KM11_TRYBB
ID KM11_TRYBB Reviewed; 92 AA.
AC P69300; Q26773;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Kinetoplastid membrane protein 11;
DE Short=KMP-11;
GN Name=KMP-11/1;
GN and
GN Name=KMP-11/2;
GN and
GN Name=KMP-11/3;
GN and
GN Name=KMP-11/4;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9566527; DOI=10.1016/s0166-6851(97)00229-6;
RA Bridge M.A., Zhou Q., Koop B.F., Pearson T.W.;
RT "Cloning and characterization of the kinetoplastid membrane protein-11 gene
RT locus of Trypanosoma brucei.";
RL Mol. Biochem. Parasitol. 91:359-363(1998).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=7630374; DOI=10.1016/0166-6851(95)00022-s;
RA Stebeck C.E., Beecroft R.P., Singh B.N., Jardim A., Olafson R.W.,
RA Tuckey C., Prenevost K.D., Pearson T.W.;
RT "Kinetoplastid membrane protein-11 (KMP-11) is differentially expressed
RT during the life cycle of African trypanosomes and is found in a wide
RT variety of kinetoplastid parasites.";
RL Mol. Biochem. Parasitol. 71:1-13(1995).
CC -!- FUNCTION: May be involved in the regulation of the cytoskeleton through
CC interaction with the subpellicular microtubules. May be involved in
CC parasite mobility and attachment to the surface of the host cell.
CC Behaves as a strong immunogen during infection (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:7630374}. Note=Associated with microtubules.
CC -!- MISCELLANEOUS: There are four copies of the KMP-11 gene in T.b.brucei.
CC -!- SIMILARITY: Belongs to the KMP-11 family. {ECO:0000305}.
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DR EMBL; AF028726; AAC38990.1; -; Genomic_DNA.
DR EMBL; AF028726; AAC38991.1; -; Genomic_DNA.
DR EMBL; AF028726; AAC38992.1; -; Genomic_DNA.
DR EMBL; AF028726; AAC38993.1; -; Genomic_DNA.
DR PDB; 5Y70; NMR; -; A=1-92.
DR PDBsum; 5Y70; -.
DR AlphaFoldDB; P69300; -.
DR SMR; P69300; -.
DR OMA; HSEHFKH; -.
DR GO; GO:0005930; C:axoneme; IDA:GeneDB.
DR GO; GO:0051286; C:cell tip; IDA:GeneDB.
DR GO; GO:0036064; C:ciliary basal body; IDA:GeneDB.
DR GO; GO:0005929; C:cilium; IDA:GeneDB.
DR GO; GO:0005856; C:cytoskeleton; IDA:GeneDB.
DR GO; GO:0120119; C:flagellum attachment zone; IDA:GeneDB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0032053; P:ciliary basal body organization; IMP:GeneDB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
DR InterPro; IPR004132; KMP11.
DR Pfam; PF03037; KMP11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Microtubule.
FT CHAIN 1..92
FT /note="Kinetoplastid membrane protein 11"
FT /id="PRO_0000205715"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:5Y70"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:5Y70"
FT HELIX 18..23
FT /evidence="ECO:0007829|PDB:5Y70"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:5Y70"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:5Y70"
FT HELIX 43..47
FT /evidence="ECO:0007829|PDB:5Y70"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:5Y70"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:5Y70"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:5Y70"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:5Y70"
FT HELIX 70..87
FT /evidence="ECO:0007829|PDB:5Y70"
SQ SEQUENCE 92 AA; 11077 MW; B50328C81A770E4C CRC64;
MATTYEEFAA KLDRLDAEFA KKMEEQNKRF FADKPDEATL SPEMKEHYEK FEKMIQEHTD
KFNKKMREHS EHFKAKFAEL LEQQKNAQFP GK
