ID   SCIN_PIG                Reviewed;         125 AA.
AC   Q29297;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Scinderin;
DE   AltName: Full=Adseverin;
DE   Flags: Fragment;
GN   Name=SCIN;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Small intestine;
RX   PubMed=8672129; DOI=10.1007/s003359900153;
RA   Winteroe A.K., Fredholm M., Davies W.;
RT   "Evaluation and characterization of a porcine small intestine cDNA library:
RT   analysis of 839 clones.";
RL   Mamm. Genome 7:509-517(1996).
CC   -!- FUNCTION: Ca(2+)-dependent actin filament-severing protein that has a
CC       regulatory function in exocytosis by affecting the organization of the
CC       microfilament network underneath the plasma membrane. In vitro, also
CC       has barbed end capping and nucleating activities in the presence of
CC       Ca(2+). Severing activity is inhibited by phosphatidylinositol 4,5-bis-
CC       phosphate (PIP2) (By similarity). Required for megakaryocyte
CC       differentiation, maturation, polyploidization and apoptosis with the
CC       release of platelet-like particles (By similarity). Plays a role in
CC       osteoclastogenesis (OCG) and actin cytoskeletal organization in
CC       osteoclasts (By similarity). Regulates chondrocyte proliferation and
CC       differentiation (By similarity). Inhibits cell proliferation and
CC       tumorigenesis. Signaling is mediated by MAPK, p38 and JNK pathways (By
CC       similarity). {ECO:0000250|UniProtKB:Q28046,
CC       ECO:0000250|UniProtKB:Q5ZIV9, ECO:0000250|UniProtKB:Q60604,
CC       ECO:0000250|UniProtKB:Q9Y6U3}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q60604}. Cell projection, podosome
CC       {ECO:0000250|UniProtKB:Q60604}.
CC   -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR   EMBL; F14654; CAA23180.1; -; mRNA.
DR   STRING; 9823.ENSSSCP00000016281; -.
DR   PaxDb; Q29297; -.
DR   PeptideAtlas; Q29297; -.
DR   eggNOG; KOG0443; Eukaryota.
DR   InParanoid; Q29297; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR   GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR   GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0032330; P:regulation of chondrocyte differentiation; ISS:UniProtKB.
DR   Gene3D; 3.40.20.10; -; 2.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR030012; Adseverin.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR007122; Villin/Gelsolin.
DR   PANTHER; PTHR11977; PTHR11977; 1.
DR   PANTHER; PTHR11977:SF78; PTHR11977:SF78; 1.
DR   Pfam; PF00626; Gelsolin; 1.
DR   PRINTS; PR00597; GELSOLIN.
DR   SMART; SM00262; GEL; 1.
PE   2: Evidence at transcript level;
KW   Actin capping; Actin-binding; Calcium; Cell junction; Cell projection;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           <1..>125
FT                   /note="Scinderin"
FT                   /id="PRO_0000218746"
FT   REPEAT          59..99
FT                   /note="Gelsolin-like 1"
FT   BINDING         23..30
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   BINDING         49..57
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   MOD_RES         13
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q60604"
FT   NON_TER         1
FT   NON_TER         125
SQ   SEQUENCE   125 AA;  13971 MW;  16FE9E453B16A966 CRC64;
     TSKPVQNREL QGYESTDFXG YFKGGLKYKA GGVASGFNHV LTNXLSAQRL LHVKGRRVVR
     ATEVPLSWDS FNKGDCFIID LGSEIYQWFG SSCNKYERLK ASQVATGIRD NERNGRSQLI
     VVEEG