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Database: UniProt
Entry: GAS7_RAT
LinkDB: GAS7_RAT
Original site: GAS7_RAT 
ID   GAS7_RAT                Reviewed;         422 AA.
AC   O55148;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=Growth arrest-specific protein 7;
DE            Short=GAS-7;
GN   Name=Gas7;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Chao C.C.-K., Kuo J.D., Su L.J., Liu C.H., Lih C.J., Cohen S.N.,
RA   Lin-Chao S.;
RT   "Rat gas-7: a growth-arrest-specific gene in fibroblasts is preferentially
RT   expressed in terminally differentiated Purkinje neurons and associated with
RT   the differentiation of cultured PC12 cells.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in promoting maturation and morphological
CC       differentiation of cerebellar neurons.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA05907.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA10525.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ003148; CAA05907.1; ALT_INIT; mRNA.
DR   EMBL; AJ131902; CAA10525.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; O55148; -.
DR   SMR; O55148; -.
DR   STRING; 10116.ENSRNOP00000068570; -.
DR   PhosphoSitePlus; O55148; -.
DR   PaxDb; 10116-ENSRNOP00000067551; -.
DR   UCSC; RGD:621550; rat.
DR   AGR; RGD:621550; -.
DR   RGD; 621550; Gas7.
DR   eggNOG; KOG0940; Eukaryota.
DR   eggNOG; KOG2398; Eukaryota.
DR   InParanoid; O55148; -.
DR   PhylomeDB; O55148; -.
DR   PRO; PR:O55148; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005884; C:actin filament; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR   GO; GO:0051017; P:actin filament bundle assembly; ISO:RGD.
DR   GO; GO:0030041; P:actin filament polymerization; ISO:RGD.
DR   GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR   GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD.
DR   GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR   CDD; cd07649; F-BAR_GAS7; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 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   PANTHER; PTHR23065:SF57; GROWTH ARREST-SPECIFIC PROTEIN 7; 1.
DR   PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00397; WW; 1.
DR   Pfam; PF16623; WW_FCH_linker; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Developmental protein; Differentiation;
KW   Neurogenesis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..422
FT                   /note="Growth arrest-specific protein 7"
FT                   /id="PRO_0000076059"
FT   DOMAIN          22..55
FT                   /note="WW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          141..402
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..329
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:0000250|UniProtKB:Q60780"
SQ   SEQUENCE   422 AA;  48275 MW;  FD14E4CB4DFB01F9 CRC64;
     MATALQKPGM VPPPPGEESQ TVILPPGWHS YLSPQGRRYY VNTTTNETTW ERPSSSPGIS
     ASPGPHRSSL PTTVNGYHAS GTPAHPPETA HMSLRKSTGD SQNLGSSSPG RKQSKENTIT
     INCVTFPHPD TMPEQQLLKP TEWSYCDYFW ADKKDPQGNG TVAGFELLLQ KQLKGKQMQK
     EMSEFIRERI KIEEEYAKNL AKLSQNSLAA QEEGSLGEAW AQVKKSLADE AEVHLKFSAK
     LHSEVEKPLM NFRENFKKDM KKCDHHIADL RKQLGESRYA SVEKARKALT ERQKDLEMKT
     QQLEIKLSNK TEEDIKKARR KSTQAGDDLM RCVDLYNQAQ SKWFEEMVTT TLELERLEVE
     RVEMIRQHLC QYTQLRHETD MFNQSTVEPV DQLLRKVDPA KDRELWVREH KTGNIRPVDM
     EI
//
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