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UniProtKB - P18296 (CUT1_SCHPO)
Protein
Separin
Gene
cut1
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Functioni
Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the rad21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by securin/cut2 protein. It is also required for pointed nuclear formation.
1 PublicationCatalytic activityi
- All bonds known to be hydrolyzed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by a hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage. EC:3.4.22.49
Activity regulationi
It is inactivated via its interaction with cut2, which probably covers its active site. Cut2 degradation at anaphase, liberates it and triggers rad21 cleavage.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 1730 | 1 |
GO - Molecular functioni
- cysteine-type endopeptidase activity Source: GO_Central
- endopeptidase activity Source: PomBase
GO - Biological processi
- cell division Source: UniProtKB-KW
- cellular response to DNA damage stimulus Source: PomBase
- meiotic chromosome separation Source: PomBase
- meiotic nuclear division Source: PomBase
- mitotic sister chromatid separation Source: PomBase
Keywordsi
Molecular function | Hydrolase, Protease, Thiol protease |
Biological process | Cell cycle, Cell division, Chromosome partition |
Enzyme and pathway databases
BRENDAi | 3.4.22.49, 5613 |
Reactomei | R-SPO-2467813, Separation of Sister Chromatids |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:cut1 ORF Names:SPCC5E4.04 |
Organismi | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
Taxonomic identifieri | 284812 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › |
Proteomesi |
|
Organism-specific databases
PomBasei | SPCC5E4.04, cut1 |
VEuPathDBi | FungiDB:SPCC5E4.04 |
Subcellular locationi
Cytoskeleton
- mitotic spindle Source: PomBase
- mitotic spindle midzone Source: PomBase
- mitotic spindle pole body Source: PomBase
Cytosol
- cytosol Source: PomBase
Nucleus
- nucleus Source: GO_Central
Other locations
- cytoplasm Source: GO_Central
- separase-securin complex Source: PomBase
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1767 | D → A: Affects the formation of the pointed nucleus; when associated with V-1779. 1 Publication | 1 | |
Mutagenesisi | 1779 | E → V: Affects the formation of the pointed nucleus; when associated with A-1767. 1 Publication | 1 | |
Mutagenesisi | 1816 | A → T in cut1-T693; reduced function; when transferred at 33 degrees Celsius. 2 Publications | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000205903 | 1 – 1828 | SeparinAdd BLAST | 1828 |
Proteomic databases
MaxQBi | P18296 |
PaxDbi | P18296 |
PTM databases
iPTMneti | P18296 |
Interactioni
Subunit structurei
Interacts with cut2.
Interacts with rad21.
1 PublicationProtein-protein interaction databases
BioGRIDi | 276005, 54 interactors |
DIPi | DIP-84N |
ELMi | P18296 |
STRINGi | 4896.SPCC5E4.04.1 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1647 – 1741 | Peptidase C50Add BLAST | 95 |
Phylogenomic databases
eggNOGi | KOG1849, Eukaryota |
HOGENOMi | CLU_237201_0_0_1 |
InParanoidi | P18296 |
OMAi | IYEHMGQ |
PhylomeDBi | P18296 |
Family and domain databases
InterProi | View protein in InterPro IPR005314, Peptidase_C50 IPR030397, SEPARIN_core_dom |
PANTHERi | PTHR12792, PTHR12792, 1 hit |
PROSITEi | View protein in PROSITE PS51700, SEPARIN, 1 hit |
i Sequence
Sequence statusi: Complete.
