SEVE_DICDI
ID SEVE_DICDI Reviewed; 362 AA.
AC P10733; Q1ZXC7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Severin;
GN Name=sevA; ORFNames=DDB_G0289327;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2826459; DOI=10.1016/s0021-9258(19)35412-2;
RA Andre E., Lottspeich F., Schleicher M., Noegel A.;
RT "Severin, gelsolin, and villin share a homologous sequence in regions
RT presumed to contain F-actin severing domains.";
RL J. Biol. Chem. 263:722-727(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP INTERACTION WITH ACTIN.
RX PubMed=1847147; DOI=10.1083/jcb.112.4.665;
RA Eichinger L., Noegel A.A., Schleicher M.;
RT "Domain structure in actin-binding proteins: expression and functional
RT characterization of truncated severin.";
RL J. Cell Biol. 112:665-676(1991).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
RN [5]
RP STRUCTURE BY NMR OF 149-262.
RX PubMed=7897658; DOI=10.1006/jmbi.1994.0118;
RA Schnuchel A., Wiltscheck R., Eichinger L., Schleicher M., Holak T.A.;
RT "Structure of severin domain 2 in solution.";
RL J. Mol. Biol. 247:21-27(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 158-259.
RX PubMed=10820002; DOI=10.1021/bi992364d;
RA Puius Y.A., Fedorov E.V., Eichinger L., Schleicher M., Almo S.C.;
RT "Mapping the functional surface of domain 2 in the gelsolin superfamily.";
RL Biochemistry 39:5322-5331(2000).
CC -!- FUNCTION: Severin blocks the ends of F-actin and causes the
CC fragmentation and depolymerization of actin filaments in a Ca(2+)
CC dependent manner.
CC -!- MISCELLANEOUS: Severin changes its conformation upon binding of Ca(2+)
CC and then interacts with F-actin.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; J03515; AAA33250.1; -; mRNA.
DR EMBL; AAFI02000139; EAS66832.1; -; Genomic_DNA.
DR PIR; A28517; A28517.
DR RefSeq; XP_001134515.1; XM_001134515.1.
DR PDB; 1SVQ; NMR; -; A=149-262.
DR PDB; 1SVR; NMR; -; A=149-262.
DR PDB; 1SVY; X-ray; 1.75 A; A=149-262.
DR PDBsum; 1SVQ; -.
DR PDBsum; 1SVR; -.
DR PDBsum; 1SVY; -.
DR AlphaFoldDB; P10733; -.
DR SMR; P10733; -.
DR STRING; 44689.DDB0232954; -.
DR PaxDb; P10733; -.
DR EnsemblProtists; EAS66832; EAS66832; DDB_G0289327.
DR GeneID; 8627096; -.
DR KEGG; ddi:DDB_G0289327; -.
DR dictyBase; DDB_G0289327; sevA.
DR eggNOG; KOG0443; Eukaryota.
DR HOGENOM; CLU_002568_0_1_1; -.
DR InParanoid; P10733; -.
DR OMA; LHSYKVG; -.
DR PhylomeDB; P10733; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; P10733; -.
DR PRO; PR:P10733; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0048306; F:calcium-dependent protein binding; TAS:dictyBase.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0030043; P:actin filament fragmentation; IDA:dictyBase.
DR GO; GO:0051014; P:actin filament severing; IDA:dictyBase.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR Gene3D; 3.40.20.10; -; 3.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR Pfam; PF00626; Gelsolin; 3.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Actin capping; Actin-binding; Calcium;
KW Direct protein sequencing; Reference proteome; Repeat.
FT CHAIN 1..362
FT /note="Severin"
FT /id="PRO_0000218747"
FT REPEAT 53..102
FT /note="Gelsolin-like 1"
FT REPEAT 172..212
FT /note="Gelsolin-like 2"
FT REPEAT 280..323
FT /note="Gelsolin-like 3"
FT BINDING 162..170
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:1SVY"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1SVY"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1SVY"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1SVY"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:1SVY"
FT HELIX 208..224
FT /evidence="ECO:0007829|PDB:1SVY"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1SVY"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:1SVY"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:1SVY"
SQ SEQUENCE 362 AA; 39870 MW; F0659BFA39C85F5B CRC64;
MIKNRKLDIT STNVAGIGTD LDKKCRLDAA STEAQWKGVG QAPGLKIWRI ENFKVVPVPE
SSYGKFYDGD SYIILHTFKE GNSLKHDIHF FLGTFTTQDE AGTAAYKTVE LDDFLGGAPI
QYRQCQSYES PSFLSLFPKY FILSGGVESG FNHVKPTEYK PRLLHISGDK NAKVAEVPLA
TSSLNSGDCF LLDAGLTIYQ FNGSKSSPQE KNKAAEVARA IDAERKGLPK VEVFCETDSD
IPAEFWKLLG GKGAIAAKHE TAPTKSEKVL YKLSDASGSL KFSEVSRGKI NKSSLKSEDV
FIIDLGNEIY TWIGSKSSPN EKKTAFSHAT QYLVNNKRCE YTPIVRVLEN GTNQSFETLL
SA
