AFAP1_CHICK
ID AFAP1_CHICK Reviewed; 729 AA.
AC Q90738; Q90917;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Actin filament-associated protein 1;
DE AltName: Full=110 kDa actin filament-associated protein;
DE Short=AFAP-110;
DE AltName: Full=Neural actin filament protein;
DE AltName: Full=pp110;
GN Name=AFAP1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, AND INTERACTION WITH SRC AND FYN.
RX PubMed=8247004; DOI=10.1128/mcb.13.12.7892-7900.1993;
RA Flynn D.C., Leu T.H., Reynolds A.B., Parsons J.T.;
RT "Identification and sequence analysis of cDNAs encoding a 110-kilodalton
RT actin filament-associated pp60src substrate.";
RL Mol. Cell. Biol. 13:7892-7900(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=7876134; DOI=10.1074/jbc.270.28.16911;
RA Flynn D.C., Koay T.C., Humphries C.G., Guappone A.C.;
RT "AFAP-120. A variant form of the Src SH2/SH3-binding partner AFAP-110 is
RT detected in brain and contains a novel internal sequence which binds to a
RT 67-kDa protein.";
RL J. Biol. Chem. 270:3894-3899(1995).
RN [3]
RP SUBCELLULAR LOCATION, INTERACTION WITH SRC, AND PHOSPHORYLATION.
RX PubMed=2476666; DOI=10.1128/mcb.9.9.3951-3958.1989;
RA Reynolds A.B., Kanner S.B., Wang H.C., Parsons J.T.;
RT "Stable association of activated pp60src with two tyrosine-phosphorylated
RT cellular proteins.";
RL Mol. Cell. Biol. 9:3951-3958(1989).
RN [4]
RP SH3-BINDING MOTIF, INTERACTION WITH SRC, AND MUTAGENESIS OF PRO-71.
RX PubMed=9350057; DOI=10.1023/a:1006840104666;
RA Guappone A.C., Flynn D.C.;
RT "The integrity of the SH3 binding motif of AFAP-110 is required to
RT facilitate tyrosine phosphorylation by, and stable complex formation with,
RT Src.";
RL Mol. Cell. Biochem. 175:243-252(1997).
RN [5]
RP SH2-BINDING MOTIF, INTERACTION WITH SRC, PHOSPHORYLATION BY SRC, AND
RP MUTAGENESIS OF TYR-93; TYR-94; TYR-451 AND TYR-453.
RX PubMed=9655255;
RX DOI=10.1002/(sici)1098-2744(199806)22:2<110::aid-mc6>3.0.co;2-q;
RA Guappone A.C., Weimer T., Flynn D.C.;
RT "Formation of a stable src-AFAP-110 complex through either an amino-
RT terminal or a carboxy-terminal SH2-binding motif.";
RL Mol. Carcinog. 22:110-119(1998).
RN [6]
RP SELF-ASSOCIATION, AND SUBCELLULAR LOCATION.
RX PubMed=9619827; DOI=10.1038/sj.onc.1201753;
RA Qian Y., Baisden J.M., Westin E.H., Guappone A.C., Koay T.C., Flynn D.C.;
RT "Src can regulate carboxy terminal interactions with AFAP-110, which
RT influence self-association, cell localization and actin filament
RT integrity.";
RL Oncogene 16:2185-2195(1998).
RN [7]
RP INTERACTION WITH F-ACTIN.
RX PubMed=10666339; DOI=10.1006/excr.1999.4795;
RA Qian Y., Baisden J.M., Zot H.G., Van Winkle W.B., Flynn D.C.;
RT "The carboxy terminus of AFAP-110 modulates direct interactions with actin
RT filaments and regulates its ability to alter actin filament integrity and
RT induce lamellipodia formation.";
RL Exp. Cell Res. 255:102-113(2000).
RN [8]
RP INTERACTION WITH F-ACTIN, AND INTERACTION WITH PRKCA; PRKCB; PRKCG AND
RP PRKCI.