P18296-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSTRSIVTSK VSWTPEKFIS ALSYPEHCSI TLVKRLKASV KLKDLKQNIS
60 70 80 90 100
RDAPSWTFEH LFVAFKCAVS NLAKQWAELS TTDKEKTRRM FCTPSRLNTA
110 120 130 140 150
HRPEVFYLLE CCTYILEQMQ VVTKNTSHLY DCIRSGVSIC NRLLDMEIFE
160 170 180 190 200
PAISLLMKTH KNLIILLTYR DHDAIPTATL LNPTLDVSEI QLESCLFVPM
210 220 230 240 250
VPASYFLNIG TIVVTFQLNV LRCLSLSQIN GLSLNTINNL QSEDGPFQWI
260 270 280 290 300
ERSFPSQVQL ANSRREILAR LLTRFSMIQN NALQSFKLLI LSIALWLNIL
310 320 330 340 350
SSQRADDKEF DVNQLETRIL QLFSKVVQLC KSEDIEGSIL NKDMTQLHHL
360 370 380 390 400
LENLSKESRL HILLQLSQLY YKYNDFQLSA AYVIRGYSLS FEDISFKLKF
410 420 430 440 450
LLFSFRLSIH DNSICFPFNL IQELSSLQQL FVENALPYSE ALHLLDSIER
460 470 480 490 500
SFRLFNDSTV FDDTVFALNI SEILSWILSS VVRDILVEDE LLNLQLKIRK
510 520 530 540 550
FLMFTFHIIR SFSELTKFQS SLEGCLNLAA YYEDAEFPQK LSNHLYNLCV
560 570 580 590 600
KSSNVNYARE CISLSIKIAV SHKLTNDETY LLKILKNFQL RYHDSLQLQE
610 620 630 640 650
KCDVLHTTFN QLDLYVGTTS VGKSSVLDNI LKRIFNSLTS INDSNIEKLL
660 670 680 690 700
ESISYSLLKL FFKCANEGSR YNASAALSFK LSLMLHEKEE VLLLKTNVSC
710 720 730 740 750
VLANHGYNDI KFEEMVLCVI KGDQNLLEHN SNNNAKLALN ESLLCSWENL
760 770 780 790 800
LCYRRAEDDS RILTIIESWT IFISRFSSVI SRCSFTDFEI NSILNFFFCF
810 820 830 840 850
LHTVEPSGKL TFELAFLEIF YELFNCLLHL QFSKYLVIIG TLLSDKYMTL
860 870 880 890 900
GFSGKAHLFY TKCYSYLRQC KSSPFINFWN VSYGKYLILT GNTDKGILQL
910 920 930 940 950
KKYSLSSEED FNSNGLSRTV SLNLLLYERI QLSDALFQLG YTTVSLGFIM
960 970 980 990 1000
QNLKVIKGLF SKSSKEHFNG GKYITWRLFA VSAHSNVCAA RIYEHMGQAR
1010 1020 1030 1040 1050
EAEFFYRQAC SISEKMPFSC FSATFQLRLC SLLTRAGKLE KGEKILFDLT
1060 1070 1080 1090 1100
EAMKSTDTYH KLLWNYGAAE VCATKSELDG AICHYSECVK LLEIIKSEYY
1110 1120 1130 1140 1150
LFFNRNREKS LTKGIKRLSL SSQPTFVTES NTTEFDDWSI LQNTAANLLR
1160 1170 1180 1190 1200
LISMFELKRG NLEIAKALMT DSTKCSIASF FNIVSANILK SKLIVCEADS
1210 1220 1230 1240 1250
TLFGDPVLRT LPDSVISLPG ISHKFQKNQS KTKALGENTG FRKGSKRLDY
1260 1270 1280 1290 1300
LRERLKINLQ NVRLSCEIIF SNAYERSSVC VCREVNELIS YSTIMQSALT
1310 1320 1330 1340 1350
TIGETTDVDS SSASFFLEIP KALGFHRRRE AQKFRNQHKE LHFSSLEQIL
1360 1370 1380 1390 1400
NSRLSIPDVR TFQDNFIDSL PSIWNVVSIT INNSGEDLFI SKIRKGHSPL
1410 1420 1430 1440 1450
IFRLPLQRHN SRDADEEILV FTKAQTELFR IISKSNQMAQ NGKHYTRRED
1460 1470 1480 1490 1500
KETWWKERRH LDQCLQQLLE NIEISWLGGF KGIFNPHKID TSLFAKFSSQ
1510 1520 1530 1540 1550
FQNIIAKNFN MDKKTPVPTL SPEILELFIT LGKPGYEGYE QLLEDLIYFI
1560 1570 1580 1590 1600
LDIFQFRGLH FAYDEIDTDQ LSMDLQDALN AYFNNYVSEE NRSHTVLVLD
1610 1620 1630 1640 1650
KSVHQFPWES LPCLNRQSVS RVPSLSILRD ILSQSFVVNG EYVEVRKEAG
1660 1670 1680 1690 1700
SYILNPSLDL KHTQEMFEHK LVEGGWKGLI ASQPSNRDFI KMLSGNDFFL
