ID V9HWI5_HUMAN Unreviewed; 166 AA. AC V9HWI5; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 12-APR-2017, entry version 34. DE SubName: Full=Cofilin 1 (Non-muscle), isoform CRA_b {ECO:0000313|EMBL:EAW74452.1}; DE SubName: Full=Epididymis secretory protein Li 15 {ECO:0000313|EMBL:ACJ13657.1}; GN Name=HEL-S-15 {ECO:0000313|EMBL:ACJ13657.1}; GN Synonyms=CFL1 {ECO:0000313|EMBL:EAW74452.1}; GN ORFNames=hCG_2039457 {ECO:0000313|EMBL:EAW74452.1}; 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 {ECO:0000313|EMBL:ACJ13657.1}; RN [1] {ECO:0000313|EMBL:EAW74452.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11181995; DOI=10.1126/science.1058040; RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., RA Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., RA Kodira C.D., Zheng X.H., Chen L., Skupski M., Subramanian G., RA Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., RA Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., RA Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., RA Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., RA Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., RA Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., RA Brandon R., Cargill M., Chandramouliswaran I., Charlab R., RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., RA Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., RA Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., RA Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., RA Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., RA Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., RA Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., RA Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., RA Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., RA Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., RA Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., RA Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., RA Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., RA Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., RA Kline L., Koduru S., Love A., Mann F., May D., McCawley S., RA McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., RA Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., RA Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., RA Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., RA Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., RA Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., RA Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., RA Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., RA Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., RA Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., RA Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., RA Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., RA Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., RA Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., RA McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., RA Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.; RT "The sequence of the human genome."; RL Science 291:1304-1351(2001). RN [2] {ECO:0000313|EMBL:EAW74452.1} RP NUCLEOTIDE SEQUENCE. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ACJ13657.1} RP NUCLEOTIDE SEQUENCE. RA Li J.Y., Wang H.Y., Liu F.J., Liu J.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. CC {ECO:0000256|SAAS:SAAS00548240}. 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; EU794603; ACJ13657.1; -; mRNA. DR EMBL; CH471076; EAW74452.1; -; Genomic_DNA. DR RefSeq; NP_005498.1; NM_005507.2. DR UniGene; Hs.170622; -. DR STRING; 9606.ENSP00000309629; -. DR GeneID; 1072; -. DR KEGG; hsa:1072; -. DR UCSC; uc001ofs.4; human. DR CTD; 1072; -. DR eggNOG; KOG1735; Eukaryota. DR eggNOG; ENOG41122P5; LUCA. DR KO; K05765; -. DR ChiTaRS; CFL1; human. DR GenomeRNAi; 1072; -. DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro. DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl. DR GO; GO:0030175; C:filopodium; IEA:Ensembl. DR GO; GO:0030426; C:growth cone; IEA:Ensembl. DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl. DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IEA:Ensembl. DR GO; GO:0030042; P:actin filament depolymerization; IEA:InterPro. DR GO; GO:0030030; P:cell projection organization; IEA:Ensembl. DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl. DR GO; GO:0071362; P:cellular response to ether; IEA:Ensembl. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl. DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl. DR GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl. DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; IEA:Ensembl. DR GO; GO:0007162; P:negative regulation of cell adhesion; IEA:Ensembl. DR GO; GO:2000146; P:negative regulation of cell motility; IEA:Ensembl. DR GO; GO:0045792; P:negative regulation of cell size; IEA:Ensembl. DR GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IEA:Ensembl. DR GO; GO:0010593; P:negative regulation of lamellipodium assembly; IEA:Ensembl. DR GO; GO:0051511; P:negative regulation of unidimensional cell growth; IEA:Ensembl. DR GO; GO:2000814; P:positive regulation of barbed-end actin filament capping; IEA:Ensembl. DR GO; GO:2000147; P:positive regulation of cell motility; IEA:Ensembl. DR GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl. DR GO; GO:2000784; P:positive regulation of establishment of cell polarity regulating cell shape; IEA:Ensembl. DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl. DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl. DR GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; IEA:Ensembl. DR GO; GO:1904377; P:positive regulation of protein localization to cell periphery; IEA:Ensembl. DR GO; GO:0045862; P:positive regulation of proteolysis; IEA:Ensembl. DR GO; GO:0031915; P:positive regulation of synaptic plasticity; IEA:Ensembl. DR GO; GO:0097107; P:postsynaptic density assembly; IEA:Ensembl. DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl. DR CDD; cd11286; ADF_cofilin_like; 1. DR Gene3D; 3.40.20.10; -; 1. DR InterPro; IPR002108; ADF-H. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom. DR InterPro; IPR017904; ADF/Cofilin. DR InterPro; IPR027234; Cofilin_1. DR PANTHER; PTHR11913; PTHR11913; 1. DR PANTHER; PTHR11913:SF37; PTHR11913:SF37; 1. DR Pfam; PF00241; Cofilin_ADF; 1. DR PRINTS; PR00006; COFILIN. DR SMART; SM00102; ADF; 1. DR PROSITE; PS51263; ADF_H; 1. PE 2: Evidence at transcript level; KW Actin-binding {ECO:0000256|SAAS:SAAS00495136}. FT DOMAIN 4 153 ADF-H. {ECO:0000259|PROSITE:PS51263}. SQ SEQUENCE 166 AA; 18502 MW; 589EF8FC1EC13719 CRC64; MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL //