SCIN_MOUSE
ID SCIN_MOUSE Reviewed; 715 AA.
AC Q60604; O08988; O08990; Q6P4N8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Scinderin;
DE AltName: Full=Adseverin;
DE AltName: Full=Gelsolin-like protein;
GN Name=Scin;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, FUNCTION, FUNCTION
RP (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Lymph node;
RX PubMed=9671468; DOI=10.1128/mcb.18.8.4589;
RA Robbens J., Louahed J., De Pestel K., Van Colen I., Ampe C.,
RA Vandekerckhove J., Renauld J.-C.;
RT "Murine adseverin (D5), a novel member of the gelsolin family, and murine
RT adseverin are induced by interleukin-9 in T-helper lymphocytes.";
RL Mol. Cell. Biol. 18:4589-4596(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-102 AND TYR-599, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=25275604; DOI=10.1371/journal.pone.0109078;
RA Hassanpour S., Jiang H., Wang Y., Kuiper J.W., Glogauer M.;
RT "The actin binding protein adseverin regulates osteoclastogenesis.";
RL PLoS ONE 9:E109078-E109078(2014).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=25681458; DOI=10.1096/fj.14-265744;
RA Jiang H., Wang Y., Viniegra A., Sima C., McCulloch C.A., Glogauer M.;
RT "Adseverin plays a role in osteoclast differentiation and periodontal
RT disease-mediated bone loss.";
RL FASEB J. 29:2281-2291(2015).
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 (PubMed:9671468).
CC Severing activity is inhibited by phosphatidylinositol 4,5-bis-
CC phosphate (PIP2) (By similarity). In vitro, also has barbed end capping
CC and nucleating activities in the presence of Ca(2+) (PubMed:9671468).
CC Required for megakaryocyte differentiation, maturation,
CC polyploidization and apoptosis with the release of platelet-like
CC particles (By similarity). Plays a role in osteoclastogenesis (OCG) and
CC actin cytoskeletal organization in osteoclasts (PubMed:25275604,
CC PubMed:25681458). 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:Q9Y6U3,
CC ECO:0000269|PubMed:25275604, ECO:0000269|PubMed:25681458,
CC ECO:0000269|PubMed:9671468}.
CC -!- FUNCTION: [Isoform 2]: Fails to nucleate actin polymerization, although
CC it severs and caps actin filaments in a Ca(2+)-dependent manner.
CC {ECO:0000269|PubMed:9671468}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, podosome {ECO:0000269|PubMed:25681458}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q60604-1; Sequence=Displayed;
CC Name=2; Synonyms=D5 {ECO:0000303|PubMed:9671468};
CC IsoId=Q60604-2; Sequence=VSP_006730;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in mature osteoclasts
CC (at protein level) (PubMed:25275604). Isoform 2 is expressed in blood
CC cells (PubMed:9671468). {ECO:0000269|PubMed:25275604,
CC ECO:0000269|PubMed:9671468}.
CC -!- DEVELOPMENTAL STAGE: Expression is induced during osteoclastogenesis.
CC {ECO:0000269|PubMed:25275604}.
CC -!- DISRUPTION PHENOTYPE: Knockdown in bone marrow monocytes protect mice
CC from bone resorption in periodontal disease model.
CC {ECO:0000269|PubMed:25681458}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; U04354; AAB61682.1; -; mRNA.
DR EMBL; Y13971; CAA74304.1; -; mRNA.
DR EMBL; AK133484; BAE21681.1; -; mRNA.
DR EMBL; BC063328; AAH63328.1; -; mRNA.
DR CCDS; CCDS25891.1; -. [Q60604-2]
DR CCDS; CCDS49055.1; -. [Q60604-1]
DR PIR; T10049; T10049.
DR RefSeq; NP_001139668.1; NM_001146196.1. [Q60604-1]
DR RefSeq; NP_033158.2; NM_009132.2. [Q60604-2]
DR AlphaFoldDB; Q60604; -.
DR SMR; Q60604; -.
DR BioGRID; 203095; 1.
DR STRING; 10090.ENSMUSP00000002640; -.
DR iPTMnet; Q60604; -.
DR PhosphoSitePlus; Q60604; -.
DR EPD; Q60604; -.
DR jPOST; Q60604; -.
