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T4A_PARTE
ID   T4A_PARTE               Reviewed;         363 AA.
AC   Q27182; A0BC94;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Trichocyst matrix protein T4-A;
DE   AltName: Full=Secretory granule protein T4-A;
DE   AltName: Full=TMP 4-A;
DE   Contains:
DE     RecName: Full=Trichocyst matrix protein T4-A 1;
DE   Contains:
DE     RecName: Full=Trichocyst matrix protein T4-A 2;
DE   Flags: Precursor;
GN   Name=T4A; ORFNames=GSPATT00004255001;
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 53-79.
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; U47117; AAC47029.1; -; Genomic_DNA.
DR   EMBL; CT867986; CAK56161.1; -; Genomic_DNA.
DR   RefSeq; XP_001423559.1; XM_001423522.1.
DR   AlphaFoldDB; Q27182; -.
DR   SMR; Q27182; -.
DR   EnsemblProtists; CAK56161; CAK56161; GSPATT00004255001.
DR   GeneID; 5009343; -.
DR   KEGG; ptm:GSPATT00004255001; -.
DR   eggNOG; ENOG502SR74; Eukaryota.
DR   HOGENOM; CLU_065704_0_0_1; -.
DR   InParanoid; Q27182; -.
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..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..52
FT                   /id="PRO_0000034385"
FT   CHAIN           53..189
FT                   /note="Trichocyst matrix protein T4-A 1"
FT                   /id="PRO_0000034386"
FT   PROPEP          190..221
FT                   /id="PRO_0000034387"
FT   CHAIN           222..363
FT                   /note="Trichocyst matrix protein T4-A 2"
FT                   /id="PRO_0000034388"
FT   COILED          85..119
FT                   /evidence="ECO:0000255"
FT   COILED          244..352
FT                   /evidence="ECO:0000255"
FT   CONFLICT        79..80
FT                   /note="VH -> LD (in Ref. 1; AAC47029)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="E -> Q (in Ref. 1; AAC47029)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   363 AA;  40769 MW;  7CECC42F37A1D705 CRC64;
     MARSLTILAI VFAVATARVT KSESPKEILA QVNKDSFGNS ILSVLQLQLA TGGPVGEIQI
     LLNNIASQLN GDQKKADKVH ESDTVAFEKI IADLEQEIAY HQTQIVALSN LRDSTTEALG
     EAEVEVRVVT SDIANNEKSF ADESATRQSQ HDTWVRKDAE HVDQMEAIDE ASKIVQHLQA
     GVAFAQLKSR FEKVQAKLME SKHALFKPLI NALTQLASKV DNKSIIKILE LLAQIRQQLV
     ASRASLLATE ERQAANWEVQ SSHLQEEHKR LVERKAFLEN SIVQFKVTIQ EAVEDLEDQT
     LFLEDAEDSL AIQERWAAEQ ESQYEAQTFE REQQLEVVER LQEVLTQKLS AASEFLQVRE
     EVF
 
 
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