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Protein

Severin

Gene

sevA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Severin blocks the ends of F-actin and causes the fragmentation and depolymerization of actin filaments in a Ca2+ dependent manner.

GO - Molecular functioni

  • actin filament binding Source: dictyBase
  • calcium-dependent protein binding Source: dictyBase

GO - Biological processi

  • actin filament capping Source: UniProtKB-KW
  • actin filament fragmentation Source: dictyBase
  • actin filament severing Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding, Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Severin
Gene namesi
Name:sevA
ORF Names:DDB_G0289327
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 5, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0289327. sevA.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: dictyBase
  • phagocytic vesicle Source: dictyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 362362SeverinPRO_0000218747Add
BLAST

Proteomic databases

PaxDbiP10733.
PRIDEiP10733.

Interactioni

GO - Molecular functioni

  • actin filament binding Source: dictyBase
  • calcium-dependent protein binding Source: dictyBase

Protein-protein interaction databases

STRINGi44689.DDB0232954.

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi162 – 1676Combined sources
Beta strandi173 – 1775Combined sources
Helixi181 – 1833Combined sources
Beta strandi188 – 1936Combined sources
Beta strandi195 – 2028Combined sources
Helixi208 – 22417Combined sources
Turni225 – 2273Combined sources
Beta strandi229 – 2357Combined sources
Helixi243 – 2486Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SVQNMR-A149-262[»]
1SVRNMR-A149-262[»]
1SVYX-ray1.75A149-262[»]
ProteinModelPortaliP10733.
SMRiP10733. Positions 158-251.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10733.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati53 – 10250Gelsolin-like 1Add
BLAST
Repeati172 – 21241Gelsolin-like 2Add
BLAST
Repeati280 – 32344Gelsolin-like 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni162 – 1709Polyphosphoinositide bindingBy similarity

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated
Contains 3 gelsolin-like repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
InParanoidiP10733.
KOiK05768.
OMAiDDDDNYW.
PhylomeDBiP10733.

Family and domain databases

Gene3Di3.40.20.10. 3 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PfamiPF00626. Gelsolin. 3 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10733-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKNRKLDIT STNVAGIGTD LDKKCRLDAA STEAQWKGVG QAPGLKIWRI
60 70 80 90 100
ENFKVVPVPE SSYGKFYDGD SYIILHTFKE GNSLKHDIHF FLGTFTTQDE
110 120 130 140 150
AGTAAYKTVE LDDFLGGAPI QYRQCQSYES PSFLSLFPKY FILSGGVESG
160 170 180 190 200
FNHVKPTEYK PRLLHISGDK NAKVAEVPLA TSSLNSGDCF LLDAGLTIYQ
210 220 230 240 250
FNGSKSSPQE KNKAAEVARA IDAERKGLPK VEVFCETDSD IPAEFWKLLG
260 270 280 290 300
GKGAIAAKHE TAPTKSEKVL YKLSDASGSL KFSEVSRGKI NKSSLKSEDV
310 320 330 340 350
FIIDLGNEIY TWIGSKSSPN EKKTAFSHAT QYLVNNKRCE YTPIVRVLEN
360
GTNQSFETLL SA
Length:362
Mass (Da):39,870
Last modified:July 1, 1989 - v1
Checksum:iF0659BFA39C85F5B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03515 mRNA. Translation: AAA33250.1.
AAFI02000139 Genomic DNA. Translation: EAS66832.1.
PIRiA28517.
RefSeqiXP_001134515.1. XM_001134515.1.

Genome annotation databases

EnsemblProtistsiDDB0232954; DDB0232954; DDB_G0289327.
GeneIDi8627096.
KEGGiddi:DDB_G0289327.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03515 mRNA. Translation: AAA33250.1.
AAFI02000139 Genomic DNA. Translation: EAS66832.1.
PIRiA28517.
RefSeqiXP_001134515.1. XM_001134515.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SVQNMR-A149-262[»]
1SVRNMR-A149-262[»]
1SVYX-ray1.75A149-262[»]
ProteinModelPortaliP10733.
SMRiP10733. Positions 158-251.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0232954.

Proteomic databases

PaxDbiP10733.
PRIDEiP10733.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0232954; DDB0232954; DDB_G0289327.
GeneIDi8627096.
KEGGiddi:DDB_G0289327.

Organism-specific databases

dictyBaseiDDB_G0289327. sevA.

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
InParanoidiP10733.
KOiK05768.
OMAiDDDDNYW.
PhylomeDBiP10733.

Miscellaneous databases

EvolutionaryTraceiP10733.
PROiP10733.

Family and domain databases

Gene3Di3.40.20.10. 3 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PfamiPF00626. Gelsolin. 3 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains."
    Andre E., Lottspeich F., Schleicher M., Noegel A.
    J. Biol. Chem. 263:722-727(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "The genome of the social amoeba Dictyostelium discoideum."
    Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
    , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
    Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.
  3. "Domain structure in actin-binding proteins: expression and functional characterization of truncated severin."
    Eichinger L., Noegel A.A., Schleicher M.
    J. Cell Biol. 112:665-676(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACTIN.
  4. "Proteomics fingerprinting of phagosome maturation and evidence for the role of a Galpha during uptake."
    Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M., Soldati T.
    Mol. Cell. Proteomics 5:2228-2243(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: AX2.
  5. Cited for: STRUCTURE BY NMR OF 149-262.
  6. "Mapping the functional surface of domain 2 in the gelsolin superfamily."
    Puius Y.A., Fedorov E.V., Eichinger L., Schleicher M., Almo S.C.
    Biochemistry 39:5322-5331(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 158-259.

Entry informationi

Entry nameiSEVE_DICDI
AccessioniPrimary (citable) accession number: P10733
Secondary accession number(s): Q1ZXC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: December 9, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

Severin changes its conformation upon binding of Ca2+ and then interacts with F-actin.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.