ID   DRC4_TRYBR              Reviewed;         453 AA.
AC   O15697;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Trypanin;
DE   AltName: Full=T lymphocyte-triggering factor;
DE            Short=TLTF;
OS   Trypanosoma brucei rhodesiense.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=31286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9236195; DOI=10.1084/jem.186.3.433;
RA   Vaidya T., Bakhiet M., Hill K.L., Olsson T., Kristensson K., Donelson J.E.;
RT   "The gene for a T lymphocyte triggering factor from African trypanosomes.";
RL   J. Exp. Med. 186:433-438(1997).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10969087; DOI=10.1074/jbc.m006907200;
RA   Hill K.L., Hutchings N.R., Grandgenett P.M., Donelson J.E.;
RT   "T lymphocyte-triggering factor of African trypanosomes is associated with
RT   the flagellar fraction of the cytoskeleton and represents a new family of
RT   proteins that are present in several divergent eukaryotes.";
RL   J. Biol. Chem. 275:39369-39378(2000).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11864997; DOI=10.1083/jcb.200201036;
RA   Hutchings N.R., Donelson J.E., Hill K.L.;
RT   "Trypanin is a cytoskeletal linker protein and is required for cell
RT   motility in African trypanosomes.";
RL   J. Cell Biol. 156:867-877(2002).
RN   [4]
RP   FUNCTION.
RX   PubMed=16607017; DOI=10.1128/ec.5.4.696-711.2006;
RA   Ralston K.S., Lerner A.G., Diener D.R., Hill K.L.;
RT   "Flagellar motility contributes to cytokinesis in Trypanosoma brucei and is
RT   modulated by an evolutionarily conserved dynein regulatory system.";
RL   Eukaryot. Cell 5:696-711(2006).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17009870; DOI=10.1371/journal.ppat.0020101;
RA   Ralston K.S., Hill K.L.;
RT   "Trypanin, a component of the flagellar dynein regulatory complex, is
RT   essential in bloodstream form African trypanosomes.";
RL   PLoS Pathog. 2:873-882(2006).
CC   -!- FUNCTION: Cytoskeletal linker that plays a central role in the
CC       flagellum cell motility. Required for directional cell motility. Plays
CC       a role as part of a dynein regulatory system that regulates flagellar
CC       beat in response to signals from the central pair apparatus and radial
CC       spokes in procyclic cells. Also plays an essential role in the
CC       bloodstream form of the trypanosomes as its silencing is lethal for the
CC       circulating form. {ECO:0000269|PubMed:11864997,
CC       ECO:0000269|PubMed:16607017, ECO:0000269|PubMed:17009870}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell
CC       projection, cilium, flagellum. Note=Associated with the cytoskeleton.
CC       Localized to the site of attachment of the flagellum to the
CC       subpellicular cytoskeleton. Also localized in the flagellum of the
CC       bloodstream form trypanosomes.
CC   -!- MISCELLANEOUS: Procyclic parasite mutants lacking trypanin exhibit a
CC       motility defect indicative of abnormal dynein regulation, but have an
CC       actively beating flagellum and are able to spin and tumble in place.
CC       However, bloodstream form mutants lacking trypanin exhibit a severe
CC       growth defect and are not viable. They revealed a failure of
CC       cytokinesis.
CC   -!- SIMILARITY: Belongs to the DRC4 family. {ECO:0000305}.
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DR   EMBL; AF012853; AAB81499.1; -; mRNA.
DR   AlphaFoldDB; O15697; -.
DR   SMR; O15697; -.
DR   GO; GO:0005929; C:cilium; IDA:GeneDB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IMP:CACAO.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0060285; P:cilium-dependent cell motility; IMP:GeneDB.
DR   GO; GO:0051179; P:localization; IEA:UniProt.
DR   InterPro; IPR039308; GAS8.
DR   InterPro; IPR025593; GAS8_dom.
DR   PANTHER; PTHR31543; PTHR31543; 1.
DR   Pfam; PF13851; GAS; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Flagellum;
KW   Microtubule.
FT   CHAIN           1..453
FT                   /note="Trypanin"
FT                   /id="PRO_0000220379"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          60..156
FT                   /evidence="ECO:0000255"
FT   COILED          185..377
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   453 AA;  53954 MW;  842A5E2AAA384215 CRC64;
     MPPRTAAERG GRRKSVKAPP PVDPLVELTT LESVHDALAK AERLRNYFQV ERDKVNDFWT
     ITKGEVETYR NRLFNAEASI EELERSHQVE MKVYKQRVRH LIYERKKKAQ ACQDESDRLL
     REAEDRHLQR MNEIQAKLQQ QDQQLRAAAA DHEMNVYEKR DSHSYMVTVT KTQSHEKELA
     RLQVSCEAKL KVLRDELELR RRAEIHEIEE RKNEHINALI KQHEEKFHEM KTYYNQITTN
     NLEIIHSLKE EIAQMKQNDE HNETLMYDID RENQNLVAPL EEAQREVAEL QQKRKQNEQN
     KRGLEVTRVK LRSLREEIRR QREEHQALEE RYACVHRERE ELKGKFESAL RQAVMVVEER
     NEVLQQKLIE SHALVEERDV QLEGVLRAMN LEPKTLELIA TEVDEWLQRK NQLIKDLHFE
     LKKGEKLYSA TLLEMERRCQ TANIASLPRS NFE