CERT_PONAB
ID CERT_PONAB Reviewed; 624 AA.
AC Q5R6M6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ceramide transfer protein {ECO:0000305};
DE Short=CERT;
DE AltName: Full=Collagen type IV alpha-3-binding protein;
DE AltName: Full=START domain-containing protein 11;
DE Short=StARD11;
DE AltName: Full=StAR-related lipid transfer protein 11;
GN Name=CERT1; Synonyms=CERT, COL4A3BP, STARD11;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Shelters ceramides and diacylglycerol lipids inside its START
CC domain and mediates the intracellular trafficking of ceramides and
CC diacylglycerol lipids in a non-vesicular manner.
CC {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 -!- SUBUNIT: Interacts with VAPA and VAPB. Interaction with VAPB is less
CC efficient than with VAPA. Interacts (via FFAT motif) with the MOSPD2
CC (via MSP domain). {ECO:0000250|UniProtKB:Q9Y5P4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y5P4}. Golgi
CC apparatus {ECO:0000250|UniProtKB:Q9Y5P4}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Y5P4}. Note=Preferentially localized to the
CC Golgi apparatus. {ECO:0000250|UniProtKB:Q9Y5P4}.
CC -!- DOMAIN: The START domain recognizes ceramides and diacylglycerol
CC lipids, interacts with membranes, and mediates the intermembrane
CC transfer of ceramides and diacylglycerol lipids.
CC {ECO:0000250|UniProtKB:Q9Y5P4}.
CC -!- DOMAIN: The PH domain targets the Golgi apparatus.
CC {ECO:0000250|UniProtKB:Q9Y5P4}.
CC -!- DOMAIN: The FFAT motif is required for interaction with VAPA, VAPB and
CC MOSPD2. {ECO:0000250|UniProtKB:Q9Y5P4}.
CC -!- PTM: Phosphorylation on Ser-132 decreases the affinity toward
CC phosphatidylinositol 4-phosphate at Golgi membranes and reduces
CC ceramide transfer activity. Inactivated by hyperphosphorylation of
CC serine residues by CSNK1G2/CK1 that triggers dissociation from the
CC Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide
CC and sphingomyelin synthesis. {ECO:0000250|UniProtKB:Q9Y5P4}.
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DR EMBL; CR860461; CAH92584.1; -; mRNA.
DR RefSeq; NP_001126514.1; NM_001133042.2.
DR AlphaFoldDB; Q5R6M6; -.
DR BMRB; Q5R6M6; -.
DR SMR; Q5R6M6; -.
DR STRING; 9601.ENSPPYP00000017396; -.
DR GeneID; 100173502; -.
DR KEGG; pon:100173502; -.
DR CTD; 10087; -.
DR eggNOG; KOG1739; Eukaryota.
DR InParanoid; Q5R6M6; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0097001; F:ceramide binding; ISS:UniProtKB.
DR GO; GO:0120017; F:ceramide transfer activity; ISS:UniProtKB.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; ISS:UniProtKB.
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; Lipid-binding; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..624
FT /note="Ceramide transfer protein"
FT /id="PRO_0000253586"
FT DOMAIN 23..117
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 389..618
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 263..303
FT /evidence="ECO:0000255"
FT MOTIF 321..327
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 472
FT /ligand="an N-acylsphing-4-enine"
FT /ligand_id="ChEBI:CHEBI:52639"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT BINDING 493
FT /ligand="an N-acylsphing-4-enine"
FT /ligand_id="ChEBI:CHEBI:52639"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT BINDING 530
FT /ligand="an N-acylsphing-4-enine"
FT /ligand_id="ChEBI:CHEBI:52639"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT BINDING 579
FT /ligand="an N-acylsphing-4-enine"
FT /ligand_id="ChEBI:CHEBI:52639"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT MOD_RES 132
FT /note="Phosphoserine; by PKD"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQG9"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT MOD_RES 372
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5P4"
SQ SEQUENCE 624 AA; 70854 MW; 9BDBFE9B3E34B342 CRC64;
MSDNQSWNSS GSEEDPETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN ALSYYKSEDE
TEYGCRGSIC LSKAVITPHD FDECRFDISV NDSVWYLRAQ DPDHRQQWID AIEQHKTESG
YGSESSLRRH GSMVSLVSGA SGYSATSTSS FKKGHSLREK LAEMETFRDI LCRQVDTLQK
YFDACADAVS KDELQRDKVV EDDEDDFPTT RSDGDFLHST NGNKEKLFPR VTPKGINGID
FKGEAITFKA TTVGIPATLS HCIELMVKRE DSWQKRLDKE TEKKRRTEEA YKNAMTELKK
KSHFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDEIEEQS QSEKVRLHWP TSLPSGDAFS
SVGTHRFVQK PYSRSSSVSS IDLVSASDDV HRFSSQVEEM VQNHMTYSLQ DVGGDANWQL
VVEEGEMKVY RREVEENGIV LDPLKATRAV KGVTGHEVCN YFWNVDVRND WETTIENFHV
VETLADNAII IYQTHKRVWP ASQRDVLYLS VIRKIPALTE NDPETWIVCN FSVDHDSAPL
NNRCVRAKIN VAMICQTLVS PPEGNQEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR
EYPKFLKRFT SYVQEKTAGK PILF
