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Lipoarabinomannan carrier protein LprG (27 kDa lipoprotein) (Antigen P27) (Lipoprotein LprG) (Triacylated glycolipid carrier LprG) (Triacylglyceride transfer protein LprG)

 LPRG_MYCTU              Reviewed;         236 AA.
P9WK45; L0T868; O32852; P0A5I8; P71679;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
30-AUG-2017, entry version 29.
RecName: Full=Lipoarabinomannan carrier protein LprG {ECO:0000305|PubMed:25232742, ECO:0000305|PubMed:25356793};
AltName: Full=27 kDa lipoprotein;
AltName: Full=Antigen P27 {ECO:0000303|PubMed:14998516};
AltName: Full=Lipoprotein LprG;
AltName: Full=Triacylated glycolipid carrier LprG {ECO:0000303|PubMed:20694006};
AltName: Full=Triacylglyceride transfer protein LprG {ECO:0000303|PubMed:26751071};
Flags: Precursor;
Name=lprG; Synonyms=lpp-27; OrderedLocusNames=Rv1411c;
ORFNames=MTCY21B4.28c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
DISRUPTION PHENOTYPE, AND VIRULENCE.
STRAIN=H37Rv;
PubMed=14998516; DOI=10.1016/j.micinf.2003.10.010;
Bigi F., Gioffre A., Klepp L., Santangelo M.P., Alito A., Caimi K.,
Meikle V., Zumarraga M., Taboga O., Romano M.I., Cataldi A.;
"The knockout of the lprG-Rv1410 operon produces strong attenuation of
Mycobacterium tuberculosis.";
Microbes Infect. 6:182-187(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15294983; DOI=10.4049/jimmunol.173.4.2660;
Gehring A.J., Dobos K.M., Belisle J.T., Harding C.V., Boom W.H.;
"Mycobacterium tuberculosis LprG (Rv1411c): a novel TLR-2 ligand that
inhibits human macrophage class II MHC antigen processing.";
J. Immunol. 173:2660-2668(2004).
[4]
FUNCTION.
STRAIN=H37Rv;
PubMed=18156250; DOI=10.1128/JB.01046-07;
Farrow M.F., Rubin E.J.;
"Function of a mycobacterial major facilitator superfamily pump
requires a membrane-associated lipoprotein.";
J. Bacteriol. 190:1783-1791(2008).
[5]
FUNCTION IN INFECTION, AND PROBABLE GLYCOSYLATION.
PubMed=18424702; DOI=10.4049/jimmunol.180.9.5833;
Sieling P.A., Hill P.J., Dobos K.M., Brookman K., Kuhlman A.M.,
Fabri M., Krutzik S.R., Rea T.H., Heaslip D.G., Belisle J.T.,
Modlin R.L.;
"Conserved mycobacterial lipoglycoproteins activate TLR2 but also
require glycosylation for MHC class II-restricted T cell activation.";
J. Immunol. 180:5833-5842(2008).
[6]
FUNCTION IN INFECTION.
STRAIN=H37Rv;
PubMed=19362712; DOI=10.1016/j.cellimm.2009.03.008;
Drage M.G., Pecora N.D., Hise A.G., Febbraio M., Silverstein R.L.,
Golenbock D.T., Boom W.H., Harding C.V.;
"TLR2 and its co-receptors determine responses of macrophages and
dendritic cells to lipoproteins of Mycobacterium tuberculosis.";
Cell. Immunol. 258:29-37(2009).
[7]
FUNCTION, AND GLYCOSYLATION.
STRAIN=ATCC 25177 / H37Ra, and H37Rv;
PubMed=21078852; DOI=10.1128/IAI.00806-10;
Lancioni C.L., Li Q., Thomas J.J., Ding X., Thiel B., Drage M.G.,
Pecora N.D., Ziady A.G., Shank S., Harding C.V., Boom W.H.,
Rojas R.E.;
"Mycobacterium tuberculosis lipoproteins directly regulate human
memory CD4(+) T cell activation via Toll-like receptors 1 and 2.";
Infect. Immun. 79:663-673(2011).
[8]
SUBCELLULAR LOCATION.
