ID SMC4_ARATH Reviewed; 1241 AA.
AC Q9FJL0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 144.
DE RecName: Full=Structural maintenance of chromosomes protein 4;
DE Short=AtSMC4;
DE Short=SMC protein 4;
DE Short=SMC-4;
DE AltName: Full=Chromosome-associated protein C;
DE Short=AtCAP-C;
GN Name=SMC4; Synonyms=CAP-C; OrderedLocusNames=At5g48600; ORFNames=K15N18.7;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16482433; DOI=10.1007/s00425-006-0234-z;
RA Siddiqui N.U., Rusyniak S., Hasenkampf C.A., Riggs C.D.;
RT "Disruption of the Arabidopsis SMC4 gene, AtCAP-C, compromises
RT gametogenesis and embryogenesis.";
RL Planta 223:990-997(2006).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Central component of the condensin complex, a complex
CC required for conversion of interphase chromatin into mitotic-like
CC condense chromosomes. The condensin complex probably introduces
CC positive supercoils into relaxed DNA in the presence of type I
CC topoisomerases and converts nicked DNA into positive knotted forms in
CC the presence of type II topoisomerases. Also involved in chromosome
CC segregation in meiosis. {ECO:0000269|PubMed:16482433}.
CC -!- SUBUNIT: Forms a heterodimer with a SMC2 subfamily member. Component of
CC the condensin complex, which contains the SMC2 and SMC4 heterodimer,
CC and three non SMC subunits that probably regulate the complex: CAPH,
CC CAPD2 and CAPG.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Associates with chromatin.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FJL0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in seedlings and inflorescences.
CC {ECO:0000269|PubMed:16482433}.
CC -!- DOMAIN: The SMC hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the heterodimerization with a SMC2
CC subfamily member, forming a V-shaped heterodimer.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily. {ECO:0000305}.
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DR EMBL; AB015468; BAB10693.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95694.1; -; Genomic_DNA.
DR RefSeq; NP_199671.1; NM_124236.3. [Q9FJL0-1]
DR AlphaFoldDB; Q9FJL0; -.
DR SMR; Q9FJL0; -.
DR BioGRID; 20163; 3.
DR STRING; 3702.Q9FJL0; -.
DR iPTMnet; Q9FJL0; -.
DR PaxDb; 3702-AT5G48600-2; -.
DR ProteomicsDB; 228199; -. [Q9FJL0-1]
DR EnsemblPlants; AT5G48600.1; AT5G48600.1; AT5G48600. [Q9FJL0-1]
DR GeneID; 834917; -.
DR Gramene; AT5G48600.1; AT5G48600.1; AT5G48600. [Q9FJL0-1]
DR KEGG; ath:AT5G48600; -.
DR Araport; AT5G48600; -.
DR TAIR; AT5G48600; SMC3.
DR eggNOG; KOG0996; Eukaryota.
DR HOGENOM; CLU_001042_4_1_1; -.
DR InParanoid; Q9FJL0; -.
DR PhylomeDB; Q9FJL0; -.
DR PRO; PR:Q9FJL0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJL0; baseline and differential.
DR Genevisible; Q9FJL0; AT.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF172; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Coiled coil; DNA condensation; Meiosis; Mitosis; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..1241
FT /note="Structural maintenance of chromosomes protein 4"
FT /id="PRO_0000284896"
FT DOMAIN 25..1224
FT /note="Zinc-hook"
FT DOMAIN 555..671
FT /note="SMC hinge"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 201..552
FT /evidence="ECO:0000255"
FT COILED 719..1085
FT /evidence="ECO:0000255"
FT BINDING 55..62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 1241 AA; 141130 MW; AB5D6A1B35F053F6 CRC64;
MEEDEPMGGG ESEPEQRKSG TPRLYIKELV MRNFKSYAGE QRVGPFHKSF SAVVGPNGSG
KSNVIDAMLF VFGKRAKQMR LNKVSELIHN STNHQNLDSA GVSVQFEEII DLENGLYETV
PGSDFMITRV AFRDNSSKYY INERSSNFTE VTKKLKGKGV DLDNNRFLIL QGEVEQISLM
KPKAQGPHDE GFLEYLEDII GTNKYVEKID ELNKQLETLN ESRSGVVQMV KLAEKERDNL
EGLKDEAETY MLKELSHLKW QEKATKMAYE DTVAKITEQR DSLQNLENSL KDERVKMDES
NEELKKFESV HEKHKKRQEV LDNELRACKE KFKEFERQDV KHREDLKHVK QKIKKLEDKL
EKDSSKIGDM TKESEDSSNL IPKLQENIPK LQKVLLDEEK KLEEIKAIAK VETEGYRSEL
TKIRAELEPW EKDLIVHRGK LDVASSESEL LSKKHEAALK AFTDAQKQLS DISTRKKEKA
AATTSWKADI KKKKQEAIEA RKVEEESLKE QETLVPQEQA AREKVAELKS AMNSEKSQNE
VLKAVLRAKE NNQIEGIYGR MGDLGAIDAK YDVAISTACA GLDYIVVETT SSAQACVELL
RKGNLGFATF MILEKQTDHI HKLKEKVKTP EDVPRLFDLV RVKDERMKLA FYAALGNTVV
AKDLDQATRI AYGGNREFRR VVALDGALFE KSGTMSGGGG KARGGRMGTS IRATGVSGEA
VANAENELSK IVDMLNNIRE KVGNAVRQYR AAENEVSGLE MELAKSQREI ESLNSEHNYL
EKQLASLEAA SQPKTDEIDR LKELKKIISK EEKEIENLEK GSKQLKDKLQ TNIENAGGEK
LKGQKAKVEK IQTDIDKNNT EINRCNVQIE TNQKLIKKLT KGIEEATREK ERLEGEKENL
HVTFKDITQK AFEIQETYKK TQQLIDEHKD VLTGAKSDYE NLKKSVDELK ASRVDAEFKV
QDMKKKYNEL EMREKGYKKK LNDLQIAFTK HMEQIQKDLV DPDKLQATLM DNNLNEACDL
KRALEMVALL EAQLKELNPN LDSIAEYRSK VELYNGRVDE LNSVTQERDD TRKQYDELRK
RRLDEFMAGF NTISLKLKEM YQMITLGGDA ELELVDSLDP FSEGVVFSVR PPKKSWKNIA
NLSGGEKTLS SLALVFALHH YKPTPLYVMD EIDAALDFKN VSIVGHYVKD RTKDAQFIII
SLRNNMFELA DRLVGIYKTD NCTKSITINP GSFAVCQKTP A
//
