ID PLST_HUMAN STANDARD; PRT; 627 AA. AC P13797; DT 01-JAN-1990 (Rel. 13, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE T-plastin. GN PLS3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL 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 REVISIONS. 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 SEQUENCE OF 585-627 FROM N.A. RX MEDLINE=93155095; PubMed=8428952; RA Lin C.-S., Park T., Chen Z.P., Leavitt J.; RT "Human plastin genes. Comparative gene structure, chromosome RT location, and differential expression in normal and neoplastic RT cells."; RL J. Biol. Chem. 268:2781-2792(1993). RN [4] 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 -!- SUBCELLULAR LOCATION: Cytoplasmic. 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 CALPONIN-HOMOLOGY (CH) DOMAINS. CC -!- SIMILARITY: CONTAINS 2 EF-HAND CALCIUM-BINDING 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. DR EMBL; M34427; AAA36759.1; ALT_INIT. DR EMBL; L05491; AAA61214.1; -. DR PIR; B31559; B31559. DR PIR; A34789; A34789. DR PDB; 1AOA; 31-DEC-97. DR MIM; 300131; -. DR InterPro; IPR001589; Actinin_act_bind. DR InterPro; IPR001715; Calponin_hom. DR InterPro; IPR002048; EF-hand. DR Pfam; PF00307; CH; 4. DR Pfam; PF00036; efhand; 2. 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; 2. KW Calcium-binding; Phosphorylation; Actin-binding; Repeat; 3D-structure. FT CA_BIND 22 33 EF-HAND 1 (BY SIMILARITY). FT CA_BIND 62 73 EF-HAND 2 (BY SIMILARITY). FT DOMAIN 120 236 CH 1. FT DOMAIN 264 375 CH 2. FT DOMAIN 394 503 CH 3. FT DOMAIN 515 624 CH 4. FT DOMAIN 106 379 ACTIN-BINDING 1. FT DOMAIN 380 624 ACTIN-BINDING 2. SQ SEQUENCE 627 AA; 70435 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 //