ID   AF1L2_BOVIN             Reviewed;         817 AA.
AC   Q17R10;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Actin filament-associated protein 1-like 2;
DE            Short=AFAP1-like protein 2;
GN   Name=AFAP1L2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in a signaling cascade by enhancing the
CC       kinase activity of SRC. Contributes to SRC-regulated transcription
CC       activation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with SRC. Interacts with LCK when tyrosine
CC       phosphorylated (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Tyrosine phosphorylated (by SRC). {ECO:0000250}.
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DR   EMBL; BC118084; AAI18085.1; -; mRNA.
DR   RefSeq; NP_001069843.1; NM_001076375.1.
DR   AlphaFoldDB; Q17R10; -.
DR   SMR; Q17R10; -.
DR   STRING; 9913.ENSBTAP00000006439; -.
DR   iPTMnet; Q17R10; -.
DR   PaxDb; Q17R10; -.
DR   PRIDE; Q17R10; -.
DR   GeneID; 615436; -.
DR   KEGG; bta:615436; -.
DR   CTD; 84632; -.
DR   eggNOG; ENOG502QQA8; Eukaryota.
DR   HOGENOM; CLU_014418_0_0_1; -.
DR   InParanoid; Q17R10; -.
DR   OrthoDB; 256810at2759; -.
DR   TreeFam; TF332622; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0042169; F:SH2 domain binding; IBA:GO_Central.
DR   GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR   GO; GO:0035591; F:signaling adaptor activity; IEA:InterPro.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0032675; P:regulation of interleukin-6 production; IBA:GO_Central.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR030113; AFAP.
DR   InterPro; IPR030115; AFAP1L2.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR14338; PTHR14338; 1.
DR   PANTHER; PTHR14338:SF4; PTHR14338:SF4; 1.
DR   Pfam; PF00169; PH; 2.
DR   SMART; SM00233; PH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..817
FT                   /note="Actin filament-associated protein 1-like 2"
FT                   /id="PRO_0000361276"
FT   DOMAIN          175..271
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          353..447
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          63..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          652..748
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        63..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..105
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..578
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         56
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DTU0"
FT   MOD_RES         408
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DTU0"
FT   MOD_RES         413
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DTU0"
FT   MOD_RES         484
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5DTU0"
SQ   SEQUENCE   817 AA;  90789 MW;  6FB5201822AAAABC CRC64;
     MERFKALEQL LTELDDFLRI LDQENLSSTA VVKKSGLAEL LRLYTKSSSS DEEYIYMNKV
     TVHKQQNAES QDKAPEQQNP LTNGEPPQPS SAPQKSLPDL PPPKMIPERK QLSVPKIESP
     EGYYEEAEPY DTSLNEDGEA VSSSYESYDE EESSKGKSAP HQWPSPEASI ELMRDARICA
     FLWRKKWLGQ WAKQLCVIKD TRLLCYKSSK DHSPQLDVSL LGSSVVHKEK QVRKKEHKLK
     ITPLNADVIV LGLQSRDQAE QWLRVIQEVS GLPSEGACEG SQFTPDAQRL SCPKPDITEK
     YLSASECGSP IDGHPEVPET KDVKKKCSAG LKLSNLMNLG RKKSTSLEPP DRSLETSSYL
     NVLVNSQWKS RWCSVRDSHL YFYQDRNRSK AAQQPLSLLG CEVVPDPSPD HLYSFRILHN
     GEELAKLEAK SSEEMGHWLG LLLSESGSKT DPEEFTYDYV DADRVSCIVS AAKTSLLLMQ
     RKFSEPNTYI DGLPSQDRQE LLYDDVEVSE LTTAGEAPEE ATPATDAPGE PDPDRVYLDL
     TPIKSFLHGD SGARAPSPTP PHQDPPAETL PLPEDSDPAP DEPLIKSPEN PELQMQQESQ
     EPEEPSLGGT EVKLQAGQQK TSPSPSCPDT VAVTPAGSSP PVKDRLKAAS PEIKLGKNRT
     EAEVKRYTEE KERLEKKKEE IRGHLAQLRR EKRELKETLL KCTDKGAAAS LEQKLREVDE
     ECRVEERRRV DLELSIVEVK DSLRKAEAGP VTLGTTVDTT HLESVSPRPK AATPTPAPDC
     TPVNSATALK NRPLSVMVTG KGTVLQKAKE WEKKGAS