ID   SEVE_ECHGR              Reviewed;         374 AA.
AC   Q24800; Q9BJW1; Q9BKM7;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 3.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Severin;
GN   Name=AG8;
OS   Echinococcus granulosus (Hydatid tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC   Echinococcus granulosus group.
OX   NCBI_TaxID=6210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=11384165; DOI=10.1006/expr.2001.4605;
RA   Cortez-Herrera E., Yamamoto R.R., Rodrigues J.J.S., Farias S.E.,
RA   Ferreira H.B., Zaha A.;
RT   "Echinococcus granulosus: cloning and functional in vitro characterization
RT   of an actin filament fragmenting protein.";
RL   Exp. Parasitol. 97:215-225(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zhang L.H., McManus D.P.;
RT   "Cloning of an Echinococcus granulosus protein sharing three functional
RT   domains with gelsolin.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Severin blocks the ends of F-actin and causes the
CC       fragmentation and depolymerization of actin filaments. This severin
CC       binds stably with actin both in a Ca(2+) dependent and a Ca(2+)
CC       independent 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; AF134399; AAK00052.1; -; Genomic_DNA.
DR   EMBL; AF134398; AAK00053.1; -; mRNA.
DR   EMBL; AF329317; AAK15753.1; -; mRNA.
DR   AlphaFoldDB; Q24800; -.
DR   SMR; Q24800; -.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
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; 2.
DR   PRINTS; PR00597; GELSOLIN.
DR   SMART; SM00262; GEL; 3.
PE   2: Evidence at transcript level;
KW   Actin capping; Actin-binding; Calcium; Repeat.
FT   CHAIN           1..374
FT                   /note="Severin"
FT                   /id="PRO_0000218748"
FT   REPEAT          58..109
FT                   /note="Gelsolin-like 1"
FT   REPEAT          180..220
FT                   /note="Gelsolin-like 2"
FT   REPEAT          278..369
FT                   /note="Gelsolin-like 3"
FT   CONFLICT        76
FT                   /note="S -> P (in Ref. 2; AAK15753)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152..155
FT                   /note="Missing (in Ref. 1; AAK00053 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255..258
FT                   /note="Missing (in Ref. 2; AAK15753)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   374 AA;  42162 MW;  43C1ED8B0744443B CRC64;
     MAGLVKAKDY DWKDSNMELF GSSKDRQVKK ESAMTEKCWE PVGRATSPFL MVWRVNQFTL
     EPVPSDEIGN FYNGDSYVIC KATRSPGGDK LLYNVHFWIG KHSTADEYGT AAYKTVELDT
     FLDDAAVQHR EVEGYESQLF KSYFDKLVIL KVILKGGYAS GFRHVKPDEY RPRLLRFCKE
     GKTTYMRQVA FSKQSVHSGD VFILDLGSRA YQFNGSKCSA FEKSSAAAFL QDLESKRNGR
     CNTSVLDEAD TPQDVGVLHE FWTALPDVPV KELEPPKEVI KSLYKLSDSS GKLELTIVSE
     GSASKHDIKP DDVYIILTKE GLFVYIGKDC SVLEKRNALS NAHKFLQTCP NPFLPITVVT
     DEQAESFLKG IWDE