DR MaxQB; Q60604; -.
DR PaxDb; Q60604; -.
DR PeptideAtlas; Q60604; -.
DR PRIDE; Q60604; -.
DR ProteomicsDB; 296189; -. [Q60604-1]
DR ProteomicsDB; 296190; -. [Q60604-2]
DR Antibodypedia; 6300; 108 antibodies from 23 providers.
DR DNASU; 20259; -.
DR Ensembl; ENSMUST00000002640; ENSMUSP00000002640; ENSMUSG00000002565. [Q60604-1]
DR Ensembl; ENSMUST00000078481; ENSMUSP00000077573; ENSMUSG00000002565. [Q60604-2]
DR GeneID; 20259; -.
DR KEGG; mmu:20259; -.
DR UCSC; uc007nkw.2; mouse. [Q60604-1]
DR UCSC; uc011yln.1; mouse. [Q60604-2]
DR CTD; 85477; -.
DR MGI; MGI:1306794; Scin.
DR VEuPathDB; HostDB:ENSMUSG00000002565; -.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000159083; -.
DR HOGENOM; CLU_002568_3_0_1; -.
DR InParanoid; Q60604; -.
DR OMA; GHESTDF; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; Q60604; -.
DR TreeFam; TF313468; -.
DR BioGRID-ORCS; 20259; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Scin; mouse.
DR PRO; PR:Q60604; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q60604; protein.
DR Bgee; ENSMUSG00000002565; Expressed in ectoplacental cone and 109 other tissues.
DR Genevisible; Q60604; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
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:0032991; C:protein-containing complex; ISO:MGI.
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:0051693; P:actin filament capping; ISO:MGI.
DR GO; GO:0051014; P:actin filament severing; ISO:MGI.
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:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0051127; P:positive regulation of actin nucleation; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; ISO:MGI.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0042989; P:sequestering of actin monomers; ISO:MGI.
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; Alternative splicing; Calcium; Cell junction;
KW Cell projection; Cytoplasm; Cytoskeleton; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..715
FT /note="Scinderin"
FT /id="PRO_0000218745"
FT REPEAT 27..76
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="Ca(2+)-dependent actin binding"
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 MOD_RES 102
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 599
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT VAR_SEQ 528..627
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006730"
FT CONFLICT 44..45
FT /note="DA -> EP (in Ref. 1; AAB61682/CAA74304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 715 AA; 80254 MW; 6EF9F45FBC82E249 CRC64;
MAQELQHPEF ARAGQQAGLQ VWRVEKLELV PVPQGAYGDF YVGDAYLVLH TTKSSRGFSY
RLHFWLGKEC SQDESTAAAI FTVQMDDYLG GKPVQSRELQ GYESTDFVGY FKGGLKYKAG
GVASGLNHVL TNDLTAKRLL HVKGRRVVRA TEVPLSWESF NKGDCFIIDL GTEIYQWCGS
SCNKYERLKA SQVAIGIRDN ERKGRSQLIV VEEGSEPSEL MKVLGRKPEL PDGDNDDDVV
ADISNRKMAK LYMVSDASGS MKVTLVAEEN PFSMGMLLSE ECFILDHGAA KQIFVWKGKN
ANPQERKTAM KTAEEFLQKM KYSTNTQIQV LPEGGETPIF KQFFKDWKDK DQSDGFGKVY
ITEKVAQIKQ IPFDASKLHS SPQMAAQHNM VDDGSGGVEI WRVENSGRVQ IDPSSYGEFY
GGDCYIILYT YPRGQIIYTW QGANATRDEL TMSAFLTVQL DRSLGGQAVQ VRVSQGKEPA
HLLSLFKDKP LIIYKNGTSK KEGQAPAPPT RLFQVRRNLA SITRIVEVDV DANSLNSNDT
FVLKLPRNNG FIWIGKGASQ EEEKGAEYVA DVLKCKASRI QEGKEPEEFW NSLGGRGDYQ
TSPLLETRAE DHPPRLYGCS NKTGRFIIEE VPGEFTQDDL AEDDVMLLDA WEQIFIWIGK
DANEVEKKES VKSAKMYLET DPSGRDKRTP IVIIKQGHEP PTFTGWFLGW DSSRW
