SCIN_BOVIN
ID SCIN_BOVIN Reviewed; 715 AA.
AC Q28046; Q27948;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Scinderin {ECO:0000303|Ref.2};
DE Short=SC {ECO:0000303|Ref.2};
DE AltName: Full=Adseverin {ECO:0000303|PubMed:8119933};
GN Name=SCIN {ECO:0000303|Ref.2};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal medulla;
RX PubMed=8119933; DOI=10.1016/s0021-9258(17)37545-2;
RA Nakamura S., Sakurai T., Nonomura Y.;
RT "Differential expression of bovine adseverin in adrenal gland revealed by
RT in situ hybridization. Cloning of a cDNA for adseverin.";
RL J. Biol. Chem. 269:5890-5896(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Adrenal medulla;
RA Marcu M.G., Rodriguez del Castillo A., Trifaro J.-M.;
RT "Molecular cloning of bovine chromaffin cell scinderin (Sc) cDNA reveals
RT actin and polyphosphoinositide domains.";
RL Can. J. Physiol. Pharmacol. 72:246-246(1994).
RN [3]
RP PROTEIN SEQUENCE OF 364-375, AND DOMAIN FUNCTION.
RC TISSUE=Adrenal medulla;
RX PubMed=1847925; DOI=10.1016/s0021-9258(20)64362-9;
RA Sakurai T., Kurokawa H., Nonomura Y.;
RT "The Ca2(+)-dependent actin filament-severing activity of 74-kDa protein
RT (adseverin) resides in its NH2-terminal half.";
RL J. Biol. Chem. 266:4581-4585(1991).
RN [4]
RP PROTEIN SEQUENCE OF 129-137 AND 243-247, AND FUNCTION.
RC TISSUE=Adrenal medulla;
RX PubMed=1651929; DOI=10.1016/s0021-9258(18)98504-2;
RA Sakurai T., Kurokawa H., Nonomura Y.;
RT "Comparison between the gelsolin and adseverin domain structure.";
RL J. Biol. Chem. 266:15979-15983(1991).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND ACTIN-BINDING.
RX PubMed=8780652; DOI=10.1016/s0896-6273(00)80160-9;
RA Zhang L., Marcu M.G., Nau-Staudt K., Trifaro J.M.;
RT "Recombinant scinderin enhances exocytosis, an effect blocked by two
RT scinderin-derived actin-binding peptides and PIP2.";
RL Neuron 17:287-296(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+) (PubMed:1651929, PubMed:1847925, PubMed:8780652). Severing
CC activity is inhibited by phosphatidylinositol 4,5-bis-phosphate (PIP2)
CC (PubMed:8780652). Required for megakaryocyte differentiation,
CC maturation, polyploidization and apoptosis with the release of
CC 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:Q5ZIV9,
CC ECO:0000250|UniProtKB:Q60604, ECO:0000250|UniProtKB:Q9Y6U3,
CC ECO:0000269|PubMed:1651929, ECO:0000269|PubMed:1847925,
CC ECO:0000269|PubMed:8780652}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, podosome {ECO:0000250|UniProtKB:Q60604}.
CC -!- TISSUE SPECIFICITY: In the adrenal gland, expressed in the medulla but,
CC in the cortex, found only in diffuse parts.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; D26549; BAA05548.1; -; mRNA.
DR EMBL; X78479; CAA55227.1; -; mRNA.
DR PIR; A53209; A53209.
DR PIR; I45832; I45832.
DR RefSeq; NP_776602.1; NM_174177.2.
DR AlphaFoldDB; Q28046; -.
DR SMR; Q28046; -.
DR STRING; 9913.ENSBTAP00000012910; -.
DR PeptideAtlas; Q28046; -.
DR PRIDE; Q28046; -.
DR GeneID; 281478; -.
DR KEGG; bta:281478; -.
DR CTD; 85477; -.
DR eggNOG; KOG0443; Eukaryota.
DR InParanoid; Q28046; -.
DR OrthoDB; 1376537at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0051014; P:actin filament severing; IDA:UniProtKB.
DR GO; GO:0045010; P:actin nucleation; IDA:UniProtKB.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0051047; P:positive regulation of secretion; IDA:UniProtKB.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; ISS: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 1: Evidence at protein level;
KW Actin capping; Actin-binding; Calcium; Cell junction; Cell projection;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..715
FT /note="Scinderin"
FT /id="PRO_0000218743"
FT REPEAT 27..77
FT /note="Gelsolin-like 1"
FT REPEAT 148..188
FT /note="Gelsolin-like 2"
FT REPEAT 265..307
FT /note="Gelsolin-like 3"
FT REPEAT 398..451
FT /note="Gelsolin-like 4"
FT REPEAT 523..564
FT /note="Gelsolin-like 5"
FT REPEAT 626..668
FT /note="Gelsolin-like 6"
FT REGION 1..363
FT /note="Actin-severing"
FT /evidence="ECO:0000255"
FT REGION 364..715
FT /note="Actin-binding, Ca-sensitive"
FT /evidence="ECO:0000255"
FT REGION 364..715
FT /note="Ca(2+)-dependent actin binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6U3"
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 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 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 MOD_RES 102
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60604"
FT MOD_RES 599
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q60604"
FT CONFLICT 231..232
FT /note="RD -> TH (in Ref. 2; CAA55227)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="V -> L (in Ref. 2; CAA55227)"
FT /evidence="ECO:0000305"
FT CONFLICT 454..466
FT /note="AFLTVQLDRSLGG -> DSRLFSWIDPSGD (in Ref. 2;
FT CAA55227)"
FT /evidence="ECO:0000305"
FT CONFLICT 520..522
FT /note="ASI -> DSY (in Ref. 2; CAA55227)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 715 AA; 80578 MW; A1FD7DDFC02DA044 CRC64;
MAQGLYHEEF ARAGKRAGLQ VWRIEKLELV PVPESAYGNF YVGDAYLVLH TTQASRGFTY
RLHFWLGKEC TQDESTAAAI FTVQMDDYLG GKPVQNRELQ GYESTDFVGY FKGGLKYKAG
GVASGLNHVL TNDLTAQRLL HVKGRRVVRA TEVPLSWDSF NKGDCFIIDL GTEIYQWCGS
SCNKYERLKA SQVAIGIRDN ERKGRAQLIV VEEGSEPSEL TKVLGEKPKL RDGEDDDDIK
ADITNRKMAK LYMVSDASGS MKVSLVAEEN PFSMAMLLSE ECFILDHGAA KQIFVWKGKD
ANPQERKAAM KTAEEFLQQM NYSTNTQIQV LPEGGETPIF KQFFKDWRDR DQSDGFGKVY
VTEKVAHVKQ IPFDASKLHS SPQMAAQHHV VDDGSGKVQI WRVENNGRVE IDRNSYGEFY
GGDCYIILYT YPRGQIIYTW QGANATRDEL TTSAFLTVQL DRSLGGQAVQ IRVSQGKEPA
HLLSLFKDKP LIIYKNGTSK KEGQAPAPPI RLFQVRRNLA SITRIMEVDV DANSLNSNDV
FVLKLRQNNG YIWIGKGSTQ EEEKGAEYVA SVLKCKTSTI QEGKEPEEFW NSLGGKKDYQ
TSPLLESQAE DHPPRLYGCS NKTGRFIIEE VPGEFTQDDL AEDDVMLLDA WEQIFIWIGK
DANEVEKSES LKSAKIYLET DPSGRDKRTP IVIIKQGHEP PTFTGWFLGW DSSRW