RX PubMed=12134071; DOI=10.1091/mbc.e01-12-0148;
RA Qian Y., Baisden J.M., Cherezova L., Summy J.M., Guappone-Koay A., Shi X.,
RA Mast T., Pustula J., Zot H.G., Mazloum N., Lee M.Y., Flynn D.C.;
RT "PKC phosphorylation increases the ability of AFAP-110 to cross-link actin
RT filaments.";
RL Mol. Biol. Cell 13:2311-2322(2002).
CC -!- FUNCTION: Functions as an adapter molecule that links other proteins to
CC the actin cytoskeleton. May function in facilitating interactions
CC between SRC and actin filaments. May modulate changes in actin filament
CC integrity and induce lamellipodia formation. Can cross-link actin
CC filaments into both network and bundle structures.
CC -!- SUBUNIT: Monomer and homomultimer. Interacts via its C-terminus with F-
CC actin; probably involving AFAP1 multimers. Interacts with activated SRC
CC SH3-SH2 domains. May interact with FYN SH3-SH2 domains. Interacts via
CC its PH 1 domain with PRKCA, PRKCB, PRKCI. {ECO:0000269|PubMed:10666339,
CC ECO:0000269|PubMed:12134071, ECO:0000269|PubMed:2476666,
CC ECO:0000269|PubMed:8247004, ECO:0000269|PubMed:9350057,
CC ECO:0000269|PubMed:9655255}.
CC -!- INTERACTION:
CC Q90738; P00523: SRC; NbExp=3; IntAct=EBI-8562073, EBI-848039;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:2476666, ECO:0000269|PubMed:8247004,
CC ECO:0000269|PubMed:9619827}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AFAP-110;
CC IsoId=Q90738-1; Sequence=Displayed;
CC Name=2; Synonyms=AFAP-120;
CC IsoId=Q90738-2; Sequence=VSP_031121;
CC -!- TISSUE SPECIFICITY: Isoform 2 is specifically expressed in brain.
CC {ECO:0000269|PubMed:7876134}.
CC -!- PTM: Phosphorylated on tyrosine residues by SRC.
CC {ECO:0000269|PubMed:2476666, ECO:0000269|PubMed:8247004,
CC ECO:0000269|PubMed:9655255}.
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DR EMBL; L20303; AAA18166.2; -; mRNA.
DR EMBL; L20302; AAA67326.2; -; mRNA.
DR PIR; A54592; A54592.
DR PIR; A55883; A55883.
DR RefSeq; NP_001128120.1; NM_001134648.1. [Q90738-1]
DR RefSeq; NP_989536.1; NM_204205.1. [Q90738-2]
DR AlphaFoldDB; Q90738; -.
DR SMR; Q90738; -.
DR IntAct; Q90738; 1.
DR MINT; Q90738; -.
DR PaxDb; Q90738; -.
DR GeneID; 374034; -.
DR KEGG; gga:374034; -.
DR CTD; 60312; -.
DR VEuPathDB; HostDB:geneid_374034; -.
DR eggNOG; ENOG502QQI1; Eukaryota.
DR InParanoid; Q90738; -.
DR OrthoDB; 256810at2759; -.
DR PhylomeDB; Q90738; -.
DR PRO; PR:Q90738; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042169; F:SH2 domain binding; IDA:AgBase.
DR GO; GO:0017124; F:SH3 domain binding; IDA:AgBase.
DR GO; GO:0018109; P:peptidyl-arginine phosphorylation; IMP:AgBase.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IGI:AgBase.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:InterPro.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR030113; AFAP.
DR InterPro; IPR029907; AFAP-110.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR14338; PTHR14338; 2.
DR PANTHER; PTHR14338:SF8; PTHR14338:SF8; 2.
DR Pfam; PF00169; PH; 2.
DR SMART; SM00233; PH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Repeat; SH3-binding.