STRAIN=H37Rv;
PubMed=21364279; DOI=10.1172/JCI44261;
Prados-Rosales R., Baena A., Martinez L.R., Luque-Garcia J.,
Kalscheuer R., Veeraraghavan U., Camara C., Nosanchuk J.D.,
Besra G.S., Chen B., Jimenez J., Glatman-Freedman A., Jacobs W.R. Jr.,
Porcelli S.A., Casadevall A.;
"Mycobacteria release active membrane vesicles that modulate immune
responses in a TLR2-dependent manner in mice.";
J. Clin. Invest. 121:1471-1483(2011).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=H37Rv;
PubMed=21762531; DOI=10.1186/1471-2334-11-195;
Bianco M.V., Blanco F.C., Imperiale B., Forrellad M.A., Rocha R.V.,
Klepp L.I., Cataldi A.A., Morcillo N., Bigi F.;
"Role of P27 -P55 operon from Mycobacterium tuberculosis in the
resistance to toxic compounds.";
BMC Infect. Dis. 11:195-195(2011).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[11]
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=25041568; DOI=10.1111/cbdd.12365;
Ocampo M., Curtidor H., Vanegas M., Patarroyo M.A., Patarroyo M.E.;
"Specific interaction between Mycobacterium tuberculosis lipoprotein-
derived peptides and target cells inhibits mycobacterial entry in
vitro.";
Chem. Biol. Drug Des. 84:626-641(2014).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=H37Rv;
PubMed=25232742; DOI=10.1371/journal.ppat.1004376;
Gaur R.L., Ren K., Blumenthal A., Bhamidi S., Gibbs S., Jackson M.,
Zare R.N., Ehrt S., Ernst J.D., Banaei N.;
"LprG-mediated surface expression of lipoarabinomannan is essential
for virulence of Mycobacterium tuberculosis.";
PLoS Pathog. 10:E1004376-E1004376(2014).
[13]
ERRATUM.
PubMed=26650245; DOI=10.1371/journal.ppat.1005336;
Gaur R.L., Ren K., Blumenthal A., Bhamidi S., Gibbs S., Jackson M.,
Zare R.N., Ehrt S., Ernst J.D., Banaei N.;
"Correction: LprG-mediated surface expression of lipoarabinomannan is
essential for virulence of Mycobacterium tuberculosis.";
PLoS Pathog. 11:E1005336-E1005336(2015).
[14]
FUNCTION, LIPID-BINDING, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
VAL-91.
STRAIN=H37Rv;
PubMed=25356793; DOI=10.1371/journal.ppat.1004471;
Shukla S., Richardson E.T., Athman J.J., Shi L., Wearsch P.A.,
McDonald D., Banaei N., Boom W.H., Jackson M., Harding C.V.;
"Mycobacterium tuberculosis lipoprotein LprG binds lipoarabinomannan
and determines its cell envelope localization to control
phagolysosomal fusion.";
PLoS Pathog. 10:E1004471-E1004471(2014).
[15]
REVIEW.
PubMed=20234378; DOI=10.1038/nrmicro2321;
Harding C.V., Boom W.H.;
"Regulation of antigen presentation by Mycobacterium tuberculosis: a
role for Toll-like receptors.";
Nat. Rev. Microbiol. 8:296-307(2010).
[16] {ECO:0000244|PDB:3MH8, ECO:0000244|PDB:3MH9, ECO:0000244|PDB:3MHA}
X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 28-236, FUNCTION, DOMAIN,
LIPID-BINDING, POST-TRANSLATIONAL MODIFICATION, AND MUTAGENESIS OF
VAL-91.
STRAIN=H37Rv;
PubMed=20694006; DOI=10.1038/nsmb.1869;
Drage M.G., Tsai H.C., Pecora N.D., Cheng T.Y., Arida A.R., Shukla S.,
Rojas R.E., Seshadri C., Moody D.B., Boom W.H., Sacchettini J.C.,
Harding C.V.;
"Mycobacterium tuberculosis lipoprotein LprG (Rv1411c) binds
triacylated glycolipid agonists of Toll-like receptor 2.";
Nat. Struct. Mol. Biol. 17:1088-1095(2010).
[17] {ECO:0000244|PDB:4ZRA}
X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 36-231 IN COMPLEX WITH
TRIACYLGLYCERIDE, FUNCTION, DOMAIN, TRIACYLGLYCERIDE-BINDING,
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF VAL-91.
STRAIN=H37Rv;
PubMed=26751071; DOI=10.1371/journal.ppat.1005351;
Martinot A.J., Farrow M., Bai L., Layre E., Cheng T.Y., Tsai J.H.,
Iqbal J., Annand J.W., Sullivan Z.A., Hussain M.M., Sacchettini J.,
Moody D.B., Seeliger J.C., Rubin E.J.;
"Mycobacterial metabolic syndrome: LprG and Rv1410 regulate
triacylglyceride levels, growth rate and virulence in Mycobacterium
tuberculosis.";
PLoS Pathog. 12:E1005351-E1005351(2016).
