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.
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 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
//