Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Structural maintenance of chromosomes protein 4

Gene

smc4

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerase.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi107 – 1148ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Structural maintenance of chromosomes protein 4
Short name:
SMC protein 4
Short name:
SMC-4
Alternative name(s):
Chromosome assembly protein XCAP-C
Chromosome-associated protein C
Gene namesi
Name:smc4
Synonyms:capc, smc4l1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-5865892. smc4.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Chromosome By similarity

  • Note: In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12901290Structural maintenance of chromosomes protein 4PRO_0000119009Add
BLAST

Proteomic databases

PRIDEiP50532.

Interactioni

Subunit structurei

Forms a heterodimer with XCAP-E/SMC2. Component of the condensin complex, which contains the XCAP-E/SMC2 and XCAP-C/SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: XCAP-H/BRRN1, XCAP-D2/CNAP1 and XCAP-G/CAPG.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi99138. 7 interactions.
IntActiP50532. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP50532.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni595 – 763169Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili264 – 594331Sequence analysisAdd
BLAST
Coiled coili764 – 1027264Sequence analysisAdd
BLAST
Coiled coili1094 – 112936Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi60 – 656Poly-Pro
Compositional biasi747 – 7504Poly-Gly
Compositional biasi841 – 8444Poly-Ala
Compositional biasi1196 – 122025Ala/Asp-rich (DA-box)Add
BLAST

Domaini

The hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with XCAP-E, forming a V-shaped heterodimer.By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC4 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOVERGENiHBG106696.
KOiK06675.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view]
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
SSF75553. SSF75553. 1 hit.

Sequencei

Sequence statusi: Complete.

P50532-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPKKTKTST AVAREATESP MAERSRAPDA LQADPPAPTQ ESNNELVDSR
60 70 80 90 100
SLEEILSGIP PPPPPAMTNE AGAPRLMITH IVNQNFKSYA GERILGPFHK
110 120 130 140 150
RFSCIIGPNG SGKSNVIDSM LFVFGYRAQK IRSKKLSVLI HNSDEHKDVQ
160 170 180 190 200
SCTVEVHFQK IIDKEGDDFE VIPNSNFYVS RTAYKDNSSV YHISGKKATF
210 220 230 240 250
KDVGLLLRSH GIDLDHNRFL ILQGEVEQIA MMKPKGQTEH DEGMLEYLED
260 270 280 290 300
IIGSERLKEP IQILCRRVEL LNEQRGEKLN RVKMVEKEKD ALEGEKNKAI
310 320 330 340 350
EFLTVENETF KKKNQLCQYY IHDLQKRSRD KEAQKEKIQE DTKDISEKSN
360 370 380 390 400
TLLETMKEKN KALKDVEKQL NKITKFIEEN REKFTQLDLQ DVDTREKLKH
410 420 430 440 450
SKSKVKKLQK QLQKDKEKVD ELKNVPANSQ KIIAEETNKK DLLEKQKEKE
460 470 480 490 500
EEKLKNVMDS LKKETQGLQE EKEVKEKELM EISKTVNEAR SKMDVAQSEL
510 520 530 540 550
DIYLSRHNSA LSQLNKAKEA LNTASATLKE RRAAIKELET KLPKDEGDLK
560 570 580 590 600
KREKELESLV SEEGNIKNQV RELRQKVEEA RSSLSANRSR GKVLDALIQQ
610 620 630 640 650
KKSGKIPGIF GRLGDLGAID EKYDVAISSS CGALDHIVVD TIDTAQECVN
660 670 680 690 700
FLKKQNVGVA TFIGLDKMKV WEKGLNKIQT PENIPRLFDM VKVKDEQIKP
710 720 730 740 750
AFYFALRDTI VANNLDQATR VAFQKDKRWR VVTLQGQIIE QSGTMTGGGG
760 770 780 790 800
KVMKGRMGSS VMVEISDDQL QKMENKLKTD TTRATEIQDR KAHLEEEVAK
810 820 830 840 850
LRQATREMKN TFEKYTASLQ SLSEQEVHLK AQVKELEVNV AAAAPDKNQQ
860 870 880 890 900
KQMEKNLETL KKEYEKVAEK AGKVEAEVKR LHKLIVDINN HKLKAQQDKL
910 920 930 940 950
DKVTKEIDEC ASAITKAQVS IKTADRNLKK SEEAVARTEK EIVANDKSIE
960 970 980 990 1000
ELTEDLKKLE EKATTVMNEC KEAECSLPEV QEQHRSLLQE IKAIQEKEHA
1010 1020 1030 1040 1050
LQKEALNIRL NIEQIDSHIA EHQSKIKYWQ KEITKISLHK IEDIPEEVLP
1060 1070 1080 1090 1100
GLAQEELEAI KDPDQIINQI ALLEAKSHEM KPNLGAIAEY KKKEELYLQR
1110 1120 1130 1140 1150
VAELDEITNE RDSFRRAYED LRKQRLNEFM AGFNIITNKL KENYQMLTLG
1160 1170 1180 1190 1200
GDAELELVDS LDPFSEGIMF SVRPPKKSWK KIFNLSGGEK TLSSLALVFA
1210 1220 1230 1240 1250
LHHYKPTPLY FMDEIDAALD FKNVSIVAFY IYEQTKNAQF IIISLRNNMF
1260 1270 1280 1290
EIADRLIGIY KTHNTTKSVA TNPKIIAAKG LAEMQSVGCA
Length:1,290
Mass (Da):146,989
Last modified:October 1, 1996 - v1
Checksum:i2931249924FE90F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13673 mRNA. Translation: AAA64679.1.
PIRiA55094.
RefSeqiNP_001081371.1. NM_001087902.1.
UniGeneiXl.927.

Genome annotation databases

GeneIDi397799.
KEGGixla:397799.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13673 mRNA. Translation: AAA64679.1.
PIRiA55094.
RefSeqiNP_001081371.1. NM_001087902.1.
UniGeneiXl.927.

3D structure databases

ProteinModelPortaliP50532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi99138. 7 interactions.
IntActiP50532. 2 interactions.

Proteomic databases

PRIDEiP50532.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397799.
KEGGixla:397799.

Organism-specific databases

CTDi10051.
XenbaseiXB-GENE-5865892. smc4.

Phylogenomic databases

HOVERGENiHBG106696.
KOiK06675.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view]
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSMC4_XENLA
AccessioniPrimary (citable) accession number: P50532
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.