GAS2_MOUSE
ID GAS2_MOUSE Reviewed; 314 AA.
AC P11862;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Growth arrest-specific protein 2;
DE Short=GAS-2;
GN Name=Gas2; Synonyms=Gas-2;
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].
RX PubMed=3409319; DOI=10.1016/s0092-8674(88)91065-3;
RA Schneider C., King R.M., Philipson L.;
RT "Genes specifically expressed at growth arrest of mammalian cells.";
RL Cell 54:787-793(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Embryo, and 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 [3]
RP SUBCELLULAR LOCATION.
RX PubMed=1607387; DOI=10.1083/jcb.117.6.1251;
RA Brancolini C., Bottega S., Schneider C.;
RT "Gas2, a growth arrest-specific protein, is a component of the
RT microfilament network system.";
RL J. Cell Biol. 117:1251-1261(1992).
RN [4]
RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=8120096; DOI=10.1083/jcb.124.5.743;
RA Brancolini C., Schneider C.;
RT "Phosphorylation of the growth arrest-specific protein Gas2 is coupled to
RT actin rearrangements during Go-->G1 transition in NIH 3T3 cells.";
RL J. Cell Biol. 124:743-756(1994).
RN [5]
RP PROTEOLYTIC PROCESSING.
RX PubMed=7489707; DOI=10.1002/j.1460-2075.1995.tb00202.x;
RA Brancolini C., Benedetti M., Schneider C.;
RT "Microfilament reorganization during apoptosis: the role of Gas2, a
RT possible substrate for ICE-like proteases.";
RL EMBO J. 14:5179-5190(1995).
RN [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10049561; DOI=10.1006/dbio.1998.9086;
RA Lee K.K., Tang M.K., Yew D.T., Chow P.H., Yee S.P., Schneider C.,
RA Brancolini C.;
RT "gas2 is a multifunctional gene involved in the regulation of apoptosis and
RT chondrogenesis in the developing mouse limb.";
RL Dev. Biol. 207:14-25(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-188, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
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 [9]
RP STRUCTURE BY NMR OF 198-284.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the GAS2 domain of the growth arrest specific 2
RT protein.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: May play a role in apoptosis by acting as a cell death
CC substrate for caspases. Is cleaved during apoptosis and the cleaved
CC form induces dramatic rearrangements of the actin cytoskeleton and
CC potent changes in the shape of the affected cells. May play a role in
CC chondrocyte proliferation and differentiation, and in limb myogenesis.
CC May be involved in the regulation of the apoptosis in the interdigital
CC tissues of the developing hindlimb. May be involved in the membrane
CC ruffling process. {ECO:0000269|PubMed:10049561}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:8120096}. Membrane {ECO:0000269|PubMed:8120096};
CC Peripheral membrane protein {ECO:0000269|PubMed:8120096}.
CC Note=Component of the microfilament system (PubMed:1607387).
CC Colocalizes with actin fibers at the cell border and along the stress
CC fibers in growth-arrested fibroblasts (PubMed:8120096). Mainly
CC membrane-associated (PubMed:8120096). When hyperphosphorylated,
CC accumulates at membrane ruffles (PubMed:8120096).
CC {ECO:0000269|PubMed:1607387, ECO:0000269|PubMed:8120096}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues. Highest levels in liver,
CC lung and kidney. In the embryo strongly expressed in regions that
CC undergo extensive apoptosis, such as the intervertebral tissues, the
CC cranofacial mesenchyme and the cartilage of the limbs.
CC -!- DEVELOPMENTAL STAGE: At 11.5 dpc and 13.5 dpc strongly expressed in the
CC soft connective tissue of the face and trunk, and in the invertebral
CC tissues. Low levels are found in brain and neural tube. Low levels are
CC found in 13.5 dpc lung, kidney, eye lens and in vertebral cartilage
CC located cranially. In 11.5 dpc hindlimbs weakly expressed by the
CC mesenchymal cells surrounding the perspective cartilage-forming
CC regions. In 12.5 dpc hindlimbs strongly expressed by cells enveloping
CC the chondrogenic primordia of the digits, metatarsals, tibia, and
CC femur, and the soft connective tissue in the interdigital tissues. In
CC 13.5 dpc hindlimbs expression is maintained in the intergigital tissues
CC located proximally and is found in some chondrocytes in the stylopod
CC and in mesenchymal cells surrounding the cartilage in the autopod and
CC zygopod. In 13.5 dpc forelimb strongly expressed in the pre-
CC hypertrophic and hypertrophic regions of the humerus, radius, and ulna.
CC Expression in hypertrophic chondrocytes is maintained at 14.5 dpc and
CC is not detectable at 15.5 dpc. At day 14.5 dpc also expressed by
CC chondrocytes in the cartilage forming the carpals and tarsals and by
CC mesenchymal cells in the process of condensing to form tendons. In 13.5
CC dpc hindlimbs expressed in some myoblasts in the proximal myogenic
CC region. In older limbs expression is maintained in the myotubules.
CC {ECO:0000269|PubMed:10049561}.
