ID PLST_HUMAN STANDARD; PRT; 627 AA. AC P13797; Q86YI6; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 3. DT 05-SEP-2006, entry version 77. DE Plastin-3 (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, 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 MRNA]. RC TISSUE=Placenta, and Skin; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [4] RP NUCLEOTIDE SEQUENCE 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 [5] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 118-372. RX MEDLINE=97448672; PubMed=9302997; 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). 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 -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed in a variety of organs, including CC muscle, brain, uterus, and esophagus. CC -!- PTM: Phosphorylated. 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; 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 PDB; 1AOA; X-ray; @=98-372. DR PDB; 1WJO; NMR; A=517-627. DR IntAct; P13797; -. DR Ensembl; ENSG00000102024; Homo sapiens. DR HGNC; HGNC:9091; PLS3. DR MIM; 300131; gene. DR LinkHub; P13797; -. DR ArrayExpress; P13797; -. DR RZPD-ProtExp; IOH2504; -. DR RZPD-ProtExp; S0326; -. DR GO; GO:0005515; F:protein binding; IPI. DR InterPro; IPR001589; Actnin_actin_bd. DR InterPro; IPR001715; Calponin_act_bd. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR002048; EF_hand_Ca_bd. 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. KW 3D-structure; Actin-binding; Calcium; Direct protein sequencing; KW Phosphorylation; Repeat. 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 HELIX 120 133 FT TURN 134 136 FT TURN 138 139 FT STRAND 140 140 FT TURN 141 143 FT STRAND 145 145 FT TURN 148 151 FT HELIX 152 159 FT STRAND 160 160 FT HELIX 161 170 FT STRAND 171 171 FT TURN 172 173 FT STRAND 174 175 FT HELIX 177 179 FT STRAND 180 180 FT STRAND 183 184 FT HELIX 187 203 FT TURN 204 205 FT TURN 209 210 FT HELIX 213 217 FT TURN 218 219 FT HELIX 221 241 FT STRAND 242 243 FT TURN 245 246 FT HELIX 258 262 FT TURN 263 263 FT STRAND 264 264 FT HELIX 266 280 FT TURN 281 282 FT STRAND 287 287 FT STRAND 289 290 FT TURN 291 295 FT STRAND 296 296 FT HELIX 297 306 FT STRAND 307 307 FT STRAND 310 310 FT STRAND 312 314 FT TURN 323 326 FT STRAND 328 329 FT HELIX 330 341 FT TURN 342 345 FT STRAND 349 349 FT HELIX 352 356 FT TURN 357 358 FT HELIX 360 371 FT STRAND 513 513 FT STRAND 516 516 FT HELIX 519 532 FT TURN 533 533 FT STRAND 535 535 FT STRAND 539 539 FT TURN 541 542 FT TURN 544 545 FT HELIX 546 548 FT TURN 549 549 FT HELIX 550 559 FT STRAND 560 560 FT TURN 561 562 FT STRAND 563 563 FT TURN 566 568 FT STRAND 569 569 FT STRAND 572 573 FT HELIX 576 592 FT TURN 593 593 FT STRAND 596 596 FT HELIX 601 606 FT TURN 607 607 FT TURN 609 613 FT HELIX 614 622 FT STRAND 623 623 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 //