AFAP1_RAT
ID AFAP1_RAT Reviewed; 731 AA.
AC Q8VH46;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Actin filament-associated protein 1;
DE AltName: Full=110 kDa actin filament-associated protein;
DE Short=AFAP-110;
GN Name=Afap1; Synonyms=Afap;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, PHOSPHORYLATION,
RP INTERACTION WITH SRC, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Lung;
RX PubMed=12114187; DOI=10.1152/ajplung.00492.2001;
RA Lodyga M., Bai X.-H., Mourgeon E., Han B., Keshavjee S., Liu M.;
RT "Molecular cloning of actin filament-associated protein: a putative adaptor
RT in stretch-induced Src activation.";
RL Am. J. Physiol. 283:L265-L274(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Can cross-link actin filaments into both network and bundle
CC structures. May modulate changes in actin filament integrity and induce
CC lamellipodia formation. May function as an adapter molecule that links
CC other proteins, such as SRC and PKC to the actin cytoskeleton (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homomultimer. Interacts via its C-terminus with F-
CC actin; probably involving AFAP1 multimers (By similarity). Interacts
CC with activated SRC SH3-SH2 domains. Interacts via its PH 1 domain with
CC PRKCA, PRKCB and PRKCI (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:12114187}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain.
CC {ECO:0000269|PubMed:12114187}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:12114187}.
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DR EMBL; AY063759; AAL38984.1; -; mRNA.
DR RefSeq; NP_543176.1; NM_080900.1.
DR AlphaFoldDB; Q8VH46; -.
DR SMR; Q8VH46; -.
DR STRING; 10116.ENSRNOP00000010346; -.
DR iPTMnet; Q8VH46; -.
DR PhosphoSitePlus; Q8VH46; -.
DR jPOST; Q8VH46; -.
DR PaxDb; Q8VH46; -.
DR PRIDE; Q8VH46; -.
DR GeneID; 140935; -.
DR KEGG; rno:140935; -.
DR CTD; 60312; -.
DR RGD; 619959; Afap1.
DR eggNOG; ENOG502QQI1; Eukaryota.
DR InParanoid; Q8VH46; -.
DR OrthoDB; 256810at2759; -.
DR PhylomeDB; Q8VH46; -.
DR PRO; PR:Q8VH46; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005884; C:actin filament; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042169; F:SH2 domain binding; IPI:RGD.
DR GO; GO:0017124; F:SH3 domain binding; IPI:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:InterPro.
DR GO; GO:0009966; P:regulation of signal transduction; IDA:RGD.
DR GO; GO:0007165; P:signal transduction; NAS:RGD.
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 Acetylation; Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Repeat; SH3-binding.
FT CHAIN 1..731
FT /note="Actin filament-associated protein 1"
FT /id="PRO_0000317660"
FT DOMAIN 152..248
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 348..442
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 46..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..138
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 511..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..638
FT /note="Interaction with F-actin"
FT /evidence="ECO:0000250"
FT REGION 657..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 558..649
FT /evidence="ECO:0000255"
FT MOTIF 70..73
FT /note="SH3-binding"
FT /evidence="ECO:0000250"
FT MOTIF 93..96
FT /note="SH2-binding 1"
FT /evidence="ECO:0000250"
FT MOTIF 452..457
FT /note="SH2-binding 2"
FT /evidence="ECO:0000250"
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 COMPBIAS 659..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8N556"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N556"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N556"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N556"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N556"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N556"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 676
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80YS6"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N556"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N556"
SQ SEQUENCE 731 AA; 80752 MW; ACBBB88502908F83 CRC64;
MEELIVELRL FLELLDHEYL TSTVREKKAV LTNILLRMQS SKGFEVKDHA QKAETNNLPA
PPQMPLPEIP QPWLPPDSGP PPLPTSSLPE GYYEEAVPLS PGKAPEYITS NYDSEAMGSS
YESYDEEEED GKGKKTQHQC HHEEASMDLV KDAKICAFLL RKKRFGQWTK LLCVIKDTKL
LCYKSSKDQQ PQMELPLQGC SITYIPRDSK KKKHELKITQ QGTDPLVLAV QSKEQAEQWL
KVIKEAYSGC SGPVDPECSP PPSASVPVNK AELEKKLSSE RPSSDGEGVV ENGVTTCNGK
EQAKRKKPSK SEAKGTVSKV TGKKITKIIG LGKKKPSTDE QTSSAEEDVP TCGYLNVLSN
SRWRERWCRV KDSKLILHKD RADLKTHIVS IPLRGCEVIP GLDSKHPLTF RLLRNGQEVA
VLEASSSEDM GRWIGILLAE TGSSTDPGAL HYDYIDVEMS ANVIQTAKQT FCFMNRRAVS
TSPYLGSLSN GYAHPSGTAL HYDDVPCVNG SLKNKKPPAS SNGLPVKGRA PSSQQKKVES
AGGVKRTASN AEQYKYGKNR VEADAKRLQS KEEELLKRKE ALRNRLAQLR KERKDLRAAI
EVNAGRKTQV ALEDKLKRLE EECKQREAER VSLELELTEV KESLKKALAG GVTLGLAIEP
KSGTSSPQSP VFRHRTLENS PISSCDTSDA EGPLPVNSAA VLKKSQPSSS SSPCRGHVLQ
KAREWELKNG T
