ID   KM11C_LEIIN             Reviewed;          92 AA.
AC   Q25298;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Kinetoplastid membrane protein 11C;
GN   Name=KMP-11C;
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671 {ECO:0000312|EMBL:CAA64883.1};
RN   [1] {ECO:0000312|EMBL:CAA64883.1}
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; X95627; CAA64883.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q25298; -.
DR   SMR; Q25298; -.
DR   VEuPathDB; TriTrypDB:LINF_350027500; -.
DR   eggNOG; ENOG502S6FH; Eukaryota.
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 11C"
FT                   /id="PRO_0000205713"
SQ   SEQUENCE   92 AA;  11263 MW;  C73700CC87B10CE7 CRC64;
     MATTYEEFSA KLDRLDEEFN RKMQEQNAKF FADKPDESTL SPEMKEHYEK FERMIREHTE
     KFNKKMHEHS EHFKQKFAEL LEQQKAAQYP SK