-!- FUNCTION: Probably helps membrane protein Rv1410c (P55) transport
triacylglycerides (TAG) across the inner cell membrane into the
periplasm; TAG probably regulates lipid metabolism and growth
regulation (PubMed:26751071). Binds TAG and transfers it between
lipid bilayers, probably to the outer membrane in vivo
(PubMed:26751071). Binds di- and triacylated phosphatidyl-myo-
inositol mannosides (PIMs), and glycolipid lipoglycan modulins
lipoarabinomannan (LAM) and lipomannan (LM), facilitating their
recognition by TLR2 (PubMed:20694006, PubMed:25356793). Binds LM >
PIM6 > ManLAM > PI-LAM > PIM2 (mannose-capped LAM and phospho-myo-
inositol-capped LAM, E.coli expressed without acyl-groups);
deacylated LM and LAM also bind to this protein via their mannose
moieties, showing LprG has at least 2 different ways to bind
glycolipids (PubMed:25356793). Binds triacylglycerides (TAG) in
the same cavity, is able to transfer TAG between lipid bilayers
(PubMed:26751071). Overexpression of LprG and Rv1410c leads to
increased levels of TAG in the culture medium (PubMed:26751071).
Required for Rv1410c-mediated export of drugs (PubMed:18156250,
PubMed:21762531). Required, probably with Rv1410c, for normal
surface localization of LAM (PubMed:25232742).
{ECO:0000269|PubMed:18156250, ECO:0000269|PubMed:20694006,
ECO:0000269|PubMed:21762531, ECO:0000269|PubMed:25232742,
ECO:0000269|PubMed:25356793, ECO:0000269|PubMed:26751071}.
-!- FUNCTION: A host TLR2 agonist (toll-like receptor), shown
experimentally for human and mouse (PubMed:19362712). Inhibits
primary human macrophage MHC-II Ag processing via TLR2
(PubMed:15294983). Both lipidated and nonlipidated protein act as
TLR2 agonists in antigen-presenting cells, although lipidated
protein is more efficient (PubMed:20694006). In resting human CD4+
T-cells lipidated but not nonlipidated protein is a costimulatory
ligand (with anti-CD3 and anti-CD28) for T-cell proliferation and
IFN-gamma and IL-2 production, leading to increased expression of
early T-cell activation markers, TLR2 and NFKB3 phosphorylation
(PubMed:21078852). Human CD4+ T-cells use TLR1/TLR2 heterodimers
to respond to this and probably other mycobacterial lipoproteins
(PubMed:21078852). Able to stimulate proliferation of CD4+ T-cells
derived from a human leprosy patient following protein
processing/presentation by MHC class II molecules in peripheral
blood mononuclear cells (PubMed:18424702). Requires both host TLR1
and TLR2 as coreceptors to elicit host response in mouse, although
TLR6 may play a redundant role, has a partial requirement for CD14
as an accessory receptor (PubMed:19362712).
{ECO:0000269|PubMed:15294983, ECO:0000269|PubMed:18424702,
ECO:0000269|PubMed:19362712, ECO:0000269|PubMed:20694006,
ECO:0000269|PubMed:21078852}.
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
ProRule:PRU00303, ECO:0000269|PubMed:21762531, ECO:0000305};
Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Secreted,
cell wall {ECO:0000269|PubMed:21762531}. Secreted
{ECO:0000269|PubMed:21762531}. Cell surface
{ECO:0000269|PubMed:25041568}. Note=Present in extracytoplasmic
vesicles (PubMed:21364279). Immunoelectron microscopy indicates
this protein is close to the cell surface (PubMed:25041568).
{ECO:0000269|PubMed:21364279, ECO:0000269|PubMed:25041568}.
-!- DOMAIN: Forms a U-shaped beta-half-barrel with a small hydrophobic
cavity (1500 Angstroms (3)) which holds a triacylated PIM in 1
crystal structure; the 3 acyl chains are within the cavity while
the sugar moieties bind to the protein surface (PubMed:20694006).
In the structure bound to triacylglycerides (TAG) 2 of the 3 acyl
chains are buried in the cavity, the third is solvent exposed
(PubMed:26751071). A flexible lid region may move to accommodate
different TAG molecules (PubMed:26751071). Fragments of the mature
protein (residues 81-100, 141-160 and 218-236) prevent uptake of
M.tuberculosis by a human macrophage-like cell line; lesser
effects are seen on bacterial uptake by a human lung epithelial
cell line (PubMed:25041568). {ECO:0000269|PubMed:20694006,
ECO:0000269|PubMed:25041568, ECO:0000269|PubMed:26751071}.
