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SMC4_ARATH
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   03-AUG-2022, entry version 137.
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.AT5G48600.2; -.
DR   iPTMnet; Q9FJL0; -.
DR   PaxDb; Q9FJL0; -.
DR   PRIDE; Q9FJL0; -.
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   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   CDD; cd03274; ABC_SMC4_euk; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR024704; SMC.
DR   InterPro; IPR041738; SMC4_ABC_euk.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
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; SSF52540; 1.
DR   SUPFAM; SSF75553; SSF75553; 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
 
 
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