1710 1720 1730 1740 1750
YFGHGGGEQY TTSYDLATLK RCAVTILMGC SSGALYECGS FEPWGTPLDY
1760 1770 1780 1790 1800
LSAGCPTLVA NLWDVTDKDI DRFSLKMLES WGLFENKAPF VNSTSICTAV
1810 1820
SESRSCCHLR YLNGAAPVIY GIPAYIIP
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 430 – 437 | LFVENALP → PLSKMLDR (PubMed:2203537).Curated | 8 | |
Sequence conflicti | 430 – 437 | LFVENALP → PLSKMLDR (PubMed:8978688).Curated | 8 | |
Sequence conflicti | 1125 | T → S (PubMed:2203537).Curated | 1 | |
Sequence conflicti | 1125 | T → S (PubMed:8978688).Curated | 1 | |
Sequence conflicti | 1131 | N → Y (PubMed:2203537).Curated | 1 | |
Sequence conflicti | 1131 | N → Y (PubMed:8978688).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M36179 Genomic DNA Translation: AAB06192.1 CU329672 Genomic DNA Translation: CAA21959.1 |
PIRi | A35694 T41455 |
RefSeqi | NP_587903.1, NM_001022895.2 |
Genome annotation databases
EnsemblFungii | SPCC5E4.04.1; SPCC5E4.04.1:pep; SPCC5E4.04 |
GeneIDi | 2539442 |
KEGGi | spo:SPCC5E4.04 |
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M36179 Genomic DNA Translation: AAB06192.1 CU329672 Genomic DNA Translation: CAA21959.1 |
PIRi | A35694 T41455 |
RefSeqi | NP_587903.1, NM_001022895.2 |
3D structure databases
SMRi | P18296 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 276005, 54 interactors |
DIPi | DIP-84N |
ELMi | P18296 |
STRINGi | 4896.SPCC5E4.04.1 |
PTM databases
iPTMneti | P18296 |
Proteomic databases
MaxQBi | P18296 |
PaxDbi | P18296 |
Genome annotation databases
EnsemblFungii | SPCC5E4.04.1; SPCC5E4.04.1:pep; SPCC5E4.04 |
GeneIDi | 2539442 |
KEGGi | spo:SPCC5E4.04 |
Organism-specific databases
PomBasei | SPCC5E4.04, cut1 |
VEuPathDBi | FungiDB:SPCC5E4.04 |
Phylogenomic databases
eggNOGi | KOG1849, Eukaryota |
HOGENOMi | CLU_237201_0_0_1 |
InParanoidi | P18296 |
OMAi | IYEHMGQ |
PhylomeDBi | P18296 |
Enzyme and pathway databases
BRENDAi | 3.4.22.49, 5613 |
Reactomei | R-SPO-2467813, Separation of Sister Chromatids |
Miscellaneous databases
PROi | PR:P18296 |
Family and domain databases
InterProi | View protein in InterPro IPR005314, Peptidase_C50 IPR030397, SEPARIN_core_dom |
PANTHERi | PTHR12792, PTHR12792, 1 hit |
PROSITEi | View protein in PROSITE PS51700, SEPARIN, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CUT1_SCHPO | |
Accessioni | P18296Primary (citable) accession number: P18296 Secondary accession number(s): O94304 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1990 |
Last sequence update: | August 14, 2001 | |
Last modified: | February 23, 2022 | |
This is version 161 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Schizosaccharomyces pombe
Schizosaccharomyces pombe: entries and gene names