-!- PTM: Modified by Lgt on Cys-27 with an S-linked diacylglyceral,
signal peptide is removed by LspA, Cys-27 is further modifed with
a fatty acid on its amino group by Lnt yielding a triacylated
protein (Probable). Probably glycosylated, which is required for
T-cell activation (PubMed:18424702).
{ECO:0000250|UniProtKB:P9WK47, ECO:0000269|PubMed:18424702,
ECO:0000305|PubMed:20694006}.
-!- DISRUPTION PHENOTYPE: A single deletion mutant leads to loss of
expression of efflux pump Rv1410c due to polar effects; in
infected BALB/c mice 1.5 and 2.5 log decrease in bacterial load 15
and 35 days after infection (PubMed:14998516). The single mutant
increases sensitivity to malachite green, sodium dodecyl sulfate
(SDS), isoniazid, ethambutal and ethidium bromide, alters the
permeability of the cell wall; both genes of the operon are
required to fully restore the phenotypes (PubMed:21762531). Single
deletion mutant (probably without Rv1410c) has decreased surface-
exposed glycolipid lipoarabinomannan (LAM), although cellular LAM,
LM and PIM content is normal (PubMed:25232742, PubMed:25356793).
Disruption of either Rv1410c or the lrpG-Rv1410c operon leads to
increased levels of many triacylglyceride (TAG) alkylforms; up to
100-fold increase depending on the exact TAG form
(PubMed:26751071). It also forms smaller colonies on agar
(PubMed:25232742). Loss of surface LAM has several consequences;
bacteria enter mouse macrophages with reduced efficiency and block
mouse macrophage phagosome-lysosome fusion less efficiently than
wild-type (PubMed:25232742). Reduced efficiency of mouse
macrophage phagosome-lysosome fusion was seen in another study
(PubMed:25356793). C57BL/6 mice infected with mutant bacteria have
10-fold less bacterial burden after 10 days and about 2700-fold
less burden after 70 days; attenuation of mutant is not rescued in
macrophages impaired for reactive oxygen or nitrogen generation
(disruption of Ncf1 or iNOS) (PubMed:25232742).
{ECO:0000269|PubMed:14998516, ECO:0000269|PubMed:21762531,
ECO:0000269|PubMed:25232742, ECO:0000269|PubMed:25356793,
ECO:0000269|PubMed:26751071}.
-!- MISCELLANEOUS: Bacterial LAM blocks host cell phagosome-lysosome
fusion and is one way in which M.tuberculosis evades the host
immune system. {ECO:0000305|PubMed:25232742,
ECO:0000305|PubMed:25356793}.
-!- MISCELLANEOUS: Triacylglycerides accumulate in lipid droplets in
the cytoplasm of M.tuberculosis stationary phase and dormant
bacteria, and are used as an energy source during starvation
(PubMed:26751071). {ECO:0000305|PubMed:26751071}.
-!- SIMILARITY: Belongs to the LppX/LprAFG lipoprotein family.
{ECO:0000305}.
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EMBL; AL123456; CCP44170.1; -; Genomic_DNA.
PIR; H70901; H70901.
RefSeq; NP_215927.1; NC_000962.3.
RefSeq; WP_003407315.1; NZ_KK339370.1.
PDB; 3MH8; X-ray; 2.00 A; A/B=36-231.
PDB; 3MH9; X-ray; 1.79 A; A/C=28-236.
PDB; 3MHA; X-ray; 1.85 A; A/B=36-231.
PDB; 4ZRA; X-ray; 1.83 A; A/C=36-231.
PDBsum; 3MH8; -.
PDBsum; 3MH9; -.
PDBsum; 3MHA; -.
PDBsum; 4ZRA; -.
ProteinModelPortal; P9WK45; -.
SMR; P9WK45; -.
STRING; 83332.Rv1411c; -.
PaxDb; P9WK45; -.
EnsemblBacteria; CCP44170; CCP44170; Rv1411c.
GeneID; 886700; -.
KEGG; mtu:Rv1411c; -.
TubercuList; Rv1411c; -.
eggNOG; ENOG41064B9; Bacteria.
eggNOG; ENOG4112A10; LUCA.
KO; K14954; -.
OMA; WGEPVTV; -.
