CERT_XENTR
ID CERT_XENTR Reviewed; 617 AA.
AC Q6P3Q6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ceramide transfer protein {ECO:0000305};
DE Short=CERT;
DE AltName: Full=Collagen type IV alpha-3-binding protein;
GN Name=cert1; Synonyms=cert, col4a3bp;
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 (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May mediate the intracellular trafficking of ceramide in a
CC non-vesicular manner. {ECO:0000250|UniProtKB:Q9Y5P4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-hexadecanoylsphing-4-enine(in) = N-hexadecanoylsphing-4-
CC enine(out); Xref=Rhea:RHEA:45720, ChEBI:CHEBI:72959;
CC Evidence={ECO:0000250|UniProtKB:Q6VVX2};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y5P4}. Golgi
CC apparatus {ECO:0000250|UniProtKB:Q9Y5P4}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Y5P4}.
CC -!- DOMAIN: The START domain recognizes ceramide and mediates the
CC intermembrane transfer of ceramide. {ECO:0000250|UniProtKB:Q9Y5P4}.
CC -!- DOMAIN: The PH domain targets the Golgi apparatus.
CC {ECO:0000250|UniProtKB:Q9Y5P4}.
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DR EMBL; BC063901; AAH63901.1; -; mRNA.
DR RefSeq; NP_988844.1; NM_203513.1.
DR AlphaFoldDB; Q6P3Q6; -.
DR SMR; Q6P3Q6; -.
DR STRING; 8364.ENSXETP00000011086; -.
DR PaxDb; Q6P3Q6; -.
DR DNASU; 387331; -.
DR Ensembl; ENSXETT00000011086; ENSXETP00000011086; ENSXETG00000005085.
DR GeneID; 387331; -.
DR KEGG; xtr:387331; -.
DR CTD; 10087; -.
DR Xenbase; XB-GENE-1002414; cert1.
DR eggNOG; KOG1739; Eukaryota.
DR HOGENOM; CLU_017289_0_0_1; -.
DR InParanoid; Q6P3Q6; -.
DR OrthoDB; 959972at2759; -.
DR PhylomeDB; Q6P3Q6; -.
DR Reactome; R-XTR-1660661; Sphingolipid de novo biosynthesis.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000005085; Expressed in 4-cell stage embryo and 12 other tissues.
DR ExpressionAtlas; Q6P3Q6; baseline.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; 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:0070273; F:phosphatidylinositol-4-phosphate binding; IBA:GO_Central.
DR GO; GO:0035627; P:ceramide transport; IBA:GO_Central.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; IBA:GO_Central.
DR GO; GO:0120009; P:intermembrane lipid transfer; IBA:GO_Central.
DR CDD; cd08872; START_STARD11-like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR041952; STARD11_START.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00234; START; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50848; START; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Endoplasmic reticulum; Golgi apparatus;
KW Lipid transport; Reference proteome; Transport.
FT CHAIN 1..617
FT /note="Ceramide transfer protein"
FT /id="PRO_0000307358"
FT DOMAIN 23..117
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 383..611
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 268..302
FT /evidence="ECO:0000255"
FT MOTIF 320..326
FT /note="FFAT"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 466
FT /ligand="an N-acylsphing-4-enine"
FT /ligand_id="ChEBI:CHEBI:52639"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT BINDING 487
FT /ligand="an N-acylsphing-4-enine"
FT /ligand_id="ChEBI:CHEBI:52639"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT BINDING 524
FT /ligand="an N-acylsphing-4-enine"
FT /ligand_id="ChEBI:CHEBI:52639"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT BINDING 572
FT /ligand="an N-acylsphing-4-enine"
FT /ligand_id="ChEBI:CHEBI:52639"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
SQ SEQUENCE 617 AA; 70153 MW; 50EBC427B6B43D6C CRC64;
MSDNQSWNSS GSEEDLETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN TLSYYKSEDE
TEYGCRGSIC LSKAVITPHE FDECRFDISV NDSVWYLRAQ DPDHRQRWID SIEQHKSESG
YGSESSLRRH GSMVSLVSGA SGYSATSTSS FKKGHSLREK LAEMETFRDI LCRQVDTLQK
YFDACADAVS KDELERDKVE DDEDDFLHSH PNGDYIHSSI GSKDKLFQHV SPKGINGIDF
KGEAITFKAT TAGILATLSH CIDLMVKRED SWQKRLDKEI EKRRRVEEAY KNAMTELKKK
SHFGGPDYEE GPNSLINEEE FFDAVEAALD RQDKIEQSQS EKGRSHWPSS LPSTEAYTTA
GSHRFVQAPP SCPPPTDLVS SSDEHRFRIQ VEEMVQNHMT YSLQDVGGDA NWQLVVEEGE
MKVYRREVEE NGIVLDPLKA THSVKGVTGH EVCQHFWNVD VRNDWETTIE NFHVVEKLSP
NAIIVYQTHK RVWPASQRDV LYLSAIRMVP AASENEMDTW IVCNFSVDHD NAPLNRCVRA
KINIAMICQT LVSPPEGNKE ISRDNIQCKI TYVANVNPGG WAPASVLRAV AKREYPKFLK
RFTSYVQEKT AGKSILF
