SCIN_CHICK
ID SCIN_CHICK Reviewed; 717 AA.
AC Q5ZIV9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Scinderin;
DE AltName: Full=Adseverin;
GN Name=SCIN; ORFNames=RCJMB04_23d8;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=17097081; DOI=10.1016/j.ydbio.2006.09.052;
RA Nurminsky D., Magee C., Faverman L., Nurminskaya M.;
RT "Regulation of chondrocyte differentiation by actin-severing protein
RT adseverin.";
RL Dev. Biol. 302:427-437(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 (PubMed:17097081). 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:Q60604, ECO:0000250|UniProtKB:Q9Y6U3,
CC ECO:0000269|PubMed:17097081}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q60604}. Cell projection, podosome
CC {ECO:0000250|UniProtKB:Q60604}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the pre-hypertrophic and hypertrophic
CC cartilage of the embryonic growth plate. {ECO:0000269|PubMed:17097081}.
CC -!- INDUCTION: Up-regulated in pre-hypertrophic and hypertrophic
CC chondrocytes during the embryonic development of long bones.
CC {ECO:0000269|PubMed:17097081}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG32334.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAG32334.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ020143; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ720675; CAG32334.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001231522.1; NM_001244593.1.
DR AlphaFoldDB; Q5ZIV9; -.
DR SMR; Q5ZIV9; -.
DR STRING; 9031.ENSGALP00000017495; -.
DR PaxDb; Q5ZIV9; -.
DR GeneID; 420588; -.
DR KEGG; gga:420588; -.
DR CTD; 85477; -.
DR VEuPathDB; HostDB:geneid_420588; -.
DR eggNOG; KOG0443; Eukaryota.
DR HOGENOM; CLU_002568_3_2_1; -.
DR InParanoid; Q5ZIV9; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; Q5ZIV9; -.
DR PRO; PR:Q5ZIV9; -.
DR Proteomes; UP000000539; 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; IDA:UniProtKB.
DR Gene3D; 3.40.20.10; -; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR030012; Adseverin.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR PANTHER; PTHR11977:SF78; PTHR11977:SF78; 1.
DR Pfam; PF00626; Gelsolin; 6.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
DR SUPFAM; SSF82754; SSF82754; 1.
PE 2: Evidence at transcript level;
KW Actin capping; Actin-binding; Calcium; Cell junction; Cell projection;
KW Cytoplasm; Cytoskeleton; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..717
FT /note="Scinderin"
FT /id="PRO_0000404255"
FT REPEAT 28..108
FT /note="Gelsolin-like 1"
FT REPEAT 148..220
FT /note="Gelsolin-like 2"
FT REPEAT 265..340
FT /note="Gelsolin-like 3"
FT REPEAT 408..483
FT /note="Gelsolin-like 4"
FT REPEAT 526..590
FT /note="Gelsolin-like 5"
FT REPEAT 628..703
FT /note="Gelsolin-like 6"
FT REGION 1..363
FT /note="Actin-severing"
FT /evidence="ECO:0000250"
FT REGION 364..715
FT /note="Ca(2+)-dependent actin binding"
FT /evidence="ECO:0000250"
FT BINDING 112..119
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 138..146
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 538
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6U3"
FT BINDING 539
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6U3"
FT BINDING 562
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6U3"
FT BINDING 643
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6U3"
FT BINDING 644
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6U3"
FT BINDING 666
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6U3"
FT CONFLICT 96
FT /note="S -> R (in Ref. 1; DQ020143)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="E -> K (in Ref. 2; CAG32334)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="L -> V (in Ref. 2; CAG32334)"
FT /evidence="ECO:0000305"
FT CONFLICT 253..254
FT /note="MV -> KA (in Ref. 1; DQ020143)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="N -> D (in Ref. 1; DQ020143)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="D -> V (in Ref. 1; DQ020143)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="N -> T (in Ref. 1; DQ020143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 717 AA; 80533 MW; 1447FE1421E19AE7 CRC64;
MAPERHPPAF EGAGQESGLQ VWRVERLELV PVPPSRHGDF FVGDAYLVLH TVRRGAAVAY
RLHYWLGKEC TQDESTAAAI FTVQLDDYLG GKPVQSREIQ GYESNEFVSY FKGGIKYKAG
GVASGFNHVV TNDLSAQRLL HIKGRRVVRA TEVPLTWASF NKGDCFIIDL GNEIYQWCGS
SCNKYERLKA TQVAVGIRDN ERNGRSRLIT VEEGSEPDEL ITVLGEKPEL PECSDDDDEM
ADIANRKSAK LYMVSDASGS MKLSVVAEEN PFSMAMLLSE ECFILDNGAA RKIFVWKGKD
ANPQERKAAM KNAETFVQQM NYPANTQIQV LPEGGETPIF KQFFKDWKDK DQSDGFGKVY
VTERVAKIEQ IEFDATKLHE SPQMAAQHNM IDDGSGKVQI WRVESSGRVP VEPETYGQFY
GGDCYIILYT YPKGQIIYTW QGACATKDEL TASAFLTVQL DRSLNDQAVQ IRVSQGKEPP
HLLSLFKNKP LIVYKNGTSK KEGQKPAPPT RLFQIRRNLM SVTRIAEVDV DAMSLNSNDA
FVLKLPNNTG YTWVGKGVNK EEEQGAQYIA SVLKCQTAKI NEGQEPEEFW KALGGKKKYQ
TSSQLLTKAE DHPPRLFGCS NKTGRFIIEE VPGEFTQDDL AEDDVMLLDA WEQVFVWIGK
EANETERQES VKSAKRYIET DPSGRDKGTP IVIVKQGHEP PTFTGWFLAW DSNKWKN
