ID A0A5F5XH19_FELCA Unreviewed; 476 AA.
AC A0A5F5XH19;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
DE RecName: Full=Growth arrest-specific protein 7 {ECO:0000256|ARBA:ARBA00071534};
GN Name=GAS7 {ECO:0000313|Ensembl:ENSFCAP00000053423.1,
GN ECO:0000313|VGNC:VGNC:62470};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000053423.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000053423.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000053423.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000053423.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000053423.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000053423.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000053423.1};
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: May play a role in promoting maturation and morphological
CC differentiation of cerebellar neurons. {ECO:0000256|ARBA:ARBA00055699}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; AANG04000740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_023099621.1; XM_023243853.2.
DR AlphaFoldDB; A0A5F5XH19; -.
DR STRING; 9685.ENSFCAP00000053423; -.
DR PaxDb; 9685-ENSFCAP00000001709; -.
DR Ensembl; ENSFCAT00000083080.1; ENSFCAP00000053423.1; ENSFCAG00000001845.6.
DR GeneID; 101084661; -.
DR VGNC; VGNC:62470; GAS7.
DR GeneTree; ENSGT00940000156268; -.
DR InParanoid; A0A5F5XH19; -.
DR OMA; HGENSHN; -.
DR OrthoDB; 28357at2759; -.
DR Proteomes; UP000011712; Chromosome E1.
DR Bgee; ENSFCAG00000001845; Expressed in prefrontal cortex and 10 other cell types or tissues.
DR GO; GO:0005905; C:clathrin-coated pit; IBA:GO_Central.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR CDD; cd07649; F-BAR_GAS7; 1.
DR CDD; cd11829; SH3_GAS7; 1.
DR FunFam; 2.20.70.10:FF:000033; Growth arrest specific 7; 1.
DR FunFam; 2.30.30.40:FF:000216; growth arrest-specific protein 7 isoform X1; 1.
DR FunFam; 1.20.1270.60:FF:000024; growth arrest-specific protein 7 isoform X2; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
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; PF14604; SH3_9; 1.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF16623; WW_FCH_linker; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..62
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 77..110
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 196..456
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT REGION 100..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 308..367
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 108..120
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 54454 MW; 1A9445AE130F9728 CRC64;
MSGARCRTLY PFSGERHGQG LRFAAGEFIR LLQVPDGGWW EGEKEDGLRG WFPASYVQLL
EKPGMVPPPP GEESQIILLP PGWQSYLSPQ GRRYYVNTTT NETTWERPSS SSGIPASPGP
HRSSLPPTVN GYHAAGTPAH PPETAHMSVR KSTGDSQNLG SSSPGKKQNK ENTITINCVT
FPHPDTMPEQ QLLKPTEWSY CDYFWADKKD PQGNGTMAGF ELLLQKQLKG KQMQKEMSEF
IRERIKIEEE YAKNLAKLSQ NSLAAQEEGS LGEAWAQVKK SLADEAEVHL KFSAKLHSEV
EKPLMNFREN FKKDMKKCEH HITDLRKQLA SRHAAVEKAR KALTERQRDL EIKTQQLEIK
LSNKTEEDIK KARRKSTQAG DDLMRCVDLY NQAQSKWFEE MVTTTLELER LEAERVEMIR
QHLCQYTQLR HETDMFNQST VEPVDQLLRK VDPAKDRELW VREHKTGNIR PVDMEI
//