PhylomeDB; P9WK45; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0097691; C:bacterial extracellular vesicle; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0051861; F:glycolipid binding; IDA:MTBBASE.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IMP:MTBBASE.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
CDD; cd16334; LppX-like; 1.
InterPro; IPR029046; LolA/LolB/LppX.
InterPro; IPR009830; LppX/LprAFG.
Pfam; PF07161; LppX_LprAFG; 1.
ProDom; PD017293; DUF1396; 1.
SUPFAM; SSF89392; SSF89392; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Cell inner membrane;
Cell membrane; Cell wall; Complete proteome; Glycoprotein;
Lipid transport; Lipid-binding; Lipoprotein; Membrane; Palmitate;
Reference proteome; Secreted; Signal; Transport; Virulence.
SIGNAL 1 26 {ECO:0000255|PROSITE-ProRule:PRU00303}.
CHAIN 27 236 Lipoarabinomannan carrier protein LprG.
{ECO:0000255|PROSITE-ProRule:PRU00303}.
/FTId=PRO_0000018146.
REGION 81 100 Prevents bacterial uptake by a human
macrophage-like cell line.
{ECO:0000269|PubMed:25041568}.
REGION 141 160 Prevents bacterial uptake by a human
macrophage-like cell line.
{ECO:0000269|PubMed:25041568}.
REGION 218 236 Prevents bacterial uptake by a human
macrophage-like cell line.
{ECO:0000269|PubMed:25041568}.
LIPID 27 27 N-palmitoyl cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303,
ECO:0000305|PubMed:20694006}.
LIPID 27 27 S-diacylglycerol cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303,
ECO:0000305|PubMed:20694006}.
MUTAGEN 91 91 V->W: Decreased TLR2 agonist activity,
cannot acquire lipid from mycobacterial
extracts, cavity entrance and size
decrease. Binds PIM6, LM and ManLAM 10-
100-fold less well than wild-type, binds
de-acylated LM and ManLAM as well as
wild-type. Decreased ability to transfer
triacylglyceride between lipid bilayers.
{ECO:0000269|PubMed:20694006,
ECO:0000269|PubMed:25356793,
ECO:0000269|PubMed:26751071}.
HELIX 41 53 {ECO:0000244|PDB:3MH9}.
STRAND 57 66 {ECO:0000244|PDB:3MH9}.
STRAND 73 81 {ECO:0000244|PDB:3MH9}.
TURN 82 85 {ECO:0000244|PDB:3MH9}.
STRAND 86 95 {ECO:0000244|PDB:3MH9}.
STRAND 98 107 {ECO:0000244|PDB:3MH9}.
STRAND 110 116 {ECO:0000244|PDB:3MH9}.
STRAND 119 125 {ECO:0000244|PDB:3MH9}.
HELIX 126 128 {ECO:0000244|PDB:3MH9}.
HELIX 132 135 {ECO:0000244|PDB:3MH9}.
TURN 138 140 {ECO:0000244|PDB:3MH9}.
HELIX 142 147 {ECO:0000244|PDB:3MH9}.
STRAND 149 160 {ECO:0000244|PDB:3MH9}.
STRAND 163 172 {ECO:0000244|PDB:3MH9}.
HELIX 174 180 {ECO:0000244|PDB:3MH9}.
HELIX 182 184 {ECO:0000244|PDB:3MH9}.
STRAND 190 199 {ECO:0000244|PDB:3MH9}.
STRAND 204 212 {ECO:0000244|PDB:3MH9}.
STRAND 215 223 {ECO:0000244|PDB:3MH9}.