CC -!- INDUCTION: Down-regulated by mitogens.
CC -!- PTM: Cleaved, during apoptosis, on a specific aspartic residue by
CC caspases. {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine residues during the G0-G1 transition
CC phase. {ECO:0000269|PubMed:8120096}.
CC -!- SIMILARITY: Belongs to the GAS2 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
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DR EMBL; M21828; AAA37660.1; -; mRNA.
DR EMBL; BC013456; AAH13456.1; -; mRNA.
DR EMBL; BC053446; AAH53446.1; -; mRNA.
DR CCDS; CCDS21310.1; -.
DR PIR; A31590; A31590.
DR RefSeq; NP_001317536.1; NM_001330607.1.
DR RefSeq; NP_032113.1; NM_008087.3.
DR RefSeq; XP_006540687.1; XM_006540624.3.
DR RefSeq; XP_006540688.1; XM_006540625.3.
DR RefSeq; XP_006540689.1; XM_006540626.3.
DR PDB; 1V5R; NMR; -; A=201-284.
DR PDBsum; 1V5R; -.
DR AlphaFoldDB; P11862; -.
DR BMRB; P11862; -.
DR SMR; P11862; -.
DR BioGRID; 199833; 1.
DR STRING; 10090.ENSMUSP00000103217; -.
DR iPTMnet; P11862; -.
DR PhosphoSitePlus; P11862; -.
DR jPOST; P11862; -.
DR MaxQB; P11862; -.
DR PaxDb; P11862; -.
DR PeptideAtlas; P11862; -.
DR PRIDE; P11862; -.
DR ProteomicsDB; 271632; -.
DR Antibodypedia; 12653; 336 antibodies from 32 providers.
DR DNASU; 14453; -.
DR Ensembl; ENSMUST00000051912; ENSMUSP00000053514; ENSMUSG00000030498.
DR Ensembl; ENSMUST00000107591; ENSMUSP00000103217; ENSMUSG00000030498.
DR Ensembl; ENSMUST00000208711; ENSMUSP00000146537; ENSMUSG00000030498.
DR GeneID; 14453; -.
DR KEGG; mmu:14453; -.
DR UCSC; uc009hch.1; mouse.
DR CTD; 2620; -.
DR MGI; MGI:95657; Gas2.
DR VEuPathDB; HostDB:ENSMUSG00000030498; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000155755; -.
DR HOGENOM; CLU_025484_1_0_1; -.
DR InParanoid; P11862; -.
DR OMA; KFKESME; -.
DR OrthoDB; 1343422at2759; -.
DR PhylomeDB; P11862; -.
DR TreeFam; TF323754; -.
DR Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR BioGRID-ORCS; 14453; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Gas2; mouse.
DR EvolutionaryTrace; P11862; -.
DR PRO; PR:P11862; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P11862; protein.
DR Bgee; ENSMUSG00000030498; Expressed in vestibular epithelium and 259 other tissues.
DR ExpressionAtlas; P11862; baseline and differential.
DR Genevisible; P11862; MM.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR GO; GO:0001547; P:antral ovarian follicle growth; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071711; P:basement membrane organization; IMP:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0001544; P:initiation of primordial ovarian follicle growth; IMP:MGI.
DR GO; GO:0030728; P:ovulation; IMP:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:MGI.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.30.920.20; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR003108; GAR_dom.
DR InterPro; IPR036534; GAR_dom_sf.
DR InterPro; IPR029929; GAS2.
DR PANTHER; PTHR46756:SF9; PTHR46756:SF9; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF02187; GAS2; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00243; GAS2; 1.
DR SUPFAM; SSF143575; SSF143575; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51460; GAR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cell cycle; Cell shape; Cytoplasm; Cytoskeleton;
KW Growth arrest; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..314
FT /note="Growth arrest-specific protein 2"
FT /id="PRO_0000190441"
FT DOMAIN 35..157
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 198..271
FT /note="GAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792"
FT REGION 176..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 279..280
FT /note="Cleavage; by a caspase during apoptosis"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 279
FT /note="D->A: Abolishes proteolytic processing."
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:1V5R"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1V5R"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:1V5R"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:1V5R"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:1V5R"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1V5R"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:1V5R"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:1V5R"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:1V5R"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:1V5R"
SQ SEQUENCE 314 AA; 34901 MW; 7F2CC704B4057FAC CRC64;
MMCTALSPKV RSGPGLSDMH QYSQWLASRH EANLLPMKED LALWLTNLLG KEITAETFME
KLDNGALLCQ LAATVQEKFK ESMDANKPAK TLPLKKIPCK ASAPSGSFFA RDNTANFLSW
CRDLGVDETC LFESEGLVLH KQPREVCLCL LELGRIAARY GVEPPGLIKL EKEIEQEETL
SAPSPSPSPS SKSSGKKSTG NLLDDAVKRI SEDPPCKCPT KFCVERLSQG RYRVGEKILF
IRMLHNKHVM VRVGGGWETF AGYLLKHDPC RMLQISRVDG KTSPVQSKSP TLKDMNPDNY
LVVSATYKAK KEIK
