CERT_BOVIN
ID CERT_BOVIN Reviewed; 624 AA.
AC Q9GKI7; Q9GKI6;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ceramide transfer protein;
DE Short=CERT;
DE AltName: Full=Collagen type IV alpha-3-binding protein;
DE AltName: Full=Goodpasture antigen-binding protein;
DE Short=GPBP;
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=11007769; DOI=10.1074/jbc.m002769200;
RA Raya A., Revert-Ros F., Martinez-Martinez P., Navarro S., Rosello E.,
RA Vieites B., Granero F., Forteza J., Saus J.;
RT "Goodpasture antigen-binding protein, the kinase that phosphorylates the
RT Goodpasture antigen, is an alternatively spliced variant implicated in
RT autoimmune pathogenesis.";
RL J. Biol. Chem. 275:40392-40399(2000).
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 MOSPD2 (via
CC 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9GKI7-1; Sequence=Displayed;
CC Name=2; Synonyms=Delta26, GPBPD26, CERT {ECO:0000250|UniProtKB:Q9Y5P4};
CC IsoId=Q9GKI7-2; Sequence=VSP_006275;
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; AF232931; AAG42047.1; -; mRNA.
DR EMBL; AF232933; AAG42049.1; -; mRNA.
DR RefSeq; NP_777190.1; NM_174765.2. [Q9GKI7-1]
DR AlphaFoldDB; Q9GKI7; -.
DR BMRB; Q9GKI7; -.
DR SMR; Q9GKI7; -.
DR STRING; 9913.ENSBTAP00000000092; -.
DR PaxDb; Q9GKI7; -.
DR PRIDE; Q9GKI7; -.
DR Ensembl; ENSBTAT00000000092; ENSBTAP00000000092; ENSBTAG00000000081. [Q9GKI7-1]
DR Ensembl; ENSBTAT00000056797; ENSBTAP00000049666; ENSBTAG00000000081. [Q9GKI7-2]
DR GeneID; 286797; -.
DR KEGG; bta:286797; -.
DR CTD; 10087; -.
DR VEuPathDB; HostDB:ENSBTAG00000000081; -.
DR eggNOG; KOG1739; Eukaryota.
DR GeneTree; ENSGT00940000155123; -.
DR HOGENOM; CLU_017289_0_0_1; -.
DR InParanoid; Q9GKI7; -.
DR OMA; EDQSKKF; -.
DR OrthoDB; 959972at2759; -.
DR TreeFam; TF106160; -.
DR BRENDA; 2.7.11.9; 908.
DR Reactome; R-BTA-1660661; Sphingolipid de novo biosynthesis.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000000081; Expressed in semitendinosus and 110 other tissues.
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:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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:0016301; F:kinase activity; IEA:Ensembl.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0006672; P:ceramide metabolic process; IEA:Ensembl.
DR GO; GO:0035627; P:ceramide transport; IBA:GO_Central.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:Ensembl.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; IBA:GO_Central.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0120009; P:intermembrane lipid transfer; IBA:GO_Central.
DR GO; GO:0120012; P:intermembrane sphingolipid transfer; IEA:Ensembl.
DR GO; GO:0055088; P:lipid homeostasis; IEA:Ensembl.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
DR GO; GO:0006936; P:muscle contraction; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:Ensembl.
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 Alternative splicing; Coiled coil; Cytoplasm; Endoplasmic reticulum;
KW Golgi apparatus; Lipid transport; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..624
FT /note="Ceramide transfer protein"
FT /id="PRO_0000220664"
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"
FT VAR_SEQ 371..396
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11007769"
FT /id="VSP_006275"
SQ SEQUENCE 624 AA; 70847 MW; 490D7FD950195476 CRC64;
MSDNQSWNSS GSEEDPETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN TLSYYKSEDE
TEYGCRGSIC LSKAVITPHD FDECRFDISV NDSVWYLRAQ DPDHRQQWID AIEQHKTESG
YGSESSLRRH GSMVSLVSGA SGYSATSTSS FKKGHSLREK LAEMETFRDI LCRQVDTLQK
FFDACADAVS KDEFQRDKVV EDDEDDFPTT RSDGDFLHNT NGNKEKVFPH VTPKGINGID
FKGEAITFKA TTAGILATLS HCIELMVKRE DSWQKRMDKE TEKRRRVEEA YKNAMTELKK
KSHFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDKIEEQS QSEKVRLHWS TSMPSGDAFS
SVGTHRFVQK PYSRSSSMSS IDLVSASDGV HRFSSQVEEM VQNHMTYSLQ DVGGDANWQL
VVEEGEMKVY RREVEENGIV LDPLKATHAV KGVTGHEVCN YFWNVDVRND WETTIENFHV
VETLADNAII IYQTHKRVWP ASQRDVLYLS AIRKIPALNE NDPETWIVCN FSVDHSSAPL
NNRCVRAKIN VAMICQTLVS PPEGNQEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR
EYPKFLKRFT SYVQEKTAGK PILF
