ID PLST_HUMAN Reviewed; 627 AA. AC P13797; B1AQ09; Q86YI6; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 3. DT 16-DEC-2008, entry version 105. DE RecName: Full=Plastin-3; DE AltName: Full=T-plastin; GN Name=PLS3; 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], AND PARTIAL PROTEIN SEQUENCE. RX MEDLINE=89096835; PubMed=3211125; RA Lin C.-S., Aebersold R.H., Kent S.B., Varma M., Leavitt J.; RT "Molecular cloning and characterization of plastin, a human leukocyte RT protein expressed in transformed human fibroblasts."; RL Mol. Cell. Biol. 8:4659-4668(1988). RN [2] RP SEQUENCE REVISION. RX MEDLINE=90205868; PubMed=2378651; RA Lin C.-S., Aebersold R.H., Leavitt J.; RT "Correction of the N-terminal sequences of the human plastin isoforms RT by using anchored polymerase chain reaction: identification of a RT potential calcium-binding domain."; RL Mol. Cell. Biol. 10:1818-1821(1990). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta, and Skin; 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 585-627. RX MEDLINE=93155095; PubMed=8428952; RA Lin C.-S., Park T., Chen Z.P., Leavitt J.; RT "Human plastin genes. Comparative gene structure, chromosome location, RT and differential expression in normal and neoplastic cells."; RL J. Biol. Chem. 268:2781-2792(1993). RN [6] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-165, AND MASS RP SPECTROMETRY. RX PubMed=17370265; DOI=10.1002/pmic.200600410; RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; RT "Tryptic digestion of ubiquitin standards reveals an improved strategy RT for identifying ubiquitinated proteins by mass spectrometry."; RL Proteomics 7:868-874(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-114, AND MASS RP SPECTROMETRY. RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474 AND THR-489, AND RP MASS SPECTROMETRY. RX PubMed=18187866; DOI=10.2116/analsci.24.161; RA Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; RT "Automated phosphoproteome analysis for cultured cancer cells by two- RT dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; RL Anal. Sci. 24:161-166(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND THR-388, AND RP MASS SPECTROMETRY. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 118-372. RX MEDLINE=97448672; PubMed=9302997; DOI=10.1038/nsb0997-708; RA Goldsmith S.C., Pokala N., Shen W., Fedorov A.A., Matsudaira P., RA Almo S.C.; RT "The structure of an actin-crosslinking domain from human fimbrin."; RL Nat. Struct. Biol. 4:708-712(1997). RN [11] RP STRUCTURE BY NMR OF 517-627. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the fourth CH domain from human plastin 3 T- RT isoform."; RL Submitted (NOV-2004) to the PDB data bank. RN [12] RP VARIANT [LARGE SCALE ANALYSIS] ALA-485. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Actin-bundling protein found in intestinal microvilli, CC hair cell stereocilia, and fibroblast filopodia. CC -!- SUBUNIT: Monomer. CC -!- INTERACTION: CC Q99700:ATXN2; NbExp=1; IntAct=EBI-698052, EBI-697691; CC P30480:HLA-B; NbExp=1; IntAct=EBI-698052, EBI-1054175; CC Q14164:IKBKE; NbExp=1; IntAct=EBI-698052, EBI-307369; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed in a variety of organs, including CC muscle, brain, uterus, and esophagus. CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. CC -!- SIMILARITY: Contains 2 actin-binding domains. CC -!- SIMILARITY: Contains 4 CH (calponin-homology) domains. CC -!- SIMILARITY: Contains 2 EF-hand domains. 