ID   AF1L1_BOVIN             Reviewed;         763 AA.
AC   A6QQV9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Actin filament-associated protein 1-like 1;
DE            Short=AFAP1-like protein 1;
GN   Name=AFAP1L1;
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=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in podosome and invadosome formation.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CTTN. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TED9}. Cell
CC       projection, podosome {ECO:0000250|UniProtKB:Q8TED9}. Cell projection,
CC       invadopodium {ECO:0000250|UniProtKB:Q8TED9}. Cytoplasm, cytoskeleton,
CC       stress fiber {ECO:0000250|UniProtKB:Q8TED9}.
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DR   EMBL; BC150012; AAI50013.1; -; mRNA.
DR   RefSeq; NP_001093804.1; NM_001100334.2.
DR   AlphaFoldDB; A6QQV9; -.
DR   STRING; 9913.ENSBTAP00000013389; -.
DR   PaxDb; A6QQV9; -.
DR   PRIDE; A6QQV9; -.
DR   Ensembl; ENSBTAT00000087224; ENSBTAP00000061779; ENSBTAG00000019948.
DR   GeneID; 510738; -.
DR   KEGG; bta:510738; -.
DR   CTD; 134265; -.
DR   VEuPathDB; HostDB:ENSBTAG00000019948; -.
DR   VGNC; VGNC:25707; AFAP1L1.
DR   eggNOG; ENOG502R3HG; Eukaryota.
DR   GeneTree; ENSGT00950000183067; -.
DR   HOGENOM; CLU_014418_1_0_1; -.
DR   InParanoid; A6QQV9; -.
DR   OrthoDB; 256810at2759; -.
DR   TreeFam; TF332622; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000019948; Expressed in bone marrow and 99 other tissues.
DR   ExpressionAtlas; A6QQV9; baseline.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR030113; AFAP.
DR   InterPro; IPR030112; AFAP1L1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR14338; PTHR14338; 1.
DR   PANTHER; PTHR14338:SF1; PTHR14338:SF1; 1.
DR   Pfam; PF00169; PH; 2.
DR   SMART; SM00233; PH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..763
FT                   /note="Actin filament-associated protein 1-like 1"
FT                   /id="PRO_0000317657"
FT   DOMAIN          220..316
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          413..507
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          83..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          606..694
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        111..125
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..595
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:D4AB98"
FT   MOD_RES         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:D4AB98"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BZI0"
FT   MOD_RES         329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BZI0"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BZI0"
FT   MOD_RES         552
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BZI0"
FT   MOD_RES         742
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BZI0"
SQ   SEQUENCE   763 AA;  85931 MW;  36E2AF7EE8652637 CRC64;
     MDRGRVLEQL LPELTGLLSL LDHEYLSDTT LEKKMAVASI LQSLQPLPAK EVSYLYVNTA
     DLHSGPSFVE SLFEEFDCDL SGLQDMPEDE AESCKAASPE PAKSPSLRHT ADLPPPLPNR
     PPPEDYYEEA LPLGPGKSPE YISSHNGCSP AHSLMDGYYE DADSSYPATR MNGELKNSYN
     DSDAMSSSYE SYDEEEEEGK GPQPTHQWPS EEASMHLVRD CRICAFLLRK KRFGQWAKQL
     TVIKEDQLLC YKSSKDRQPH LRLALDVCSV IYVPKDSRHK RHELRFAQGA TEVLVLALQS
     REQAEEWLKV IREVSKPVGG TEGADVPRSP VLLCKADLDK RLSQEKQTSD SDSLGMGDSC
     STLGREHGKG KKSSLSELKG SMSRAAGRKI TRIISFSKKK ALADDLQASS TEEVPCCGYL
     NVLVNHGWKE RWCRLKCNTL YFHKDRTDLR THVNAIALRG CEVAPGFGPR HPFAFRILHN
     RQEVAILEAS CSEDMGRWLG LLLVEMGSKV TPEALHYDYV DVETLTSIVS AGRNSFLYAR
     SCQDQWPEPR VYDDVPYEKM QDEEPERPPG AQVKRHASTC SEKSHRVDPQ VKVKRHASSA
     HQYKYGKNRA EEDARRYLVE KEKLEKEKET IRTELMALRQ EKRELKEAIR NNPGAKLKAL
     EEALATLEAQ CRAKEEHRID LELRLVTVKE RLQQSLAGGP ALGLSVNSKI KSGETANKPQ
     NNVPEQPLPV NCVSELRKRS PSIINSNQGR VLQKAKEWEM KKT