AF1L2_MOUSE
ID AF1L2_MOUSE Reviewed; 825 AA.
AC Q5DTU0; Q8BID1; Q8K2G0;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Actin filament-associated protein 1-like 2;
DE Short=AFAP1-like protein 2;
GN Name=Afap1l2; Synonyms=Kiaa1914;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 IDENTIFICATION BY 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 TYR-56 AND TYR-413, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113; SER-408 AND SER-484, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
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: 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5DTU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5DTU0-2; Sequence=VSP_014257;
CC -!- PTM: Tyrosine phosphorylated (by SRC). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31515.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC39879.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD90264.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK087449; BAC39879.1; ALT_FRAME; mRNA.
DR EMBL; AK220430; BAD90264.1; ALT_INIT; mRNA.
DR EMBL; BC031515; AAH31515.1; ALT_INIT; mRNA.
DR CCDS; CCDS50476.1; -. [Q5DTU0-1]
DR CCDS; CCDS50477.1; -. [Q5DTU0-2]
DR RefSeq; NP_001171267.1; NM_001177796.1. [Q5DTU0-2]
DR RefSeq; NP_001171268.1; NM_001177797.1. [Q5DTU0-1]
DR RefSeq; NP_666214.1; NM_146102.2.
DR AlphaFoldDB; Q5DTU0; -.
DR SMR; Q5DTU0; -.
DR BioGRID; 230491; 1.
DR STRING; 10090.ENSMUSP00000107210; -.
DR iPTMnet; Q5DTU0; -.
DR PhosphoSitePlus; Q5DTU0; -.
DR jPOST; Q5DTU0; -.
DR MaxQB; Q5DTU0; -.
DR PaxDb; Q5DTU0; -.
DR PeptideAtlas; Q5DTU0; -.
DR PRIDE; Q5DTU0; -.
DR ProteomicsDB; 285558; -. [Q5DTU0-1]
DR ProteomicsDB; 285559; -. [Q5DTU0-2]
DR Antibodypedia; 31934; 135 antibodies from 34 providers.
DR DNASU; 226250; -.
DR Ensembl; ENSMUST00000111584; ENSMUSP00000107210; ENSMUSG00000025083. [Q5DTU0-2]
DR Ensembl; ENSMUST00000118800; ENSMUSP00000113745; ENSMUSG00000025083. [Q5DTU0-1]
DR GeneID; 226250; -.
DR KEGG; mmu:226250; -.
DR UCSC; uc008hzm.2; mouse. [Q5DTU0-2]
DR UCSC; uc008hzn.2; mouse. [Q5DTU0-1]
DR CTD; 84632; -.
DR MGI; MGI:2147658; Afap1l2.
DR VEuPathDB; HostDB:ENSMUSG00000025083; -.
DR eggNOG; ENOG502QQA8; Eukaryota.
DR GeneTree; ENSGT00950000183067; -.
DR HOGENOM; CLU_014418_0_0_1; -.
DR InParanoid; Q5DTU0; -.
DR OrthoDB; 256810at2759; -.
DR PhylomeDB; Q5DTU0; -.
DR TreeFam; TF332622; -.
DR BioGRID-ORCS; 226250; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Afap1l2; mouse.
DR PRO; PR:Q5DTU0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q5DTU0; protein.
DR Bgee; ENSMUSG00000025083; Expressed in placenta labyrinth and 215 other tissues.
DR ExpressionAtlas; Q5DTU0; baseline and differential.
DR Genevisible; Q5DTU0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; ISO:MGI.
DR GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0035591; F:signaling adaptor activity; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0032675; P:regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..825
FT /note="Actin filament-associated protein 1-like 2"
FT /id="PRO_0000050806"
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 62..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 657..754
FT /evidence="ECO:0000255"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 413
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..6
FT /note="MERYKA -> MERYKAQGCCCLVVQRRILQVSAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_014257"
FT CONFLICT 124
FT /note="Y -> N (in Ref. 1; BAC39879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 825 AA; 92175 MW; E0D929590FED4764 CRC64;
MERYKALEQL LTELDDFLKV LDQENLSSAA VLKKSGLSEL LRLYTKSSSS DEEYIYMNKV
SVNGEQNSAS PDKVPEEQGP LTNGEPSQHS SAPQKSLPDL PPPKMIPERK QPTVPKIESP
EGYYEEAEPF DRSINEDGEA VSSSYESYDE DENSKGKAAP YQWPSPEASI ELMRDARICA
FLWRKKWLGQ WAKQLCVIRD TRLLCYKSSK DHSPQLDVNL RGSSVVHKEK QVRKKGHKLK
ITPMNADVIV LGLQSKDQAE QWLRVIQEVS GLPSEGASEG NQYTPDAQRL NCQKPDIAEK
YLSAAEYGIT INGHPEIPET KDVKKKCSAG LKLSNLMNLG RKKSTSLEPP ERSLETSSYL
NVLVNSQWKS RWCFVRDSHL HFYQDRNRSK VAQQPLSLVG CDVLPDPSPD HLYSFRILHN
GEELAKLEAK SSEEMGHWLG LLLSESGSKT DPEELTYDYV DAERVSCIVS AAKTSLLLMQ
RKFSEPNTYI DGLPSRDCQD DLYDDVEVSE LIAVVEPAEE AAPAVDANSG SEPDRVYLDL
TPVKSFLHSS SEAQAQASLP AVPHQDDVAE TLTVDPKPGT TPEEPHTESP GDPEVQQRQP
EVQESSEPIE PTPRITMVKL QAEQQRISFP ANCPDTMASA PIAASPPVKE KLRVTSAEIK
LGKNRTEAEV KRYTEEKERL ERSKEEIRGH LAQLRREKRE LKETLLRCTD KGVLAKLEQT
LKKIDEECRM EESRRVDLEL SIMEVKDNLK KAEAGPVTLG TTVDTTHLDN MSPRPQPKAA
TPNPPPDSTP VNSASVLKNR PLSVMVTGKG TVLQKAKEWE KKGAS
