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Database: UniProt
Entry: E9Q8X9_MOUSE
LinkDB: E9Q8X9_MOUSE
Original site: E9Q8X9_MOUSE 
ID   E9Q8X9_MOUSE            Unreviewed;       627 AA.
AC   E9Q8X9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Actin filament associated protein 1 {ECO:0000313|Ensembl:ENSMUSP00000119364.2};
DE   Flags: Fragment;
GN   Name=Afap1 {ECO:0000313|Ensembl:ENSMUSP00000119364.2,
GN   ECO:0000313|MGI:MGI:1917542};
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 {ECO:0000313|Ensembl:ENSMUSP00000119364.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0007829|PubMed:17242355}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000119364.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000119364.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [4] {ECO:0000313|Ensembl:ENSMUSP00000119364.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000119364.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; E9Q8X9; -.
DR   SMR; E9Q8X9; -.
DR   jPOST; E9Q8X9; -.
DR   MaxQB; E9Q8X9; -.
DR   PeptideAtlas; E9Q8X9; -.
DR   ProteomicsDB; 367392; -.
DR   Antibodypedia; 2882; 584 antibodies from 32 providers.
DR   Ensembl; ENSMUST00000141824.2; ENSMUSP00000119364.2; ENSMUSG00000029094.13.
DR   AGR; MGI:1917542; -.
DR   MGI; MGI:1917542; Afap1.
DR   VEuPathDB; HostDB:ENSMUSG00000029094; -.
DR   GeneTree; ENSGT00950000183067; -.
DR   HOGENOM; CLU_014418_1_0_1; -.
DR   OMA; DNMGLYD; -.
DR   ChiTaRS; Afap1; mouse.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000029094; Expressed in pineal body and 226 other cell types or tissues.
DR   ExpressionAtlas; E9Q8X9; baseline and differential.
DR   CDD; cd13306; PH1_AFAP; 1.
DR   CDD; cd13307; PH2_AFAP; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   InterPro; IPR030113; AFAP.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR14338:SF8; ACTIN FILAMENT-ASSOCIATED PROTEIN 1; 1.
DR   PANTHER; PTHR14338; ACTIN FILAMENT-ASSOCIATED PROTEIN 1 FAMILY MEMBER; 1.
DR   Pfam; PF00169; PH; 2.
DR   SMART; SM00233; PH; 2.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Proteomics identification {ECO:0007829|EPD:E9Q8X9,
KW   ECO:0007829|MaxQB:E9Q8X9};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          152..248
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          348..442
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          56..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          558..622
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        60..87
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         627
FT                   /evidence="ECO:0000313|Ensembl:ENSMUSP00000119364.2"
SQ   SEQUENCE   627 AA;  69666 MW;  F9B3E30CE4D4690D CRC64;
     MEELIVELRL FLELLDHEYL TSTVREKKAV LTNILLRLQS SKGFEVKDHA QKAEANNLPA
     PPQMPLPEIP QPWLPPDSGP PPLPTSSLPE GYYEEAVPLS PGKAPEYITS NYDSDAMSSS
     YESYDEEEED GKGKKTRHQW PSEEASMDLV KDAKICAFLL RKKRFGQWTK LLCVIKDTKL
     LCYKSSKDQQ PQMELPLQGC SITYIPRDSK KKKHELKITQ QGTDPLVLAV QSKEQAEQWL
     KVIKEAYSGC SGPVDPECSP PPSTSAPVNK AELEKKLSSE RPSSDGEGGV ENGVTTCNGK
     EQAKRKKPSK SEAKGTVSKV TGKKITKIIG LGKKKPSTDE QTSSAEEDVP TCGYLNVLSN
     SRWRERWCRV KDSKLILHKD RADLKTHLVS IPLRGCEVIP GLDSKHPLTF RLLRNGQEVA
     VLEASSSEDM GRWIGILLAE TGSSTDPGAL HYDYIDVEMS ANVIQTAKQT FCFMNRRAVS
     TSPYLGSLSN GYAHPSGTAL HYDDVPCVNG SLKNKKPPAS SNGVPVKGKA PSSQQKKVET
     AGGVKRTASN AEQYKYGKNR VEADAKRLQS KEEELLKRKE ALRNRLAQLR KERKDLRAAI
     EVNAGRKTQA ALEDKLKRLE EECKQRE
//
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