ID H0VMB5_CAVPO Unreviewed; 494 AA.
AC H0VMB5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Phospholipid transfer protein {ECO:0000313|Ensembl:ENSCPOP00000011543.3};
GN Name=PLTP {ECO:0000313|Ensembl:ENSCPOP00000011543.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000011543.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
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:ENSCPOP00000011543.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000011543.3};
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; AAKN02039553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003467746.1; XM_003467698.3.
DR RefSeq; XP_005002853.1; XM_005002796.2.
DR AlphaFoldDB; H0VMB5; -.
DR STRING; 10141.ENSCPOP00000011543; -.
DR Ensembl; ENSCPOT00000012948.3; ENSCPOP00000011543.3; ENSCPOG00000012823.4.
DR GeneID; 100720780; -.
DR KEGG; cpoc:100720780; -.
DR CTD; 5360; -.
DR VEuPathDB; HostDB:ENSCPOG00000012823; -.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01100000263545; -.
DR HOGENOM; CLU_028970_2_0_1; -.
DR InParanoid; H0VMB5; -.
DR OMA; GMFAYYS; -.
DR OrthoDB; 5307035at2759; -.
DR TreeFam; TF315617; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000012823; Expressed in hypothalamus and 13 other cell types or tissues.
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:UP000005447};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..494
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011442929"
FT DOMAIN 25..243
FT /note="Lipid-binding serum glycoprotein N-terminal"
FT /evidence="ECO:0000259|SMART:SM00328"
FT DOMAIN 258..458
FT /note="Lipid-binding serum glycoprotein C-terminal"
FT /evidence="ECO:0000259|SMART:SM00329"
FT REGION 473..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 146..185
FT /evidence="ECO:0000256|PIRSR:PIRSR002417-50"
SQ SEQUENCE 494 AA; 54845 MW; 0BB69B4628B03A28 CRC64;
MALFPALLLA LLAGAHAELP GCKIRITSKA LELVKQEGMR FLEQELETIT IPDLRGKEGQ
FHYNITEVQV TELQLNSSEL HFQPGQELIL QITNASLGLR FRRQLAYWVF SDGGYINASA
EGVSIRTGLQ LSQDPTGRMK VSNLSCQAFV SRMHMTFGGT FGRLYDFLST FIISGMRLLL
NQQICPVLYH SGMILLNSLL DTVPVRSSVD ELVGIDYSLL KDPVVSTDNL DMEFRGAFFP
LAEGNWSFLN RAVEPQLQEQ ERMVYVAFSE FFFNSALESY FWAGAFRLSL EKMPKDLDML
LRATYFGSIV FLTPAEINSP LKLELQVTAP PRCTIKLSGT TVSVTASVSI YLVPPNLPEI
QLSSMIMEAR LSAKMALRGK ALRAQLELSR FRIYSNQSAL ESLAMIPLQA PLKTVLQIGV
MPMINERTWR GVQIPLPEGI SFVREVVTNH AGFLTIGADL HFAKGLREVI EKNQPANTKD
TQASSAPPPS TAAA
//
