ID   KM11_LEIDO              Reviewed;          92 AA.
AC   Q36736;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Kinetoplastid membrane protein 11;
DE            Short=KMP-11;
DE   AltName: Full=Lipophosphoglycan-associated protein;
DE            Short=LPGAP;
GN   Name=KMP-11;
OS   Leishmania donovani.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ld3;
RX   PubMed=7826347; DOI=10.1042/bj3050315;
RA   Jardim A., Hanson S., Ullman B., McCubbin W.D., Kay C.M., Olafson R.W.;
RT   "Cloning and structure-function analysis of the Leishmania donovani
RT   kinetoplastid membrane protein-11.";
RL   Biochem. J. 305:315-320(1995).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 12-27 AND 30-92, GLYCOSYLATION, METHYLATION AT ARG-45,
RP   AND DEVELOPMENTAL STAGE.
RC   STRAIN=Ld3;
RX   PubMed=7826346; DOI=10.1042/bj3050307;
RA   Jardim A., Funk V., Caprioli R.M., Olafson R.W.;
RT   "Isolation and structural characterization of the Leishmania donovani
RT   kinetoplastid membrane protein-11, a major immunoreactive membrane
RT   glycoprotein.";
RL   Biochem. J. 305:307-313(1995).
RN   [3]
RP   CHARACTERIZATION.
RC   STRAIN=Ld3;
RX   PubMed=1940354;
RA   Jardim A., Tolson D.L., Turco S.J., Pearson T.W., Olafson R.W.;
RT   "The Leishmania donovani lipophosphoglycan T lymphocyte-reactive component
RT   is a tightly associated protein complex.";
RL   J. Immunol. 147:3538-3544(1991).
RN   [4] {ECO:0000305}
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=7927770; DOI=10.1128/iai.62.11.4893-4899.1994;
RA   Tolson D.L., Jardim A., Schnur L.F., Stebeck C., Tuckey C., Beecroft R.P.,
RA   Teh H.-S., Olafson R.W., Pearson T.W.;
RT   "The kinetoplastid membrane protein 11 of Leishmania donovani and African
RT   trypanosomes is a potent stimulator of T-lymphocyte proliferation.";
RL   Infect. Immun. 62:4893-4899(1994).
RN   [5] {ECO:0000305}
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).
RN   [6] {ECO:0000305}
RP   FUNCTION.
RC   STRAIN=AG83;
RX   PubMed=9645879; DOI=10.2307/3284745;
RA   Mukhopadhyay S., Sen P., Majumder H.K., Roy S.;
RT   "Reduced expression of lipophosphoglycan (LPG) and kinetoplastid membrane
RT   protein (KMP)-11 in Leishmania donovani promastigotes in axenic culture.";
RL   J. Parasitol. 84:644-647(1998).
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       Strongly stimulates T-cell proliferation and is thought to play a role
CC       in the immunology of leishmaniasis. {ECO:0000269|PubMed:7927770,
CC       ECO:0000269|PubMed:9645879}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q25297}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:7630374}. Note=Associated with microtubules.
CC   -!- DEVELOPMENTAL STAGE: Present in both promastigotes and amastigotes.
CC       {ECO:0000269|PubMed:7826346, ECO:0000269|PubMed:7927770}.
CC   -!- PTM: A minor in vivo processed fragment (IVP) also exists, probably as
CC       a result of proteolysis. {ECO:0000269|PubMed:7826346}.
CC   -!- PTM: Probably O-glycosylated. Contains equimolar amounts of
CC       galactosamine, galactose, glucose and mannose.
CC       {ECO:0000269|PubMed:7826346}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7826346}.
CC   -!- SIMILARITY: Belongs to the KMP-11 family. {ECO:0000305}.
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DR   EMBL; S77039; AAB33127.2; -; Genomic_DNA.
DR   PIR; S53443; S53443.
DR   AlphaFoldDB; Q36736; -.
DR   SMR; Q36736; -.
DR   iPTMnet; Q36736; -.
DR   VEuPathDB; TriTrypDB:LdBPK_352260.1; -.
DR   VEuPathDB; TriTrypDB:LdCL_350027500; -.
DR   VEuPathDB; TriTrypDB:LDHU3_35.2890; -.
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: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   GO; GO:0042098; P:T cell proliferation; IDA:UniProtKB.
DR   InterPro; IPR004132; KMP11.
DR   Pfam; PF03037; KMP11; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycoprotein;
KW   Methylation; Microtubule.
FT   CHAIN           1..92
FT                   /note="Kinetoplastid membrane protein 11"
FT                   /id="PRO_0000205711"
FT   MOD_RES         45
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000269|PubMed:7826346"
FT   CONFLICT        17
FT                   /note="Q -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   92 AA;  11262 MW;  1041C82DC4B7799C CRC64;
     MATTYEEFSA KLDRLDQEFN RKMQEQNAKF FADKPDESTL SPEMREHYEK FERMIKEHTE
     KFNKKMHEHS EHFKQKFAEL LEQQKAAQYP SK