ID PLST_HUMAN STANDARD; PRT; 630 AA. AC P13797; DT 01-JAN-1990 (REL. 13, CREATED) DT 01-FEB-1991 (REL. 17, LAST SEQUENCE UPDATE) DT 01-JUL-1993 (REL. 26, LAST ANNOTATION UPDATE) DE T-PLASTIN (FIMBRIN). OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. 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.; RL MOL. CELL. BIOL. 8:4659-4668(1988). RN [2] RP REVISIONS. RX MEDLINE; 90205868. RA LIN C.-S., AEBERSOLD R.H., LEAVITT J.; RL MOL. CELL. BIOL. 10:1818-1821(1990). RN [3] RP SEQUENCE OF 588-630 FROM N.A. RX MEDLINE; 93155095. RA LIN C.-S., PARK T., CHEN Z.P., LEAVITT J.; 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: THERE EXIST AT LEAST TWO ISOFORMS OF PLASTIN, CC L-PLASTIN AND T-PLASTIN. THEIR EXPRESSION IS REGULATED IN A CC TISSUE-SPECIFIC MANNER. T-PLASTIN OCCURS ON NORMAL AND TRANSFORMED CC FIBROBLASTS, BUT NOT ON LEUCOCYTES. CC -!- PTM: PHOSPHORYLATED. CC -!- SIMILARITY: THE CALCIUM-BINDING DOMAINS BELONG TO THE EF-HAND CC MORE SPECIFICALLY TO THE LIGHT CHAIN OF CALPAIN. 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 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; M22299. DR EMBL; M34427; M34427. DR EMBL; L05491; L05491. DR PIR; B31559; B31559. DR PIR; A34789; A34789. DR HSSP; P02588; 1TOP. DR PROSITE; PS00018; EF_HAND. DR PROSITE; PS00019; ACTININ_1. DR PROSITE; PS00020; ACTININ_2. KW CALCIUM-BINDING; PHOSPHORYLATION; ACTIN-BINDING; DUPLICATION. FT CA_BIND 25 36 BY SIMILARITY. FT CA_BIND 65 76 BY SIMILARITY. FT DOMAIN 109 382 ACTIN-BINDING 1. FT DOMAIN 383 624 ACTIN-BINDING 2. SQ SEQUENCE 630 AA; 70811 MW; 1956642 CN; 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 //