SEQUENCE 236 AA; 24548 MW; 2591DAE6D2E2DC22 CRC64;
MRTPRRHCRR IAVLAAVSIA ATVVAGCSSG SKPSGGPLPD AKPLVEEATA QTKALKSAHM
VLTVNGKIPG LSLKTLSGDL TTNPTAATGN VKLTLGGSDI DADFVVFDGI LYATLTPNQW
SDFGPAADIY DPAQVLNPDT GLANVLANFA DAKAEGRDTI NGQNTIRISG KVSAQAVNQI
APPFNATQPV PATVWIQETG DHQLAQAQLD RGSGNSVQMT LSKWGEKVQV TKPPVS


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EIAAB27355 Chicken,Gallus gallus,Non-specific lipid-transfer protein,NSL-TP,Propanoyl-CoA C-acyltransferase,SCP2,SCP-2,SCP-chi,SCPX,SCP-X,Sterol carrier protein 2,Sterol carrier protein X
EIAAB37563 Calcium-binding mitochondrial carrier protein SCaMC-2,Mcsc,Mitochondrial ATP-Mg_Pi carrier protein,Pcscl,Peroxisomal Ca(2+)-dependent solute carrier-like protein,Rat,Rattus norvegicus,Scamc2,Slc25a25,
orb81946 Lipoprotein(a)-Lp(a) protein Lipoprotein(a)-Lp(a) is a purified lipoprotein. For research use only. 100
EIAAB37565 APC3,Calcium-binding mitochondrial carrier protein SCaMC-2,Homo sapiens,Human,KIAA1896,MCSC3,Mitochondrial ATP-Mg_Pi carrier protein 3,Mitochondrial Ca(2+)-dependent solute carrier protein 3,SCAMC2,SL
EIAAB37568 APC2,Calcium-binding mitochondrial carrier protein SCaMC-3,Homo sapiens,Human,MCSC2,Mitochondrial ATP-Mg_Pi carrier protein 2,Mitochondrial Ca(2+)-dependent solute carrier protein 2,SCAMC3,SLC25A23,Sm
EIAAB37561 APC1,Calcium-binding mitochondrial carrier protein SCaMC-1,Homo sapiens,Human,MCSC1,Mitochondrial ATP-Mg_Pi carrier protein 1,Mitochondrial Ca(2+)-dependent solute carrier protein 1,SCAMC1,SLC25A24,Sm
orb82281 Lipoprotein, Low Density protein Lipoprotein, Low Density (LDL) is a purified lipoprotein. For research use only. 1 mg
orb81991 Human LDL protein Lipoprotein, Low Density (LDL) is a purified lipoprotein. For research use only. 5 mg
EIAAB37566 Calcium-binding mitochondrial carrier protein SCaMC-2,Kiaa1896,Mouse,Mus musculus,Scamc2,Slc25a25,Small calcium-binding mitochondrial carrier protein 2,Solute carrier family 25 member 25
EIAAB37567 Calcium-binding mitochondrial carrier protein SCaMC-3,Mouse,Mus musculus,Scamc3,Slc25a23,Small calcium-binding mitochondrial carrier protein 3,Solute carrier family 25 member 23
EIAAB37560 Calcium-binding mitochondrial carrier protein SCaMC-1,Mouse,Mus musculus,Scamc1,Slc25a24,Small calcium-binding mitochondrial carrier protein 1,Solute carrier family 25 member 24
EIAAB37564 Bos taurus,Bovine,Calcium-binding mitochondrial carrier protein SCaMC-2,SCAMC2,SLC25A25,Small calcium-binding mitochondrial carrier protein 2,Solute carrier family 25 member 25
EIAAB37562 Bos taurus,Bovine,Calcium-binding mitochondrial carrier protein SCaMC-1,SCAMC1,SLC25A24,Small calcium-binding mitochondrial carrier protein 1,Solute carrier family 25 member 24
orb82274 Lipoprotein, High Density protein Lipoprotein, High Density (HDL) (d 1.063-1.210) is a purified lipoprotein. For research use only. 1 mg
EIAAB08043 Aralar1,Calcium-binding mitochondrial carrier protein Aralar1,Mitochondrial aspartate glutamate carrier 1,Mouse,Mus musculus,Slc25a12,Solute carrier family 25 member 12
EIAAB08046 Aralar2,Calcium-binding mitochondrial carrier protein Aralar2,Citrin,Mitochondrial aspartate glutamate carrier 2,Mouse,Mus musculus,Slc25a13,Solute carrier family 25 member 13
EIAAB08044 ARALAR1,Calcium-binding mitochondrial carrier protein Aralar1,Homo sapiens,Human,Mitochondrial aspartate glutamate carrier 1,SLC25A12,Solute carrier family 25 member 12
EIAAB08045 ARALAR2,Calcium-binding mitochondrial carrier protein Aralar2,Citrin,Homo sapiens,Human,Mitochondrial aspartate glutamate carrier 2,SLC25A13,Solute carrier family 25 member 13
EIAAB36770 BMSC-MCP,Bone marrow stromal cell mitochondrial carrier protein,Homo sapiens,HuBMSC-MCP,Human,Protein PNC1,SLC25A33,Solute carrier family 25 member 33
EIAAB44652 Citrate transport protein,CTP,Homo sapiens,Human,SLC20A3,SLC25A1,Solute carrier family 25 member 1,Tricarboxylate carrier protein,Tricarboxylate transport protein, mitochondrial


 

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