ID PLST_HUMAN Reviewed; 630 AA. AC P13797; B1AQ09; Q86YI6; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 4. DT 08-MAR-2011, entry version 131. 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 588-630. 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-168, AND MASS RP SPECTROMETRY. RC TISSUE=Mammary cancer; 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-117, AND MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; 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-477 AND THR-492, AND RP MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; 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-326 AND THR-391, AND RP MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [11] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 101-375. 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 [12] RP STRUCTURE BY NMR OF 520-630. 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 [13] RP VARIANT [LARGE SCALE ANALYSIS] ALA-488. 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 -!- SEQUENCE CAUTION: CC Sequence=CAI39884.1; Type=Erroneous initiation; 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; -; mRNA. DR EMBL; M34427; AAA36759.1; -; mRNA. DR EMBL; AL589842; CAI39884.1; ALT_INIT; Genomic_DNA. DR EMBL; AC005000; CAI39884.1; JOINED; Genomic_DNA. DR EMBL; BC039049; AAH39049.1; -; mRNA. DR EMBL; BC056898; AAH56898.1; -; mRNA. DR EMBL; L05491; AAA61214.1; -; Genomic_DNA. DR IPI; IPI00216694; -. DR PIR; A34789; A34789. DR RefSeq; NP_001129497.1; NM_001136025.3. DR RefSeq; NP_005023.2; NM_005032.5. DR UniGene; Hs.496622; -. DR PDB; 1AOA; X-ray; 2.40 A; A=101-375. DR PDB; 1WJO; NMR; -; A=520-627. DR PDBsum; 1AOA; -. DR PDBsum; 1WJO; -. DR ProteinModelPortal; P13797; -. DR SMR; P13797; 11-85, 121-375, 398-630. DR IntAct; P13797; 16. DR STRING; P13797; -. DR PhosphoSite; P13797; -. DR PRIDE; P13797; -. DR Ensembl; ENST00000355899; ENSP00000348163; ENSG00000102024. DR Ensembl; ENST00000420625; ENSP00000398945; ENSG00000102024. DR GeneID; 5358; -. DR KEGG; hsa:5358; -. DR CTD; 5358; -. DR GeneCards; GC0XP114795; -. DR H-InvDB; HIX0028362; -. DR HGNC; HGNC:9091; PLS3. DR MIM; 300131; gene. DR neXtProt; NX_P13797; -. DR eggNOG; prNOG16165; -. DR HOGENOM; HBG316743; -. DR HOVERGEN; HBG003082; -. DR InParanoid; P13797; -. DR OMA; MLQQADR; -. DR OrthoDB; EOG4FJ88C; -. DR PhylomeDB; P13797; -. DR NextBio; 20770; -. DR ArrayExpress; P13797; -. DR Bgee; P13797; -. DR CleanEx; HS_PLS3; -. DR Genevestigator; P13797; -. DR GermOnline; ENSG00000102024; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH-domain. DR InterPro; IPR011992; EF-hand-like_dom. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR018249; EF_HAND_2. 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 SMART; SM00033; CH; 4. DR SMART; SM00054; EFh; 2. DR SUPFAM; SSF47576; Calponin-homology; 1. 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; Complete proteome; Cytoplasm; KW Direct protein sequencing; Isopeptide bond; Phosphoprotein; KW Polymorphism; Repeat; Ubl conjugation. FT CHAIN 1 630 Plastin-3. FT /FTId=PRO_0000073747. FT DOMAIN 12 47 EF-hand 1. FT DOMAIN 52 87 EF-hand 2. FT DOMAIN 109 382 Actin-binding 1. FT DOMAIN 123 239 CH 1. FT DOMAIN 267 378 CH 2. FT DOMAIN 383 627 Actin-binding 2. FT DOMAIN 397 506 CH 3. FT DOMAIN 518 627 CH 4. FT CA_BIND 25 36 1 (By similarity). FT CA_BIND 65 76 2 (By similarity). FT MOD_RES 117 117 Phosphothreonine. FT MOD_RES 326 326 Phosphoserine. FT MOD_RES 391 391 Phosphothreonine. FT MOD_RES 477 477 Phosphoserine. FT MOD_RES 492 492 Phosphothreonine. FT CROSSLNK 168 168 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT VARIANT 488 488 D -> A (in a breast cancer sample; FT somatic mutation). FT /FTId=VAR_035462. FT HELIX 123 136 FT TURN 137 139 FT TURN 144 146 FT TURN 151 154 FT HELIX 155 159 FT HELIX 160 162 FT HELIX 164 173 FT HELIX 180 182 FT HELIX 190 206 FT HELIX 216 220 FT HELIX 224 244 FT HELIX 261 265 FT HELIX 269 283 FT TURN 294 298 FT HELIX 300 309 FT STRAND 315 317 FT TURN 326 329 FT HELIX 333 344 FT TURN 345 348 FT HELIX 355 359 FT HELIX 363 374 FT HELIX 522 535 FT HELIX 549 551 FT HELIX 553 562 FT TURN 569 571 FT HELIX 579 595 FT HELIX 604 609 FT TURN 612 616 FT HELIX 617 625 SQ SEQUENCE 630 AA; 70811 MW; 631E6F803DC56A56 CRC64; MDEMATTQIS KDELDELKEA FAKVDLNSNG FICDYELHEL FKEANMPLPG YKVREIIQKL MLDGDRNKDG KISFDEFVYI FQEVKSSDIA KTFRKAINRK EGICALGGTS ELSSEGTQHS YSEEEKYAFV NWINKALEND PDCRHVIPMN PNTDDLFKAV GDGIVLCKMI NLSVPDTIDE RAINKKKLTP FIIQENLNLA LNSASAIGCH VVNIGAEDLR AGKPHLVLGL LWQIIKIGLF ADIELSRNEA LAALLRDGET LEELMKLSPE ELLLRWANFH LENSGWQKIN NFSADIKDSK AYFHLLNQIA PKGQKEGEPR IDINMSGFNE TDDLKRAESM LQQADKLGCR QFVTPADVVS GNPKLNLAFV ANLFNKYPAL TKPENQDIDW TLLEGETREE RTFRNWMNSL GVNPHVNHLY ADLQDALVIL QLYERIKVPV DWSKVNKPPY PKLGANMKKL ENCNYAVELG KHPAKFSLVG IGGQDLNDGN QTLTLALVWQ LMRRYTLNVL EDLGDGQKAN DDIIVNWVNR TLSEAGKSTS IQSFKDKTIS SSLAVVDLID AIQPGCINYD LVKSGNLTED DKHNNAKYAV SMARRIGARV YALPEDLVEV KPKMVMTVFA CLMGRGMKRV //