ID   CERT_XENLA              Reviewed;         617 AA.
AC   Q6NRZ4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
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 laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) 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; BC070560; AAH70560.1; -; mRNA.
DR   RefSeq; NP_001084949.1; NM_001091480.1.
DR   AlphaFoldDB; Q6NRZ4; -.
DR   SMR; Q6NRZ4; -.
DR   DNASU; 432007; -.
DR   GeneID; 432007; -.
DR   KEGG; xla:432007; -.
DR   CTD; 432007; -.
DR   Xenbase; XB-GENE-1002420; cert1.L.
DR   OMA; EDQSKKF; -.
DR   OrthoDB; 959972at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 432007; Expressed in testis and 19 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
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_0000307357"
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          341..382
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..15
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;  70333 MW;  04BBA0F19D1D56DB CRC64;
     MSDNQSWNSS GSEEDLEPES GPPVERCGVL SKWTNYIHGW QDRWVDLKNN TLSYYKSEDE
     TEYGCRGSIC LSKAVITPHE FDECRFDISV NDSVWYIRAQ DPDHRQRWID SIEQHKSESG
     YGSESSLRRH GSMVSLVSGA SSYSATSTSS FKKGHSLREK LAEMETFRDI LCRQVDTLQK
     YFDACAGAVS KDELERDKVE DDEDDFLHNH PNEDYIHSNN GNKEKLFQHV TPKCIDGIDF
     KGEAITFKAT TAGILATLSH CIELMVKRED SWQKRLDKEI EKRRRVEEAY KNAMTELKKK
     SHFGGPDYEE GPNSLINEEE FFDAVEAALD RQDKIELCQS EKGRSHWPPS PPSSEAHTAA
     GSHRLVQAPP SCPPPTDLVS SSDEHRFRIQ VEDMVQNHMT YSLQDVGGDA NWQLVVEEGE
     MKVYRREVEE NGIVLDPLKA THSVKGVTGH EVCQYFWNVD VRNDWETTIE NFHVVEKLSP
     NAIIVYQTHK RVWPASQRDV LYLSAIRVVP AASENEMDTW IVCNFSVDHD KAPLNRCVRA
     KINIAMICQT LVSPPEGNKE ISRDNIQCKI TYVANVNPGG WAPASVLRAV AKREYPKFLK
     RFTSYVQEKT ADKPILF