ID A0A9L0RQI4_HORSE Unreviewed; 850 AA. AC A0A9L0RQI4; DT 13-SEP-2023, integrated into UniProtKB/TrEMBL. DT 13-SEP-2023, sequence version 1. DT 02-SEP-2026, entry version 14. DE RecName: Full=Actin filament-associated protein 1-like 2 {ECO:0000256|ARBA:ARBA00072612}; GN Name=AFAP1L2 {ECO:0000313|Ensembl:ENSECAP00000066139.1}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000066139.1, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000066139.1, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000066139.1, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O., RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T., RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T., RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S., RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G., RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R., RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000066139.1} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000066139.1}; RG Ensembl; RL Submitted (JAN-2026) to UniProtKB. 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. {ECO:0000256|ARBA:ARBA00059761}. CC -!- SUBUNIT: Interacts with SRC. Interacts with LCK when tyrosine CC phosphorylated. {ECO:0000256|ARBA:ARBA00061961}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; A0A9L0RQI4; -. DR Ensembl; ENSECAT00000130227.1; ENSECAP00000066139.1; ENSECAG00000014979.4. DR GeneTree; ENSGT00950000183067; -. DR Proteomes; UP000002281; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR CDD; cd13306; PH1_AFAP; 1. DR CDD; cd13307; PH2_AFAP; 1. DR FunFam; 2.30.29.30:FF:000020; Actin filament-associated protein 1-like 2 isoform 1; 1. DR FunFam; 2.30.29.30:FF:000171; Actin filament-associated protein 1-like 2 isoform 1; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2. DR InterPro; IPR030113; AFAP. DR InterPro; IPR063177; AFAP_C. DR InterPro; IPR063153; AFAP_N. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR PANTHER; PTHR14338; ACTIN FILAMENT-ASSOCIATED PROTEIN 1 FAMILY MEMBER; 1. DR PANTHER; PTHR14338:SF4; ACTIN FILAMENT-ASSOCIATED PROTEIN 1-LIKE 2; 1. DR Pfam; PF30810; AFAP_C; 1. DR Pfam; PF30812; AFAP_N; 1. DR Pfam; PF00169; PH; 2. DR SMART; SM00233; PH; 2. DR SUPFAM; SSF50729; PH domain-like; 2. DR PROSITE; PS50003; PH_DOMAIN; 2. PE 4: Predicted; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}. FT DOMAIN 186..282 FT /note="PH" FT /evidence="ECO:0000259|PROSITE:PS50003" FT DOMAIN 364..458 FT /note="PH" FT /evidence="ECO:0000259|PROSITE:PS50003" FT REGION 76..174 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 522..546 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 559..618 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 664..691 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 794..819 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 90..105 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 134..150 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 524..537 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 681..691 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 800..815 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 850 AA; 94944 MW; B76997B3D5CE68E8 CRC64; MRSTMWVLLA NTATSNALEQ LLTELDDFLK ILDQENLSST AEVKKSGLAE LLRLYTKSSS SDEEYIYMNK VTVHKQQNAE SQDKVPEEQS PLTNGEPSQH TSAPQKSLPD LPPPKIIPER KQLSIPRIES PEGYYEEAEP YDTSLNEDGE AVSSSYESYD EEESNKGKSA PYQWPSPEAS IELMRDARIC AFLWRKKWLG QWAKQLCVIK DTRLLCYKSS KDHSPQLDVN LLGSSVVHKE KQVRKKEHKL KITPMNADVI VLGLQSKDQA EQWLRVIQEV SGLPSEGVSE GNQYTPDAQR PNCQKPDITE KFLSASEYGS SIEGHPEVPE TKDVKKKCSA GLKLSNLMNL GRKKSTSLEP PERSLETSSY LNVLVNSQWK SRWCSVRDSH LHFYQDRNRS KVAQQPLSLV GCEVVPDPSP DHLYSFRILH NGEELAKLEA KSSEEMGHWL GLLLSESGSK TDPEEFTYDY VDADRVSCIV SAAKNSLLLM QRKFSEPNTY IDGLPSQDRQ EMLYDDVEMS ELSATVEPTE EATPATDALD ESGPDRVYLD LTPVKSFLHS SGSAQAQAPS PPLSHLDPLA EALPADPGPS PTPDEALEMS PETPELQMQQ ENLESEEPSL RTTMVKIQTE QQKISFPSSC PDAVALTPAG ASPPVKDRLR VTTADEQTEV QRGEGTCPRS HSKEEIKLGK NRTEAEVKRY TEEKERLERK KEEIRGHLAQ LRKEKRELKE TLSKCTDKGV LASLEQKLKE MEEECRIEES RRVDLELNIV EVKDNLKKAE AGPVTLGTTV DTTHLESVSP RPKAATPTPA PDCTPVNSAT ALKNRPLSVM VTGKGTVLQK AKEWEKKGAS //