ID DBNL_HUMAN Reviewed; 430 AA. AC Q9UJU6; P84070; Q6IAI8; Q96F30; Q96K74; Q9HBN8; Q9NR72; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 20-MAR-2007, entry version 51. DE Drebrin-like protein (SH3 domain-containing protein 7) (Drebrin-F) DE (Cervical SH3P7) (HPK1-interacting protein of 55 kDa) (HIP-55) DE (Cervical mucin-associated protein). GN Name=DBNL; Synonyms=CMAP, SH3P7; ORFNames=PP5423; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH MAP4K1. RX MEDLINE=20036526; PubMed=10567356; DOI=10.1074/jbc.274.48.33945; RA Ensenat D., Yao Z., Wang X.-S., Kori R., Zhou G., Lee S.C., Tan T.-H.; RT "A novel src homology 3 domain-containing adaptor protein, HIP-55, RT that interacts with hematopoietic progenitor kinase 1."; RL J. Biol. Chem. 274:33945-33950(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Zhang W., Yuan Z., Wan T., He L., Cao X.; RT "Molecular cloning of cDNA encoding drebrin F."; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Cervix; RA Toribara N.W., Ho S.B., Wang R., Arthur M., Shekels L.L., RA Spurr-Michaud S., Keutmann H.T., Hill J.A., Gipson I.K.; RT "Expression cloning of a novel cervical mucin-associated protein RT (CMAP)."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., RA Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Mammary gland; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Eye; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP IDENTIFICATION. RX PubMed=9891087; RA Larbolette O., Wollscheid B., Schweikert J., Nielsen P.J., RA Wienands J.; RT "SH3P7 is a cytoskeleton adapter protein and is coupled to signal RT transduction from lymphocyte antigen receptors."; RL Mol. Cell. Biol. 19:1539-1546(1999). RN [9] RP DEGRADATION BY CASPASES. RX PubMed=11689006; DOI=10.1006/bbrc.2001.5862; RA Chen Y.-R., Kori R., John B., Tan T.-H.; RT "Caspase-mediated cleavage of actin-binding and SH3-domain-containing RT proteins cortactin, HS1, and HIP-55 during apoptosis."; RL Biochem. Biophys. Res. Commun. 288:981-989(2001). RN [10] RP FUNCTION. RX PubMed=14729663; DOI=10.1074/jbc.M312659200; RA Le Bras S., Foucault I., Foussat A., Brignone C., Acuto O., RA Deckert M.; RT "Recruitment of the actin-binding protein HIP-55 to the immunological RT synapse regulates T cell receptor signaling and endocytosis."; RL J. Biol. Chem. 279:15550-15560(2004). RN [11] RP INTERACTION WITH PRAM1, CLEAVAGE BY CASPASES, AND MUTAGENESIS OF RP ASP-361. RX PubMed=15637062; DOI=10.1074/jbc.M413564200; RA Denis F.M., Benecke A., Di Gioia Y., Touw I.P., Cayre Y.E., Lutz P.G.; RT "PRAM-1 potentiates arsenic trioxide-induced JNK activation."; RL J. Biol. Chem. 280:9043-9048(2005). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, AND MASS RP SPECTROMETRY. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, AND MASS RP SPECTROMETRY. RX PubMed=16094384; DOI=10.1038/nmeth776; RA Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., RA Bodenmiller B., Watts J.D., Hood L., Aebersold R.; RT "Quantitative phosphoproteome analysis using a dendrimer conjugation RT chemistry and tandem mass spectrometry."; RL Nat. Methods 2:591-598(2005). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASS RP SPECTROMETRY. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS RP SPECTROMETRY. RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [16] RP STRUCTURE BY NMR OF 1-133. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the cofilin homology domain of HIP-55 (drebrin- RT like protein)."; RL Submitted (NOV-2005) to the PDB data bank. CC -!- FUNCTION: Actin-binding adapter protein. May act as a common CC effector of antigen receptor-signaling pathways in leukocytes. Its CC association with dynamin suggests that it may also connect the CC actin cytoskeleton to endocytic function. Acts as a key component CC of the immunological synapse that regulates T-cell activation by CC bridging TCRs and the actin cytoskeleton to gene activation and CC endocytic processes. Binds to F-actin but is not involved in actin CC polymerization, capping or bundling. Does not bind G-actin. CC -!