ID   T1B_PARTE               Reviewed;         369 AA.
AC   Q27180; A0EI57; Q27247;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Trichocyst matrix protein T1-B;
DE   AltName: Full=Secretory granule protein T1-B;
DE   AltName: Full=TMP 1-B;
DE   Contains:
DE     RecName: Full=Trichocyst matrix protein T1-B 1;
DE   Contains:
DE     RecName: Full=Trichocyst matrix protein T1-B 2;
DE   Flags: Precursor;
GN   Name=T1B; ORFNames=GSPATT00027326001;
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Stock d4-2;
RX   PubMed=8626591; DOI=10.1074/jbc.271.17.10247;
RA   Gautier M.-C., Sperling L., Madeddu L.;
RT   "Cloning and sequence analysis of genes coding for paramecium secretory
RT   granule (trichocyst) proteins. A unique protein fold for a family of
RT   polypeptides with different primary structures.";
RL   J. Biol. Chem. 271:10247-10255(1996).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 226-259.
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   [4]
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   -!- PTM: Two components are produced by post-translational processing from
CC       the precursor peptide.
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";
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DR   EMBL; U47115; AAC47027.1; -; Genomic_DNA.
DR   EMBL; CT868680; CAK94998.1; -; Genomic_DNA.
DR   EMBL; U27504; AAA92604.1; -; Genomic_DNA.
DR   RefSeq; XP_001462371.1; XM_001462334.1.
DR   AlphaFoldDB; Q27180; -.
DR   SMR; Q27180; -.
DR   EnsemblProtists; CAK94998; CAK94998; GSPATT00027326001.
DR   GeneID; 5048156; -.
DR   KEGG; ptm:GSPATT00027326001; -.
DR   HOGENOM; CLU_065271_0_0_1; -.
DR   InParanoid; Q27180; -.
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                   /id="PRO_0000034377"
FT   CHAIN           56..189
FT                   /note="Trichocyst matrix protein T1-B 1"
FT                   /id="PRO_0000034378"
FT   PROPEP          190..225
FT                   /id="PRO_0000034379"
FT   CHAIN           226..369
FT                   /note="Trichocyst matrix protein T1-B 2"
FT                   /id="PRO_0000034380"
FT   COILED          56..180
FT                   /evidence="ECO:0000255"
FT   COILED          262..354
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   369 AA;  41963 MW;  82CFD93E424BA3AD CRC64;
     MYKLAVCTLL ILSVTAIDVT NSVWTSHDQK AFAQIKQSGW GNFILNFGEL HLQTGGILAE
     LNTEIAKLID ELDEELAEVH HQYARRTDVH NREVSRLEQE IQDKEREVFN AHDFYDNVLI
     PQRDRFAAQL EQLQENIAQN RRTLNEATVQ RANDHAEFES QVAEHNEAIS AIDESLQLLS
     QLESPSLVQI QKVQKNLTKI QQSLKRHSTF QTFIKTLLEI AVEANFADQG ALREILTAFN
     NLRVQLVDSL NQLTADEAEA QKDFEARVIQ LNQEHAEFQR AVVVKTAEIE ANANKIEQTL
     DLIDVLHADL DTLNGQLQAE NDDYAFATDV YNATVSEYNK ELNAAHQALD LLNQPRFTDY
     VKSQLKGAF