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 15-JUL-1998 (REL. 36, LAST ANNOTATION UPDATE) DE T-PLASTIN. GN PLS3. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; MAMMALIA; EUTHERIA; OC PRIMATES; CATARRHINI; HOMINIDAE; HOMO. RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE; 89096835. 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. 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. 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). 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: TO OTHER EF-HAND CALCIUM BINDING PROTEINS. CC -!- SIMILARITY: THE ACTIN-BINDING DOMAIN IS OF A TYPE FOUND IN MANY CC ACTIN-BINDING PROTEINS (SUCH AS ACTININ, DYSTROPHIN, FIMBRIN, CC ABP-120, ABP-180, OR BETA-FODRIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; G190028; ALT_INIT. DR EMBL; M34427; G339848; ALT_INIT. DR EMBL; L05491; G292832; -. DR PIR; B31559; B31559. DR PIR; A34789; A34789. DR PDB; 1AOA; 31-DEC-97. DR MIM; 300131; -. DR PROSITE; PS00018; EF_HAND; 2. DR PROSITE; PS00019; ACTININ_1; 2. DR PROSITE; PS00020; ACTININ_2; 2. DR PFAM; PF00036; efhand; 2. DR PFAM; PF00307; actinin-binding; 2. KW CALCIUM-BINDING; PHOSPHORYLATION; ACTIN-BINDING; REPEAT; 3D-STRUCTURE. FT CA_BIND 22 33 SITE 1 (BY SIMILARITY). FT CA_BIND 62 73 SITE 2 (BY SIMILARITY). FT DOMAIN 106 379 ACTIN-BINDING 1. FT DOMAIN 380 621 ACTIN-BINDING 2. SQ SEQUENCE 627 AA; 70435 MW; 7B10D65E CRC32; 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 //