FT CHAIN 1..729
FT /note="Actin filament-associated protein 1"
FT /id="PRO_0000317661"
FT DOMAIN 153..249
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 347..441
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 56..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..637
FT /note="Interaction with F-actin"
FT REGION 701..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 557..648
FT /evidence="ECO:0000255"
FT MOTIF 71..74
FT /note="SH3-binding"
FT MOTIF 94..97
FT /note="SH2-binding 1"
FT MOTIF 451..456
FT /note="SH2-binding 2"
FT COMPBIAS 59..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 510
FT /note="S -> SWEPEDGFPSSRSRNMGEEMLYDNAGLYDNLPSPKIFARYPPADRKT
FT NRLSTDKLSSNHYKHPVSSNLSSAQSVTNTSAVGRGSVSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7876134"
FT /id="VSP_031121"
FT MUTAGEN 71
FT /note="P->A: Abolishes interaction with SRC SH3 domain and
FT decreases tyrosine phosphorylation."
FT /evidence="ECO:0000269|PubMed:9350057"
FT MUTAGEN 93
FT /note="Y->A: Reduces phosphorylation and abolishes
FT interaction with activated SRC; when associated with A-94;
FT A-451 and A-453."
FT /evidence="ECO:0000269|PubMed:9655255"
FT MUTAGEN 94
FT /note="Y->A: Reduces phosphorylation and abolishes
FT interaction with activated SRC; when associated with A-93;
FT A-451 and A-453."
FT /evidence="ECO:0000269|PubMed:9655255"
FT MUTAGEN 451
FT /note="Y->A: Reduces phosphorylation and abolishes
FT interaction with activated SRC; when associated with A-93;
FT A-94 and A-451."
FT /evidence="ECO:0000269|PubMed:9655255"
FT MUTAGEN 453
FT /note="Y->A: Reduces phosphorylation and abolishes
FT interaction with activated SRC; when associated with A-93;
FT A-94 and A-451."
FT /evidence="ECO:0000269|PubMed:9655255"
SQ SEQUENCE 729 AA; 81160 MW; 4735A746E665890B CRC64;
MEELIVELRL FLELLDHEYL TSTVREKKAV ITNILLRIQS SKGFEIKEHV QKPEVANSLP
APPQMPLPEI PQQWLPPDNG PPPLPTSSLP EGYYEEAVPV SPGKAPEYIT SNYDSDAMSS
SYESYDEEEE DGKGKKMRHQ WPSEEASMDL VKDAKICAFL LRKKRFGQWT KLLCVIKENK
LLCYKSSKDQ QPQMELLLND CSITYIPKDS KKKKHELKIS HQGADALVLA VQSKEQAEQW
LKVIKDVCSN CTGTVDSDGP LSSSPVHKTE LEKKLSSERP SSDGEGAVEN GITTVCNGKE
QVKRKKSSKT EAKGTVTKVT GKKITKIIGL GKKKPSTDEQ TSSAEEDVPT CGYLNVLSNN
RWRERWCRVK DNKLIFHKDR TDLKTHIVSI PLRGCEVIPG LDSKHPLTFR LLRNGQEVAV
LEASSSEDMG RWIGMLLAET GSSTDPGALH YDYIDVEMTA SVIQAAKQTF CFMNRRVIST
NPYRGSTANG YACPSGMALH YDDVPCINGS FKGKKPPATA NGITGKVRTL NSQPKKPESV
SCVKRTASNA EQYKYGKNRV EAVAKRLQSK EEELLKRKEA LRNRLAQLRK ERKDLRAAIE
VNAGRKTQVI LEDKLKKLEE ECKTKEAERV NLELELTEVK ESLKKALAGG ITLGLAIEPK
SGTSSPQSPI FKHRTLENSP ISSCDTSDTE CSIPVNSAAA LKRPPSSNNS PCRGHVLRKA
KEWEMKNGT
