ID G1M1Z4_AILME Unreviewed; 496 AA.
AC G1M1Z4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Phospholipid transfer protein {ECO:0000313|Ensembl:ENSAMEP00000013355.2};
GN Name=PLTP {ECO:0000313|Ensembl:ENSAMEP00000013355.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000013355.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000013355.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000013355.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000256|ARBA:ARBA00007292}.
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DR RefSeq; XP_002928111.1; XM_002928065.3.
DR AlphaFoldDB; G1M1Z4; -.
DR STRING; 9646.ENSAMEP00000013355; -.
DR Ensembl; ENSAMET00000013913.2; ENSAMEP00000013355.2; ENSAMEG00000012654.2.
DR GeneID; 100477355; -.
DR KEGG; aml:100477355; -.
DR CTD; 5360; -.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01100000263545; -.
DR HOGENOM; CLU_028970_2_0_1; -.
DR InParanoid; G1M1Z4; -.
DR TreeFam; TF315617; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0097001; F:ceramide binding; IEA:Ensembl.
DR GO; GO:0140340; F:cerebroside transfer activity; IEA:Ensembl.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:Ensembl.
DR GO; GO:0140337; F:diacylglyceride transfer activity; IEA:Ensembl.
DR GO; GO:0019992; F:diacylglycerol binding; IEA:Ensembl.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0070300; F:phosphatidic acid binding; IEA:Ensembl.
DR GO; GO:1990050; F:phosphatidic acid transfer activity; IEA:Ensembl.
DR GO; GO:0031210; F:phosphatidylcholine binding; IEA:Ensembl.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; IEA:Ensembl.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IEA:Ensembl.
DR GO; GO:1904121; F:phosphatidylethanolamine transfer activity; IEA:Ensembl.
DR GO; GO:1901611; F:phosphatidylglycerol binding; IEA:Ensembl.
DR GO; GO:0140339; F:phosphatidylglycerol transfer activity; IEA:Ensembl.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IEA:Ensembl.
DR GO; GO:0140338; F:sphingomyelin transfer activity; IEA:Ensembl.
DR GO; GO:0034189; F:very-low-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0035627; P:ceramide transport; IEA:Ensembl.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IEA:Ensembl.
DR CDD; cd00025; BPI1; 1.
DR CDD; cd00026; BPI2; 1.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR030675; BPI/LBP.
DR InterPro; IPR032942; BPI/LBP/Plunc.
DR InterPro; IPR001124; Lipid-bd_serum_glycop_C.
DR InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR PANTHER; PTHR10504; BACTERICIDAL PERMEABILITY-INCREASING BPI PROTEIN-RELATED; 1.
DR PANTHER; PTHR10504:SF16; PHOSPHOLIPID TRANSFER PROTEIN; 1.
DR Pfam; PF01273; LBP_BPI_CETP; 1.
DR Pfam; PF02886; LBP_BPI_CETP_C; 1.
DR PIRSF; PIRSF002417; Lipid_binding_protein; 1.
DR SMART; SM00328; BPI1; 1.
DR SMART; SM00329; BPI2; 1.
DR SUPFAM; SSF55394; Bactericidal permeability-increasing protein, BPI; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002417-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..496
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030171243"
FT DOMAIN 25..243
FT /note="Lipid-binding serum glycoprotein N-terminal"
FT /evidence="ECO:0000259|SMART:SM00328"
FT DOMAIN 258..460
FT /note="Lipid-binding serum glycoprotein C-terminal"
FT /evidence="ECO:0000259|SMART:SM00329"
FT REGION 475..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 146..185
FT /evidence="ECO:0000256|PIRSR:PIRSR002417-50"
SQ SEQUENCE 496 AA; 54893 MW; 1D1ED11AB5F86F8E CRC64;
MALFGALFVA LLAGAQAELS GCKIRVTSKA LELVKQEGLR FLEQELETIT IPDLRGREGH
FYYNISEVKV TELQLTPSEL HFQPEQELVL QISNASLGLR FRRQLLYWFF YDGGYINASA
EGVSIRTALQ LSRDATGRIK VSNVSCQASV SRMHAAFGGT FKKVYEFLST FITSGMRFLL
NQQICPVLYH AGMVLLNSLL DTVPVRSSVD ELVGIDYSLL KDPVASDSNL DMEFRGAFFP
LAEGNWSLLN RAVEPQLQEA ERMVYVAFSE FFFDSAMESY FRAGALQLSL VGDKVPHDLD
MLLRATYFGS IVLLSPAVID SPLKLELRVL APPRCTIKPS GTTVSVTASV TIALVPPDLP
EVQLSSMIMD ARLSAKMALR GKALRTQLDL RRFRIYSNQS ALESLALIPL QAPLKTMLQI
GVMPMLNERM WRGVQIPLPE GMNFVREVVT NHVGFLTIGA DLHFAKGLRE VIEKNRPANT
RDPLASSAPP PSTAAA
//
