SCC12_ARATH
ID SCC12_ARATH Reviewed; 810 AA.
AC Q9FQ20; Q8W1Y1; Q8W1Y2; Q9FKS2;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Sister chromatid cohesion 1 protein 2;
DE AltName: Full=SCC1 homolog 2;
DE Short=AtRAD21-1;
GN Name=SYN2; OrderedLocusNames=At5g40840; ORFNames=MHK7.7;
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 2).
RC STRAIN=cv. Wassilewskija;
RX PubMed=11410371; DOI=10.1016/s0378-1119(01)00499-1;
RA Dong F., Cai X., Makaroff C.A.;
RT "Cloning and characterization of two Arabidopsis genes that belong to the
RT RAD21/REC8 family of chromosome cohesin proteins.";
RL Gene 271:99-108(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Costa-Nunes J.A., Bhatt A.M., Dickinson H.G.;
RT "Functional analysis of the three Arabidopsis RAD21 homologs.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [4]
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).
CC -!- FUNCTION: May be involved in sister chromatid cohesion during mitosis.
CC -!- SUBUNIT: Component of the cohesin complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FQ20-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FQ20-2; Sequence=VSP_007493;
CC -!- TISSUE SPECIFICITY: Low expression in shoots, buds, siliques, leaves
CC and roots. Found in, but not limited to, actively dividing cells: in
CC procambium, protoderm and ground meristem in roots, and in shoot and
CC floral meristems.
CC -!- MISCELLANEOUS: [Isoform 2]: Intron 9 uses an acceptor splice site 3
CC nucleotides downstream of the one used in isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the rad21 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11346.1; 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; AF281154; AAG44842.1; -; mRNA.
DR EMBL; AF400126; AAL62057.1; -; mRNA.
DR EMBL; AF400127; AAL62058.1; -; mRNA.
DR EMBL; AB011477; BAB11346.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94602.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94603.1; -; Genomic_DNA.
DR RefSeq; NP_568586.2; NM_123449.3. [Q9FQ20-1]
DR RefSeq; NP_851110.1; NM_180779.2. [Q9FQ20-2]
DR AlphaFoldDB; Q9FQ20; -.
DR SMR; Q9FQ20; -.
DR STRING; 3702.AT5G40840.2; -.
DR PaxDb; Q9FQ20; -.
DR PRIDE; Q9FQ20; -.
DR ProteomicsDB; 232691; -. [Q9FQ20-1]
DR EnsemblPlants; AT5G40840.1; AT5G40840.1; AT5G40840. [Q9FQ20-2]
DR EnsemblPlants; AT5G40840.2; AT5G40840.2; AT5G40840. [Q9FQ20-1]
DR GeneID; 834084; -.
DR Gramene; AT5G40840.1; AT5G40840.1; AT5G40840. [Q9FQ20-2]
DR Gramene; AT5G40840.2; AT5G40840.2; AT5G40840. [Q9FQ20-1]
DR KEGG; ath:AT5G40840; -.
DR Araport; AT5G40840; -.
DR TAIR; locus:2164501; AT5G40840.
DR eggNOG; KOG1213; Eukaryota.
DR HOGENOM; CLU_015577_0_0_1; -.
DR InParanoid; Q9FQ20; -.
DR OMA; MTCSYAD; -.
DR OrthoDB; 171779at2759; -.
DR PhylomeDB; Q9FQ20; -.
DR PRO; PR:Q9FQ20; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FQ20; baseline and differential.
DR Genevisible; Q9FQ20; AT.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0000798; C:nuclear cohesin complex; ISS:TAIR.
DR GO; GO:0005634; C:nucleus; ISS:TAIR.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:TAIR.
DR GO; GO:0000278; P:mitotic cell cycle; IEP:TAIR.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IBA:GO_Central.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR Gene3D; 1.10.10.580; -; 1.
DR InterPro; IPR039781; Rad21/Rec8-like.
DR InterPro; IPR006909; Rad21/Rec8_C_eu.
DR InterPro; IPR006910; Rad21_Rec8_N.
DR InterPro; IPR023093; ScpA-like_C.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12585; PTHR12585; 1.
DR Pfam; PF04824; Rad21_Rec8; 1.
DR Pfam; PF04825; Rad21_Rec8_N; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Chromosome partition;
KW Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..810
FT /note="Sister chromatid cohesion 1 protein 2"
FT /id="PRO_0000097876"
FT REGION 200..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 716
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11410371, ECO:0000303|Ref.2"
FT /id="VSP_007493"
FT CONFLICT 196
FT /note="A -> S (in Ref. 1; AAG44842)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="E -> K (in Ref. 1; AAG44842)"
FT /evidence="ECO:0000305"
FT CONFLICT 309..311
FT /note="SLP -> ALS (in Ref. 1; AAG44842)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="T -> A (in Ref. 1; AAG44842)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="V -> A (in Ref. 1; AAG44842)"
FT /evidence="ECO:0000305"
FT CONFLICT 787
FT /note="V -> L (in Ref. 1; AAG44842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 810 AA; 91459 MW; CF1159DDA743EB57 CRC64;
MFYSHCLVSR KGPLGAIWVA AYFFKKLKKS QVKATHIPSS VDQILQKELD ALTYRVLAYL
LLGVVRIYSK KVDFLFDDCN KALIGVKEFV AKERNREKTG VSLPASIECF SIALPERFEL
DAFDLGVLED FHGGNVKPHE DITLKDGSQE TERMDMYSME RFDMEEDLLF TFHETFSTNH
NENKHESFAH DMELDAENVR DTTEEASVRV VEAEPLDSNE PSRDHQNASR HREDPESDDI
LLEPQMSEDI RIAQEEDTVR ETICTIVQRL VDSHESSGDN LHRDGHTENL ESEKTSKKTS
CEEMQHDRSL PSECGIPEAI HGIEDQPSGA TRINGEKEIP EMSTLEKPEP VSVTGSRDLQ
EGVEKCRDHN EAEMADFELF HGSHKEQSET SEVNLHGSEK GFLSDMTVSK DPSSEFNATD
TPVTVTPKTP SRLKISEGGT SPQFSIIPTP AAKESSRVSR KRKCLIDDEV IIPNKVMKEM
IEDSSKLLAK RRNVPHTDCP ERRTKRFANP FRSFLEPLIQ YGSSDLQSLF CQPIKLKNWA
TTGTPKDTKI ARHKEKSSLD TVRSPGVILS SDQTENTQEI METPQAAALA GLKVTAGNSN
VVSVEMGASS TTSGTAHQTE NAAETPVKPS VIAPETPVRT SEQTVIAPET PVVSEQVEIA
PETPVRESMS KRFFKDPGTC YKKSRPASPF TSFEEHPSVY YVENRDLDTI LMNDEQVNAD
ERQDLQQETW SSRTRNVAKF LEKTFLEQRE REEEEKVSLL QLCRGRTQKE SARLFYETLV
LKTKGYVEVK QNHPYSDVFL MRVSRPQKAC
