AFAP1_MOUSE
ID AFAP1_MOUSE Reviewed; 731 AA.
AC Q80YS6; Q3UGX1; Q6ZPE4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=Kiaa3018;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Melanocyte, Placenta, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-284; SER-666;
RP SER-669; THR-676 AND SER-680, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
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).
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. Interacts with activated SRC
CC SH3-SH2 domains. Interacts via its PH 1 domain with PRKCA, PRKCB and
CC PRKCI (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q8N556}.
CC -!- PTM: Phosphorylated on tyrosine residues by SRC. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98293.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129483; BAC98293.1; ALT_INIT; mRNA.
DR EMBL; AK147706; BAE28086.1; -; mRNA.
DR EMBL; AK148000; BAE28280.1; -; mRNA.
DR EMBL; AK161385; BAE36364.1; -; mRNA.
DR EMBL; BC050814; AAH50814.1; -; mRNA.
DR CCDS; CCDS19236.1; -.
DR RefSeq; NP_081649.1; NM_027373.2.
DR AlphaFoldDB; Q80YS6; -.
DR SMR; Q80YS6; -.
DR BioGRID; 213967; 2.
DR IntAct; Q80YS6; 1.
DR MINT; Q80YS6; -.
DR STRING; 10090.ENSMUSP00000067779; -.
DR iPTMnet; Q80YS6; -.
DR PhosphoSitePlus; Q80YS6; -.
DR EPD; Q80YS6; -.
DR jPOST; Q80YS6; -.
DR MaxQB; Q80YS6; -.
DR PaxDb; Q80YS6; -.
DR PeptideAtlas; Q80YS6; -.
DR PRIDE; Q80YS6; -.
DR ProteomicsDB; 285767; -.
DR Antibodypedia; 2882; 515 antibodies from 32 providers.
DR DNASU; 70292; -.
DR Ensembl; ENSMUST00000064571; ENSMUSP00000067779; ENSMUSG00000029094.
DR GeneID; 70292; -.
DR KEGG; mmu:70292; -.
DR UCSC; uc008xej.1; mouse.
DR CTD; 60312; -.
DR MGI; MGI:1917542; Afap1.
DR VEuPathDB; HostDB:ENSMUSG00000029094; -.
DR eggNOG; ENOG502QQI1; Eukaryota.
DR GeneTree; ENSGT00950000183067; -.
DR HOGENOM; CLU_014418_2_0_1; -.
DR InParanoid; Q80YS6; -.
DR OMA; NHYKYPV; -.
DR PhylomeDB; Q80YS6; -.
DR TreeFam; TF332622; -.
DR BioGRID-ORCS; 70292; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Afap1; mouse.
DR PRO; PR:Q80YS6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80YS6; protein.
DR Bgee; ENSMUSG00000029094; Expressed in pineal body and 223 other tissues.
DR ExpressionAtlas; Q80YS6; baseline and differential.
DR Genevisible; Q80YS6; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:InterPro.
DR GO; GO:0009966; P:regulation of signal transduction; ISO:MGI.
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_0000317659"
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 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 REGION 595..638
FT /note="Interaction with F-actin"
FT /evidence="ECO:0000250"
FT REGION 658..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..715
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:0007744|PubMed:21183079"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0007744|PubMed:21183079"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 676
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N556"
FT CONFLICT 43
FT /note="G -> R (in Ref. 2; BAE28086)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="K -> R (in Ref. 2; BAE28086)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="S -> G (in Ref. 1; BAC98293)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="G -> D (in Ref. 1; BAC98293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 731 AA; 80615 MW; 58D3D31BED5C2FCD 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 EECKQREAER VSLELELTEV KESLKKALAG GVTLGLAIEP
RSGTSSPQSP VFRHRTLENS PISSCDTSDA EGPLPVNSAA VLKKSQPSSG SSPCRGHVLQ
KAKEWELKNG T
