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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

Keywordsi

Molecular functionActin capping, Actin-binding
LigandCalcium

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002187471 – 362SeverinAdd BLAST362

Proteomic databases

PaxDbiP10733.

Interactioni

GO - Molecular functioni

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

Protein-protein interaction databases

STRINGi44689.DDB0232954.

Structurei

Secondary structure

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi162 – 167Combined sources6
Beta strandi173 – 177Combined sources5
Helixi181 – 183Combined sources3
Beta strandi188 – 193Combined sources6
Beta strandi195 – 202Combined sources8
Helixi208 – 224Combined sources17
Turni225 – 227Combined sources3
Beta strandi229 – 235Combined sources7
Helixi243 – 248Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP10733.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati53 – 102Gelsolin-like 1Add BLAST50
Repeati172 – 212Gelsolin-like 2Add BLAST41
Repeati280 – 323Gelsolin-like 3Add BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni162 – 170Polyphosphoinositide bindingBy similarity9

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

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

Family and domain databases

Gene3Di3.40.20.10. 3 hits.
InterProiView protein in InterPro
IPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
PANTHERiPTHR11977. PTHR11977. 1 hit.
PfamiView protein in Pfam
PF00626. Gelsolin. 3 hits.
PRINTSiPR00597. GELSOLIN.
SMARTiView protein in SMART
SM00262. GEL. 3 hits.

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

EnsemblProtistsiEAS66832; EAS66832; 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SVQNMR-A149-262[»]
1SVRNMR-A149-262[»]
1SVYX-ray1.75A149-262[»]
ProteinModelPortaliP10733.
SMRiP10733.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0232954.

Proteomic databases

PaxDbiP10733.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAS66832; EAS66832; 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.
InterProiView protein in InterPro
IPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
PANTHERiPTHR11977. PTHR11977. 1 hit.
PfamiView protein in Pfam
PF00626. Gelsolin. 3 hits.
PRINTSiPR00597. GELSOLIN.
SMARTiView protein in SMART
SM00262. GEL. 3 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiSEVE_DICDI
AccessioniPrimary (citable) accession number: P10733
Secondary accession number(s): Q1ZXC7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: February 15, 2017
This is version 112 of the entry and version 1 of the sequence. See 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.