ID   T2C_PARTE               Reviewed;         387 AA.
AC   Q27181; A0E6M9; Q27175;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Trichocyst matrix protein T2-C;
DE   AltName: Full=Secretory granule protein T2-C;
DE   AltName: Full=TMP 2-C;
DE   Contains:
DE     RecName: Full=Trichocyst matrix protein T2-C 1;
DE   Contains:
DE     RecName: Full=Trichocyst matrix protein T2-C 2;
DE   Flags: Precursor;
GN   Name=T2C; ORFNames=GSPATT00003811001;
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 49-72.
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; U47116; AAC47028.1; -; Genomic_DNA.
DR   EMBL; CT868660; CAK90946.1; -; Genomic_DNA.
DR   EMBL; U27511; AAA92611.1; -; Genomic_DNA.
DR   RefSeq; XP_001458343.1; XM_001458306.1.
DR   AlphaFoldDB; Q27181; -.
DR   SMR; Q27181; -.
DR   EnsemblProtists; CAK90946; CAK90946; GSPATT00003811001.
DR   GeneID; 5044128; -.
DR   KEGG; ptm:GSPATT00003811001; -.
DR   eggNOG; ENOG502SUHG; Eukaryota.
DR   HOGENOM; CLU_062544_0_0_1; -.
DR   InParanoid; Q27181; -.
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..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..48
FT                   /id="PRO_0000034381"
FT   CHAIN           49..183
FT                   /note="Trichocyst matrix protein T2-C 1"
FT                   /id="PRO_0000034382"
FT   PROPEP          184..239
FT                   /id="PRO_0000034383"
FT   CHAIN           240..387
FT                   /note="Trichocyst matrix protein T2-C 2"
FT                   /id="PRO_0000034384"
FT   COILED          51..163
FT                   /evidence="ECO:0000255"
FT   COILED          294..333
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   387 AA;  43312 MW;  D6885D7E22EED1D8 CRC64;
     MKTIILALAL IVLASSTQAD VIATIKKIDQ SPFGRTLFDT IWLELQTGDP LDRLLQTLTD
     LEDRYVAEQK EDDARNHEYQ DACTVDIKAF DKDLAESNRK KIELEARLEG QLYPQRGILQ
     GLVAQKQAEV KGYQKDLDEL DAQRAEEKAD FEEKVLEHQE ATAIIAEARR LFADNIEHES
     FIQKGKATKQ PAHKFTKEVA SMIQKHFTTS AKKAAKFQHR KGYSKLFKAF ATIASKVEQL
     ADAGAVSKII DLADELLAKI ADSLSLLRFA EDKRVEAYKK SRNFIVISLT VAGTALANAQ
     SDLAALNDVI AQVEASLDTT NQRIENVSAD RNDRFTQCEE AVQDYQDARS ARSSDRDVVS
     QTIGLVNKEL RTLREQLALR QSAGEEI