KM11B_LEIIN
ID KM11B_LEIIN Reviewed; 92 AA.
AC Q25297;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Kinetoplastid membrane protein 11B;
GN Name=KMP-11B;
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671 {ECO:0000312|EMBL:CAA64882.1};
RN [1] {ECO:0000312|EMBL:CAA64882.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LEM 78 / MON-1;
RX PubMed=9024210; DOI=10.1006/expr.1996.4120;
RA Berberich C., Requena J.M., Alonso C.;
RT "Cloning of genes, expression and antigenicity analysis of the Leishmania
RT infantum KMP-11 protein.";
RL Exp. Parasitol. 85:105-108(1997).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9804960; DOI=10.1016/s0167-4781(98)00176-6;
RA Berberich C., Machado G., Morales G., Carrillo G., Jimenez-Ruiz A.,
RA Alonso C.;
RT "The expression of the Leishmania infantum KMP-11 protein is
RT developmentally regulated and stage specific.";
RL Biochim. Biophys. Acta 1442:230-237(1998).
RN [3] {ECO:0000305}
RP SUBUNIT, AND SECONDARY STRUCTURE PREDICTION.
RX PubMed=10095795; DOI=10.1046/j.1432-1327.1999.00217.x;
RA Fuertes M.A., Berberich C., Lozano R.M., Gimenez-Gallego G., Alonso C.;
RT "Folding stability of the kinetoplastid membrane protein-11 (KMP-11) from
RT Leishmania infantum.";
RL Eur. J. Biochem. 260:559-567(1999).
RN [4] {ECO:0000305}
RP CALCIUM-BINDING DATA.
RX PubMed=11191218; DOI=10.1007/s007750000175;
RA Fuertes M.A., Perez J.M., Soto M., Lopez M.C., Alonso C.;
RT "Calcium-induced conformational changes in Leishmania infantum
RT kinetoplastid membrane protein-11.";
RL J. Biol. Inorg. Chem. 6:107-117(2001).
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.
CC {ECO:0000250|UniProtKB:Q9U6Z1, ECO:0000269|PubMed:9024210}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10095795}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9804960}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:9804960}. Note=Associated with microtubules.
CC Associated with the flagellum and flagellar pocket.
CC -!- DEVELOPMENTAL STAGE: Expressed abundantly in logarithmic phase
CC promastigotes, and to a lesser extent in stationary phase promastigotes
CC and amastigotes. {ECO:0000269|PubMed:9804960}.
CC -!- MISCELLANEOUS: Binds calcium. {ECO:0000269|PubMed:11191218}.
CC -!- SIMILARITY: Belongs to the KMP-11 family. {ECO:0000305}.
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DR EMBL; X95626; CAA64882.1; -; Genomic_DNA.
DR AlphaFoldDB; Q25297; -.
DR SMR; Q25297; -.
DR VEuPathDB; TriTrypDB:LINF_350027500; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
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 Calcium; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Flagellum;
KW Microtubule.
FT CHAIN 1..92
FT /note="Kinetoplastid membrane protein 11B"
FT /id="PRO_0000205712"
SQ SEQUENCE 92 AA; 11177 MW; 78CA90CC923FA7D4 CRC64;
MATTYEEFSA KLDRLGEEFN RKMQEQNAKF FADKPDESTL SPEMKEHYEK FERMIKEHTE
KFNKKMHEHS EHFKQKFAEL LEQQKAAQYP SK