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GLTP_XENTR
ID   GLTP_XENTR              Reviewed;         209 AA.
AC   B0BLT4;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Glycolipid transfer protein;
DE            Short=GLTP;
GN   Name=gltp;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Accelerates the intermembrane transfer of various
CC       glycolipids. Catalyzes the transfer of various glycosphingolipids
CC       between membranes but does not catalyze the transfer of phospholipids.
CC       May be involved in the intracellular translocation of glucosylceramides
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GLTP family. {ECO:0000305}.
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DR   EMBL; BC158153; AAI58154.1; -; mRNA.
DR   AlphaFoldDB; B0BLT4; -.
DR   SMR; B0BLT4; -.
DR   STRING; 8364.ENSXETP00000040315; -.
DR   PaxDb; B0BLT4; -.
DR   eggNOG; KOG3221; Eukaryota.
DR   InParanoid; B0BLT4; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:1902387; F:ceramide 1-phosphate binding; IBA:GO_Central.
DR   GO; GO:1902388; F:ceramide 1-phosphate transfer activity; IBA:GO_Central.
DR   GO; GO:0035627; P:ceramide transport; IBA:GO_Central.
DR   GO; GO:0120009; P:intermembrane lipid transfer; IBA:GO_Central.
DR   Gene3D; 1.10.3520.10; -; 1.
DR   InterPro; IPR036497; GLTP_sf.
DR   InterPro; IPR014830; Glycolipid_transfer_prot_dom.
DR   Pfam; PF08718; GLTP; 1.
DR   SUPFAM; SSF110004; SSF110004; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lipid transport; Reference proteome; Repeat; Transport.
FT   CHAIN           1..209
FT                   /note="Glycolipid transfer protein"
FT                   /id="PRO_0000343613"
FT   REPEAT          45..55
FT                   /note="1"
FT   REPEAT          56..66
FT                   /note="2"
FT   REGION          45..66
FT                   /note="2 X 12 AA approximate tandem repeats"
FT   BINDING         48..55
FT                   /ligand="beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-
FT                   N-[(9Z)-octadecenoyl]-sphing-4-enine"
FT                   /ligand_id="ChEBI:CHEBI:131557"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZD2"
FT   BINDING         140
FT                   /ligand="beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-
FT                   N-[(9Z)-octadecenoyl]-sphing-4-enine"
FT                   /ligand_id="ChEBI:CHEBI:131557"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZD2"
FT   BINDING         207
FT                   /ligand="beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-
FT                   N-[(9Z)-octadecenoyl]-sphing-4-enine"
FT                   /ligand_id="ChEBI:CHEBI:131557"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZD2"
SQ   SEQUENCE   209 AA;  23906 MW;  1BB26DA823C91966 CRC64;
     MSVLLQHQFK PLPADKQIDT CCFLDSVSHL PAFFDCFGSA IFSPIKADIT GNISKIRSVY
     ESNPSKFKTL QMILEGEKEL HGPQWPKVGA TLALMWLKRG LKFIQVMLQS IADGERDDQN
     PNLIKVNITK AYEIALKKYH GWFVQKIFQT ALIAAPYKDD FLKALSKGQT VKEEECIEKI
     RQFLVNYTTT IEAIYIMYNK MNAELDYKA
 
 
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