- SUBUNIT: Interacts with SHANK2 and SHANK3 (By similarity). CC Interacts with FGD1, dynamin, MAP4K1 and PRAM1. CC -!- SUBCELLULAR LOCATION: Cytoplasm; cytoskeleton. Note=Cortical CC cytoskeleton. Associates with lamellipodial actin. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9UJU6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UJU6-2; Sequence=VSP_011398; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q9UJU6-3; Sequence=VSP_011398, VSP_011399; CC Note=No experimental confirmation available; CC -!- DOMAIN: The SH3 domain mediates interaction with SHANK2, SHANK3 CC and PRAM1. CC -!- MISCELLANEOUS: Degraded by caspases during apoptosis. CC -!- SIMILARITY: Contains 1 ADF-H domain. CC -!- SIMILARITY: Contains 1 SH3 domain. 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 EMBL; AF197060; AAF13701.1; -; mRNA. DR EMBL; AF077353; AAF80228.1; -; mRNA. DR EMBL; AF250287; AAF81273.1; -; mRNA. DR EMBL; AF151364; AAG13120.1; -; mRNA. DR EMBL; AF218020; AAG17262.2; -; mRNA. DR EMBL; AK027367; BAB55065.1; -; mRNA. DR EMBL; CR457167; CAG33448.1; -; mRNA. DR EMBL; BC011677; AAH11677.1; -; mRNA. DR EMBL; BC031687; AAH31687.1; -; mRNA. DR UniGene; Hs.436500; -. DR PDB; 1X67; NMR; A=1-133. DR OGP; Q9UJU6; -. DR Ensembl; ENSG00000136279; Homo sapiens. DR KEGG; hsa:28988; -. DR HGNC; HGNC:2696; DBNL. DR MIM; 610106; gene. DR ArrayExpress; Q9UJU6; -. DR GermOnline; ENSG00000136279; Homo sapiens. DR RZPD-ProtExp; RZPDo834C1012; -. DR RZPD-ProtExp; U0761; -. DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB. DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc. DR GO; GO:0007257; P:activation of JNK activity; TAS:ProtInc. DR GO; GO:0016601; P:Rac protein signal transduction; ISS:UniProtKB. DR InterPro; IPR002108; cofln_actin_bd. DR InterPro; IPR001452; SH3. DR Pfam; PF00241; Cofilin_ADF; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000066; SH3; 1. DR SMART; SM00102; ADF; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS51263; ADF_H; 1. DR PROSITE; PS50002; SH3; 1. KW 3D-structure; Actin-binding; Alternative splicing; Coiled coil; KW Cytoskeleton; Endocytosis; Immune response; Phosphorylation; KW SH3 domain. FT CHAIN 1 430 Drebrin-like protein. FT /FTId=PRO_0000079793. FT DOMAIN 4 133 ADF-H. FT DOMAIN 371 430 SH3. FT COILED 176 231 Potential. FT SITE 361 362 Cleavage (by caspase-3). FT MOD_RES 162 162 Phosphotyrosine. FT MOD_RES 232 232 Phosphoserine. FT MOD_RES 269 269 Phosphoserine (By similarity). FT MOD_RES 272 272 Phosphoserine (By similarity). FT MOD_RES 283 283 Phosphoserine. FT MOD_RES 334 334 Phosphotyrosine (By similarity). FT MOD_RES 344 344 Phosphotyrosine (By similarity). FT VAR_SEQ 234 234 Q -> QS (in isoform 2 and isoform 3). FT /FTId=VSP_011398. FT VAR_SEQ 251 251 Q -> QGSTCASLQ (in isoform 3). FT /FTId=VSP_011399. FT MUTAGEN 361 361 D->A: Abolishes cleavage by caspase-3. FT CONFLICT 8 8 N -> K (in Ref. 4). FT CONFLICT 98 98 A -> S (in Ref. 3). FT CONFLICT 235 235 R -> S (in Ref. 3). FT CONFLICT 430 430 E -> D (in Ref. 5). FT HELIX 9 20 FT STRAND 22 25 FT STRAND 27 38 FT STRAND 40 48 FT HELIX 50 56 FT STRAND 61 70 FT STRAND 72 74 FT STRAND 76 85 FT HELIX 91 107 FT TURN 108 110 FT STRAND 111 115 FT HELIX 120 123 SQ SEQUENCE 430 AA; 48207 MW; 7E8C42ED047257AE CRC64; MAANLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EEMVEELNSG KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACASH VSTMASFLKG AHVTINARAE EDVEPECIME KVAKASGANY SFHKESGRFQ DVGPQAPVGS VYQKTNAVSE IKRVGKDSFW AKAEKEEENR RLEEKRRAEE AQRQLEQERR ERELREAARR EQRYQEQGGE ASPQRTWEQQ QEVVSRNRNE QESAVHPREI FKQKERAMST TSISSPQPGK LRSPFLQKQL TQPETHFGRE PAAAISRPRA DLPAEEPAPS TPPCLVQAEE EAVYEEPPEQ ETFYEQPPLV QQQGAGSEHI DHHIQGQGLS GQGLCARALY DYQAADDTEI SFDPENLITG IEVIDEGWWR GYGPDGHFGM FPANYVELIE //