ID T1F_PARTE Reviewed; 368 AA. AC Q27172; A0BE79; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 2. DT 25-MAY-2022, entry version 64. DE RecName: Full=Trichocyst matrix protein T1-F; DE AltName: Full=Secretory granule protein T1-F; DE AltName: Full=TMP 1-F; DE Contains: DE RecName: Full=Trichocyst matrix protein T1-F 1; DE Contains: DE RecName: Full=Trichocyst matrix protein T1-F 2; DE Flags: Precursor; GN Name=T1F; ORFNames=GSPATT00027878001; OS Paramecium tetraurelia. OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium. OX NCBI_TaxID=5888; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Stock d4-2; RX PubMed=17086204; DOI=10.1038/nature05230; RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R., RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F., RA Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H., RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M., RA Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E., RA Cohen J., Wincker P.; RT "Global trends of whole-genome duplications revealed by the ciliate RT Paramecium tetraurelia."; RL Nature 444:171-178(2006). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 226-258. RC STRAIN=Stock d4-2; RX PubMed=7579685; DOI=10.1091/mbc.6.6.649; RA Madeddu L., Gautier M.-C., Vayssie L., Houari A., Sperling L.; RT "A large multigene family codes for the polypeptides of the crystalline RT trichocyst matrix in Paramecium."; RL Mol. Biol. Cell 6:649-659(1995). RN [3] RP PARTIAL PROTEIN SEQUENCE. RC STRAIN=Stock d4-2; RX PubMed=7819344; DOI=10.1016/0300-9084(94)90167-8; RA Madeddu L., Gautier M.-C., le Caer J.-P., de Loubresse N., Sperling L.; RT "Protein processing and morphogenesis of secretory granules in RT Paramecium."; RL Biochimie 76:329-335(1994). CC -!- FUNCTION: Structural protein that crystallize inside the trichocyst CC matrix. CC -!- SUBCELLULAR LOCATION: Trichocyst. Note=These are architecturally CC complex secretory storage granules-docked at the plasma membrane, ready CC to rapidly respond to an exocytotic stimulus. CC -!- SIMILARITY: Belongs to the TMP family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The arsenal of Paramecium CC - Issue 3 of October 2000; CC URL="https://web.expasy.org/spotlight/back_issues/003"; 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; CT867988; CAK56846.1; -; Genomic_DNA. DR EMBL; U27508; AAA92608.1; -; Genomic_DNA. DR RefSeq; XP_001424244.1; XM_001424207.1. DR AlphaFoldDB; Q27172; -. DR SMR; Q27172; -. DR EnsemblProtists; CAK56846; CAK56846; GSPATT00027878001. DR GeneID; 5010028; -. DR KEGG; ptm:GSPATT00027878001; -. DR HOGENOM; CLU_065271_0_0_1; -. DR InParanoid; Q27172; -. DR Proteomes; UP000000600; Partially assembled WGS sequence. DR GO; GO:0055039; C:trichocyst; IEA:UniProtKB-SubCell. PE 1: Evidence at protein level; KW Coiled coil; Direct protein sequencing; Reference proteome; Signal. FT SIGNAL 1..16 FT /evidence="ECO:0000255" FT PROPEP 17..55 FT /evidence="ECO:0000250" FT /id="PRO_0000307839" FT CHAIN 56..189 FT /note="Trichocyst matrix protein T1-F 1" FT /id="PRO_0000307840" FT PROPEP 190..225 FT /evidence="ECO:0000250" FT /id="PRO_0000307841" FT CHAIN 226..368 FT /note="Trichocyst matrix protein T1-F 2" FT /id="PRO_0000221507" FT COILED 56..153 FT /evidence="ECO:0000255" FT COILED 257..354 FT /evidence="ECO:0000255" SQ SEQUENCE 368 AA; 41481 MW; 90DCDD3240141F06 CRC64; MFKVAVCALL VLASTAINVQ SSIWTSKDQK AFAQIHQSGW GKFILNFAEL HLTTGGILSE LNSEIEKLIG EMEEELAGVH HEFNRRTDVH NREVARLEQE IQDKERELFN AHDFYDNVLI PQGERFAAQL EQLQENIAHN RQTLEQATVQ RANDHETFES EVVEHNDAIS AIDECLQLLS TIAAPSLAEV KKVQKNLAKI QNSLKKHNQF QIFVKVLLEI TVDSNFADQG ALRDIIVAFN NLRVELVDSL NQITADEAEQ VADYNAQVIA LNQEHAEFQR AVVVKNAEIE ANTTKQEQTL DLIDELDEDL ATLNGQLQAE NDDYAFATDV YNATVAEYNK EINAANQALD LLNQPRFQDY VKSQLKGA //