SMC4_MICAR
ID SMC4_MICAR Reviewed; 1243 AA.
AC Q9ERA5; Q9ERA1;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Structural maintenance of chromosomes protein 4;
DE Short=SMC protein 4;
DE Short=SMC-4;
DE AltName: Full=Chromosome-associated polypeptide C;
DE AltName: Full=XCAP-C homolog;
DE Flags: Fragment;
GN Name=SMC4; Synonyms=CAPC, SMC4L1;
OS Microtus arvalis (Common vole) (Field vole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Arvicolinae; Microtus.
OX NCBI_TaxID=47230;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Pavlova S.V., Nesterova T.B., Zakian S.M.;
RT "SMC genes from common vole Microtus arvalis.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with SMC2. Component of the condensin
CC complex, which contains the SMC2 and SMC4 heterodimer, and three non
CC SMC subunits that probably regulate the complex: BRRN1/CAPH,
CC CNAP1/CAPD2 and CAPG (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the
CC condensin complex is found in the cytoplasm, while a minority of the
CC complex is associated with chromatin. A subpopulation of the complex
CC however remains associated with chromosome foci in interphase cells.
CC During mitosis, most of the condensin complex is associated with the
CC chromatin. At the onset of prophase, the regulatory subunits of the
CC complex are phosphorylated by CDC2, leading to condensin's association
CC with chromosome arms and to chromosome condensation. Dissociation from
CC chromosomes is observed in late telophase (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The SMC hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the heterodimerization with SMC2, forming a
CC V-shaped heterodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily. {ECO:0000305}.
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DR EMBL; AJ299713; CAC09583.1; -; mRNA.
DR EMBL; AJ299717; CAC09587.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ERA5; -.
DR SMR; Q9ERA5; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0007076; P:mitotic chromosome condensation; ISS: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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Chromosome;
KW Coiled coil; Cytoplasm; DNA condensation; Mitosis; Nucleotide-binding;
KW Nucleus; Phosphoprotein.
FT CHAIN <1..1243
FT /note="Structural maintenance of chromosomes protein 4"
FT /id="PRO_0000119007"
FT DOMAIN 568..682
FT /note="SMC hinge"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 225..546
FT /evidence="ECO:0000255"
FT COILED 721..975
FT /evidence="ECO:0000255"
FT COILED 1062..1090
FT /evidence="ECO:0000255"
FT BINDING 68..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTJ3"
FT MOD_RES 336
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CG47"
FT MOD_RES 634
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTJ3"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTJ3"
FT MOD_RES 1011
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NTJ3"
FT CONFLICT 241
FT /note="N -> K (in Ref. 1; CAC09587)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="E -> R (in Ref. 1; CAC09587)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 1243 AA; 142342 MW; B621BD6D954DA7F9 CRC64;
LETPGEEVDN RSLEEILSSI PPPPPPAMAS EAGAPRLMIT HIVNQNFKSC AGEKILGPFH
KRFSCIIGPN GSGKSNVIDS MLFVFGYRAQ KIRSKKLSVL IHNSDEHKDI QSCTVEVHFQ
KIIDKEGDDY EVIPNSNFCV SRTAYRDNTS VYHISGKKRT FKDVGNLLRS HGIDLDHNRF
LILQGEVEQI AMMKPKGQTE HDEGMLEYLE DIIGCGRLNE PIKVLCRRVE ILNENRGEKL
NRVKMVEKEK DAVEGEKNIA IEFLTLEKEM FKKKNHVCQY YIYDLQKRID EMKTQKEKIH
EDTKEITEKS NMLSNEMKAK NSAVKDIEKK LHKATKFIEE NKEKFRQLDL EDVQVREKLK
HATSKAKKLE KQLQKDKEKV EELKSIPAKS KTIINETTTK SSSLEKEKEK EEKKLKEVMD
SLKQETQGLQ KEKEDQEKEL MGFNKSVNEA RSKMEVAQSE LDIYLSRHNT AVSQLSKAKE
TLITASETLK ERKAAIGEIN TKLPQTQQEL KEKEKELQKL TQEEINLKSL VHDLFQKVEE
AKSSLAMNRS RGKVLDAIIQ EKKSGRIPGI YGRLGDLGAI DEKYDIAISS CCHALDYIVV
DSIDTAQECV NFLKRHNIGV ATFIGLDKMT VWAKKMAKIQ TPENTPRLFD LVKAKNEEIR
QAFYFALRDT LVADNLDQAT RVAYQKDRRW RVVTLQGQII EQSGTMTGGG SKVMRGRMGS
SVIVEISEEE VNKMESQLQK HSKQARRIQE QKVQHEERVV KLRHSEREMR NTLEKFAASI
QGLSDQEEYL TVQIKELEAN VLTTAPDKKK QKLLEENVSA FKKEYDAVAE KAGKVEAEVK
RLHDTIIEIN NRKLKAQQNK LDMINKQLDE CASAITKAQV AIKTADRNLI KAQDSVVRTE
KEIKDTEKET NDLKAELKAI EDKAEEVIKK TNAAEESLPE IQKEHRNLLQ ELKVIQENEH
ALQKDALSIK LKLEQIDGHI AEHNSKIKYW QKEISKIKLH PIEDNPVETV SVLSPEDLEA
IKNPDSITNQ IAILEAQCHE MKPNLGAIAE YKKKEELYLQ RVAELDKITS ERDNFRQAYE
DLRKQRLNEF MAGFYIITNK LKENYQMLTL GGDAELELVD SLDPFSEGIM FSVRPPKKSW
KKIFNLSGGE KTLSSLALVF ALHHYKPTPL YFMDEIDAAL DFKNVSIVAF YIYEQTKNAQ
FIIISLRNNM FEISDRLIGI YKTYNITKSV AVNPKEIASK GLC
