GenomeNet

Database: UniProt
Entry: G1NSX2_MYOLU
LinkDB: G1NSX2_MYOLU
Original site: G1NSX2_MYOLU 
ID   G1NSX2_MYOLU            Unreviewed;       519 AA.
AC   G1NSX2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Phospholipid transfer protein {ECO:0000313|Ensembl:ENSMLUP00000000246.2};
GN   Name=PLTP {ECO:0000313|Ensembl:ENSMLUP00000000246.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000000246.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000000246.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000000246.2}
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAPE02023324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1NSX2; -.
DR   STRING; 59463.ENSMLUP00000000246; -.
DR   Ensembl; ENSMLUT00000000268.2; ENSMLUP00000000246.2; ENSMLUG00000000269.2.
DR   eggNOG; KOG4160; Eukaryota.
DR   GeneTree; ENSGT01100000263545; -.
DR   HOGENOM; CLU_028970_2_0_1; -.
DR   InParanoid; G1NSX2; -.
DR   OMA; GMFAYYS; -.
DR   TreeFam; TF315617; -.
DR   Proteomes; UP000001074; 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; IPR017954; Lipid-bd_serum_glycop_CS.
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.
DR   PROSITE; PS00400; LBP_BPI_CETP; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR002417-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..519
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003417517"
FT   DOMAIN          47..265
FT                   /note="Lipid-binding serum glycoprotein N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00328"
FT   DOMAIN          280..483
FT                   /note="Lipid-binding serum glycoprotein C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00329"
FT   REGION          498..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        168..207
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002417-50"
SQ   SEQUENCE   519 AA;  57219 MW;  5B07353BF3A61C8F CRC64;
     RRVEGPGDSR DPTLPPGPLV MARFAALFLA LLAGAQADAE IPGCKIRITS KALELLKQEG
     LRFLEQELET VTIPDLGGRE GHFYYNISEV TVTEMQLTSS ELHFQPEQEL VLQTSNSSLG
     LRFRRQLRYW IFYDGGYINA SAQGISIHTA LQLSRDPTGR VKVANVSCQA SVSKLYAAFE
     GTFKIVYQFL STFVTSGMHF LLNQQICPVI HHAGMVLLNS LLDTVPVRSS VDKLVGIDYS
     LVKDPVVSSS YMDMEFRGAF FPLAQGNWSL PNRAVEPQLQ EEERMVYVAF SEFFFDSALE
     SYFQAGALQL SLVGDKVPKD LDMLLRASYF GSIVLLQSPA VIDSPLKLEL RVVAPPYCTI
     KPSGTTVSVT ASVTVALVPP NQPEVQLSSM IMDARLSAKM ALQGKALRIF IDFREFRIYS
     NQSALESLAL IPLQAPLKTM LQFGVMPLLN ERTRRGVQIP LPEGMDFVRE VVTNHAGFLT
     IAADLHFAKG LREVIEKNRP ANNMDSGVPS APPPSTAAV
//
DBGET integrated database retrieval system