GAS7_MOUSE
ID GAS7_MOUSE Reviewed; 421 AA.
AC Q60780; Q9QY25; Q9QY26; Q9QY34;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Growth arrest-specific protein 7;
DE Short=GAS-7;
GN Name=Gas7;
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], AND CHARACTERIZATION (ISOFORM 1).
RC STRAIN=SWR/J;
RX PubMed=9736752; DOI=10.1073/pnas.95.19.11423;
RA Ju Y.-T., Chang A.C.Y., She B.-R., Tsaur M.-L., Hwang H.-M., Chao C.C.-K.,
RA Cohen S.N., Lin-Chao S.;
RT "Gas7: a gene expressed preferentially in growth-arrested fibroblasts and
RT terminally differentiated Purkinje neurons affects neurite formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11423-11428(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=10552931; DOI=10.1006/geno.1999.5964;
RA Lazakovitch E.M., She B.R., Lien C.L., Woo W.M., Ju Y.T., Lin-Chao S.;
RT "The gas7 gene encodes two protein isoforms differentially expressed within
RT the brain.";
RL Genomics 61:298-306(1999).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Testis;
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).
CC -!- FUNCTION: May play a role in promoting maturation and morphological
CC differentiation of cerebellar neurons.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q60780-1; Sequence=Displayed;
CC Name=2; Synonyms=GAS7-CB;
CC IsoId=Q60780-2; Sequence=VSP_006804, VSP_006805;
CC -!- TISSUE SPECIFICITY: Expressed abundantly in brain with lower levels in
CC heart and testis. In the brain, expressed prominently in the Purkinje
CC layer of the cerebellum, moderately in hippocampus, and less
CC extensively in cerebral cortex and caudate putamen.
CC {ECO:0000269|PubMed:10552931}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U19860; AAA85259.1; -; mRNA.
DR EMBL; AF133184; AAF15397.1; -; mRNA.
DR EMBL; AF135442; AAF15398.1; -; Genomic_DNA.
DR EMBL; AF135442; AAF15399.1; -; Genomic_DNA.
DR PDB; 6IKN; X-ray; 3.00 A; A/B/C/D=102-421.
DR PDB; 6IKO; X-ray; 3.76 A; A/B=5-421.
DR PDBsum; 6IKN; -.
DR PDBsum; 6IKO; -.
DR AlphaFoldDB; Q60780; -.
DR SMR; Q60780; -.
DR IntAct; Q60780; 1.
DR STRING; 10090.ENSMUSP00000104322; -.
DR iPTMnet; Q60780; -.
DR PhosphoSitePlus; Q60780; -.
DR MaxQB; Q60780; -.
DR PaxDb; Q60780; -.
DR PeptideAtlas; Q60780; -.
DR PRIDE; Q60780; -.
DR ProteomicsDB; 267562; -. [Q60780-1]
DR ProteomicsDB; 267563; -. [Q60780-2]
DR UCSC; uc007jmx.2; mouse. [Q60780-2]
DR UCSC; uc033fwm.1; mouse. [Q60780-1]
DR MGI; MGI:1202388; Gas7.
DR eggNOG; KOG0940; Eukaryota.
DR eggNOG; KOG2398; Eukaryota.
DR InParanoid; Q60780; -.
DR PhylomeDB; Q60780; -.
DR ChiTaRS; Gas7; mouse.
DR PRO; PR:Q60780; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60780; protein.
DR GO; GO:0005884; C:actin filament; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:MGI.
DR GO; GO:0030041; P:actin filament polymerization; IDA:MGI.
DR GO; GO:0030182; P:neuron differentiation; IDA:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR CDD; cd07649; F-BAR_GAS7; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR037957; GAS7_F-BAR.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Developmental protein; Differentiation; Neurogenesis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..421
FT /note="Growth arrest-specific protein 7"
FT /id="PRO_0000076058"
FT DOMAIN 22..55
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 141..401
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 254..328
FT /evidence="ECO:0000255"
FT COMPBIAS 36..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60861"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006804"
FT VAR_SEQ 82..101
FT /note="TPAHPPETAHMSLRKSTGDS -> MGKKMSNMENSFDDGSHLSP (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006805"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:6IKN"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6IKN"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:6IKN"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:6IKN"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:6IKN"
FT HELIX 164..204
FT /evidence="ECO:0007829|PDB:6IKN"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:6IKN"
FT HELIX 214..244
FT /evidence="ECO:0007829|PDB:6IKN"
FT HELIX 246..250
FT /evidence="ECO:0007829|PDB:6IKN"
FT HELIX 256..296
FT /evidence="ECO:0007829|PDB:6IKN"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:6IKN"
FT HELIX 310..383
FT /evidence="ECO:0007829|PDB:6IKN"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:6IKN"
FT HELIX 398..409
FT /evidence="ECO:0007829|PDB:6IKN"
SQ SEQUENCE 421 AA; 48174 MW; 8659C5AE3BF36766 CRC64;
MATALQKPGM VPPPPGEESQ TVILPPGWHS YLSPQGRRYY VNTTTNETTW ERPSSSPGIS
ASPAPHRSSL PTTVNGYHAS GTPAHPPETA HMSLRKSTGD SQNLGSSSPG RKQSKENTIT
INCVTFPHPD TMPEQQLLKP TEWSYCDYFW ADKKDPQGNG TVAGFELLLQ KQLKGKQMQK
EMSEFIRERI KIEEEYAKNL AKLSQNSLAA QEEGSLGEAW AQVKKSLADE AEVHLKFSAK
LHSEVEKPLM NFRENFKKDM KKCDHHIADL RKQLASRYAS VEKARKALTE RQKDLEMKTQ
QLEIKLSNKT EEDIKKARRK STQAGDDLMR CVDLYNQAQS KWFEEMVTTT LELERLEVER
VEMIRQHLCQ YTQLRHETDM FNQSTVEPVD QLLRKVDPAK DRELWVREHK TGNIRPVDME
I