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; M22299; AAB02844.1; ALT_INIT; mRNA. DR EMBL; M34427; AAA36759.1; ALT_INIT; mRNA. DR EMBL; AL589842; CAI39884.1; -; Genomic_DNA. DR EMBL; AC005000; CAI39884.1; JOINED; Genomic_DNA. DR EMBL; BC039049; AAH39049.1; ALT_INIT; mRNA. DR EMBL; BC056898; AAH56898.1; ALT_INIT; mRNA. DR EMBL; L05491; AAA61214.1; -; Genomic_DNA. DR PIR; A34789; A34789. DR RefSeq; NP_005023.2; -. DR UniGene; Hs.496622; -. DR PDB; 1AOA; X-ray; 2.40 A; A=98-372. DR PDB; 1WJO; NMR; -; A=517-627. DR PDBsum; 1AOA; -. DR PDBsum; 1WJO; -. DR IntAct; P13797; 8. DR PhosphoSite; P13797; -. DR PRIDE; P13797; -. DR Ensembl; ENSG00000102024; Homo sapiens. DR GeneID; 5358; -. DR KEGG; hsa:5358; -. DR GeneCards; GC0XP114618; -. DR H-InvDB; HIX0028362; -. DR HGNC; HGNC:9091; PLS3. DR MIM; 300131; gene. DR PharmGKB; PA33418; -. DR HOVERGEN; P13797; -. DR LinkHub; P13797; -. DR NextBio; 20770; -. DR ArrayExpress; P13797; -. DR CleanEx; HS_PLS3; -. DR GermOnline; ENSG00000102024; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0003779; F:actin binding; IEA:InterPro. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR016146; Calponin-homology. DR InterPro; IPR001715; Calponin_act_bd. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR002048; EF_hand_Ca_bd. DR Gene3D; G3DSA:1.10.418.10; Calponin-homology; 4. DR Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1. DR Pfam; PF00307; CH; 4. DR Pfam; PF00036; efhand; 2. DR ProDom; PD000012; EF-hand; 1. DR SMART; SM00033; CH; 4. DR SMART; SM00054; EFh; 2. DR PROSITE; PS00019; ACTININ_1; 2. DR PROSITE; PS00020; ACTININ_2; 2. DR PROSITE; PS50021; CH; 4. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS50222; EF_HAND_2; 2. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Calcium; Cytoplasm; KW Direct protein sequencing; Phosphoprotein; Polymorphism; Repeat; KW Ubl conjugation. FT CHAIN 1 627 Plastin-3. FT /FTId=PRO_0000073747. FT DOMAIN 9 44 EF-hand 1. FT DOMAIN 49 84 EF-hand 2. FT DOMAIN 106 379 Actin-binding 1. FT DOMAIN 120 236 CH 1. FT DOMAIN 264 375 CH 2. FT DOMAIN 380 624 Actin-binding 2. FT DOMAIN 394 503 CH 3. FT DOMAIN 515 624 CH 4. FT CA_BIND 22 33 1 (By similarity). FT CA_BIND 62 73 2 (By similarity). FT MOD_RES 114 114 Phosphothreonine. FT MOD_RES 323 323 Phosphoserine. FT MOD_RES 388 388 Phosphothreonine. FT MOD_RES 474 474 Phosphoserine. FT MOD_RES 489 489 Phosphothreonine. FT CROSSLNK 165 165 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT VARIANT 485 485 D -> A (in a breast cancer sample; FT somatic mutation). FT /FTId=VAR_035462. FT HELIX 120 133 FT TURN 134 136 FT TURN 141 143 FT TURN 148 151 FT HELIX 152 156 FT HELIX 157 159 FT HELIX 161 170 FT HELIX 177 179 FT HELIX 187 203 FT HELIX 213 217 FT HELIX 221 241 FT HELIX 258 262 FT HELIX 266 280 FT TURN 291 295 FT HELIX 297 306 FT STRAND 312 314 FT TURN 323 326 FT HELIX 330 341 FT TURN 342 345 FT HELIX 352 356 FT HELIX 360 371 FT HELIX 519 532 FT HELIX 546 548 FT HELIX 550 559 FT TURN 566 568 FT HELIX 576 592 FT HELIX 601 606 FT TURN 609 613 FT HELIX 614 622 SQ SEQUENCE 627 AA; 70436 MW; 52AC3E044D198D19 CRC64; MATTQISKDE LDELKEAFAK VDLNSNGFIC DYELHELFKE ANMPLPGYKV REIIQKLMLD GDRNKDGKIS FDEFVYIFQE VKSSDIAKTF RKAINRKEGI CALGGTSELS SEGTQHSYSE EEKYAFVNWI NKALENDPDC RHVIPMNPNT DDLFKAVGDG IVLCKMINLS VPDTIDERAI NKKKLTPFII QENLNLALNS ASAIGCHVVN IGAEDLRAGK PHLVLGLLWQ IIKIGLFADI ELSRNEALAA LLRDGETLEE LMKLSPEELL LRWANFHLEN SGWQKINNFS ADIKDSKAYF HLLNQIAPKG QKEGEPRIDI NMSGFNETDD LKRAESMLQQ ADKLGCRQFV TPADVVSGNP KLNLAFVANL FNKYPALTKP ENQDIDWTLL EGETREERTF RNWMNSLGVN PHVNHLYADL QDALVILQLY ERIKVPVDWS KVNKPPYPKL GANMKKLENC NYAVELGKHP AKFSLVGIGG QDLNDGNQTL TLALVWQLMR RYTLNVLEDL GDGQKANDDI IVNWVNRTLS EAGKSTSIQS FKDKTISSSL AVVDLIDAIQ PGCINYDLVK SGNLTEDDKH NNAKYAVSMA RRIGARVYAL PEDLVEVKPK MVMTVFACLM GRGMKRV //