repair (By similarity).
CC Essential for the prophase removal of cohesin during meiosis thus
CC determining the timely release of meiotic cohesion (PubMed:25033056).
CC Important for proper spindle attachment and assembly during meiosis
CC (PubMed:25033056). Helps to prevent abnormal centromere association
CC during prophase I in meiocytes (PubMed:25033056). Required for early
CC embryonic patterning (PubMed:25033056). Also involved in chromosome
CC segregation during mitosis (PubMed:25033056).
CC {ECO:0000250|UniProtKB:Q7Z5K2, ECO:0000269|PubMed:25033056,
CC ECO:0000269|PubMed:26813623}.
CC -!- SUBUNIT: Interacts with the cohesin complex throughout the cell cycle.
CC {ECO:0000250|UniProtKB:Q7Z5K2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7Z5K2}.
CC Chromosome {ECO:0000250|UniProtKB:Q7Z5K2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C951-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C951-2; Sequence=VSP_060585, VSP_060586;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, buds and siliques.
CC {ECO:0000269|PubMed:25033056}.
CC -!- DISRUPTION PHENOTYPE: Plants missing both WAPL1 and WAPL2 have
CC relatively normal growth (slightly slower) and development but exhibit
CC a significant reduction in male and female fertility (aborted pollen
CC and ovules prior to fertilization and embryo defects in fertilized
CC seed), due to blocked removal of cohesin from chromosomes during
CC meiotic prophase (late zygotene/pachytene stage) resulting in
CC chromosome bridges, broken chromosomes and uneven chromosome
CC segregation, and leading to shorter siliques containing fewer seeds;
CC this double mutant restores pollen viablitity to pollen-lethal ctf7
CC mutation (PubMed:25033056, PubMed:26813623). During mitosis, abnormal
CC chromosome segregation but normal cohesin release (PubMed:25033056).
CC {ECO:0000269|PubMed:25033056, ECO:0000269|PubMed:26813623}.
CC -!- SIMILARITY: Belongs to the WAPL family. {ECO:0000305}.
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DR EMBL; AC018908; AAG51640.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33769.1; -; Genomic_DNA.
DR EMBL; AK175556; BAD43319.1; -; mRNA.
DR PIR; H96635; H96635.
DR RefSeq; NP_176298.1; NM_104783.3. [Q9C951-1]
DR AlphaFoldDB; Q9C951; -.
DR SMR; Q9C951; -.
DR STRING; 3702.AT1G61030.1; -.
DR PaxDb; Q9C951; -.
DR PRIDE; Q9C951; -.
DR ProteomicsDB; 177244; -. [Q9C951-1]
DR EnsemblPlants; AT1G61030.1; AT1G61030.1; AT1G61030. [Q9C951-1]
DR GeneID; 842394; -.
DR Gramene; AT1G61030.1; AT1G61030.1; AT1G61030. [Q9C951-1]
DR KEGG; ath:AT1G61030; -.
DR Araport; AT1G61030; -.
DR TAIR; locus:2205991; AT1G61030.
DR eggNOG; KOG2152; Eukaryota.
DR HOGENOM; CLU_015006_0_0_1; -.
DR InParanoid; Q9C951; -.
DR OMA; SEQDMIP; -.
DR OrthoDB; 554620at2759; -.
DR PhylomeDB; Q9C951; -.
DR PRO; PR:Q9C951; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C951; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:1990571; P:meiotic centromere clustering; IMP:UniProtKB.
DR GO; GO:0045132; P:meiotic chromosome segregation; IGI:TAIR.
DR GO; GO:0010789; P:meiotic sister chromatid cohesion involved in meiosis I; IGI:TAIR.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:UniProtKB.
DR GO; GO:0090306; P:meiotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IGI:TAIR.
DR GO; GO:0060623; P:regulation of chromosome condensation; IBA:GO_Central.
DR GO; GO:0071922; P:regulation of cohesin loading; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039874; WAPL.
DR InterPro; IPR022771; WAPL_C.
DR PANTHER; PTHR22100; PTHR22100; 2.
DR Pfam; PF07814; WAPL; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Chromosome;
KW Chromosome partition; Meiosis; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..840
FT /note="Wings apart-like protein 2"
FT /id="PRO_0000450126"
FT DOMAIN 764..819
FT /note="WAPL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00603"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 322
FT /note="S -> V (in isoform 2)"
FT /id="VSP_060585"
FT VAR_SEQ 323..840
FT /note="Missing (in isoform 2)"
FT /id="VSP_060586"
SQ SEQUENCE 840 AA; 92934 MW; BBD393AA4E18EB9B CRC64;
MMERTYGRRK PGMLNDDVSR AEHIFPSSSS PELEPVDFST QESSCVWNYS SRSTFSDNDF
SEKRNKRPRN GGGGFGSNST LMEAQEFGEL IENEDEVNFA LDGLKKGHKV RIRRAALSSL
LSICESQYQR RSLRALGISQ SIIDAILGLC LDDIPSNLAA ATLFFVLTTD GQDDHFMESP
NSIKFLVKLL RPVVSASTKV KPRNIGSRLL SIIKDVDAAR DAASMHDLSS CDIIDRAQEI
LVNCKELRLI DSYKIERMRP ELSTKWVALL VMEKACLSKI SFDDTSGTVK KSGGMFKEKL
RELGGLDAVF DVVMDCHTVM ESWVTHDTLS VEDIKDDLNK QSLMLLLKCL KIMENATFLS
TENQIHLLRL NKSMGSHESR LSFTELMISV IKILSGLQLR AHRNEKHPHP QPHLASAVKK
GFVTIISSDT CSTTGFSSIK SLSVSKRNQS AFLVGCSTTP KPGSQSSVMS TIDHCTLTTT
AGSNTGSFAG RLASLGSGIS RSKTRTSQTR ESSCKKVENF ASFEDSQDPF SFDLEDSGPS
RWAVGKQKKS KGQKRKGSYR DKKDERSLQL FSSQEESNHG LNSQEESSDR DHHVTEQPSL
TYDIDKGCLC LLSDCLLTAV KVLMNLTNGN SVGCREVAAC GGLESMAELV VGHFPSFTRS
PLYSQMESGT CHQKDKHLTD QELDFLVAIL GLLVNLVEKN GINRSRLAAA SVPITNPEGL
QDSEQDMIPL LCSIFLTNKG SADTKDETST FTLDDEEAVL ESEKEAEKMI VEAYSALLLA
FLSTESRSIR NAIRDYLPKR DMAILVPVLD RFVAFHTTLD MIPPETHKVV MEVIESCKLP
