CERT_MOUSE
ID CERT_MOUSE Reviewed; 624 AA.
AC Q9EQG9; Q3TQF6; Q8BNN8; Q8C8H3; Q8CAR3; Q91WB1; Q9CU52; Q9EQG8;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-425 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Adipose tissue, Cerebellum, Embryo, Medulla oblongata, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-414 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-135; SER-377 AND
RP SER-380, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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=3;
CC Name=1;
CC IsoId=Q9EQG9-1; Sequence=Displayed;
CC Name=2; Synonyms=Delta26, GPBPD26, CERT {ECO:0000250|UniProtKB:Q9Y5P4};
CC IsoId=Q9EQG9-2; Sequence=VSP_006277;
CC Name=3;
CC IsoId=Q9EQG9-3; Sequence=VSP_028735, VSP_028736;
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}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16197.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AF232932; AAG42048.1; -; mRNA.
DR EMBL; AF232934; AAG42050.1; -; mRNA.
DR EMBL; AK012989; BAB28581.1; -; mRNA.
DR EMBL; AK018103; BAB31070.1; -; mRNA.
DR EMBL; AK038061; BAC29927.1; -; mRNA.
DR EMBL; AK047100; BAC32962.1; -; mRNA.
DR EMBL; AK080958; BAC38095.2; -; mRNA.
DR EMBL; AK163624; BAE37427.1; -; mRNA.
DR EMBL; BC016197; AAH16197.1; ALT_SEQ; mRNA.
DR CCDS; CCDS26705.1; -. [Q9EQG9-1]
DR CCDS; CCDS49335.1; -. [Q9EQG9-2]
DR RefSeq; NP_001157694.1; NM_001164222.1. [Q9EQG9-2]
DR RefSeq; NP_075909.1; NM_023420.2. [Q9EQG9-1]
DR AlphaFoldDB; Q9EQG9; -.
DR SMR; Q9EQG9; -.
DR BioGRID; 212600; 4.
DR IntAct; Q9EQG9; 1.
DR STRING; 10090.ENSMUSP00000076856; -.
DR iPTMnet; Q9EQG9; -.
DR PhosphoSitePlus; Q9EQG9; -.
DR EPD; Q9EQG9; -.
DR jPOST; Q9EQG9; -.
DR MaxQB; Q9EQG9; -.
DR PaxDb; Q9EQG9; -.
DR PeptideAtlas; Q9EQG9; -.
DR PRIDE; Q9EQG9; -.
DR ProteomicsDB; 273856; -. [Q9EQG9-1]
DR ProteomicsDB; 273857; -. [Q9EQG9-2]
DR ProteomicsDB; 273858; -. [Q9EQG9-3]
DR Antibodypedia; 24390; 373 antibodies from 35 providers.
DR DNASU; 68018; -.
DR Ensembl; ENSMUST00000077672; ENSMUSP00000076856; ENSMUSG00000021669. [Q9EQG9-1]
DR Ensembl; ENSMUST00000109444; ENSMUSP00000105070; ENSMUSG00000021669. [Q9EQG9-2]
DR Ensembl; ENSMUST00000179226; ENSMUSP00000136766; ENSMUSG00000021669. [Q9EQG9-2]
DR GeneID; 68018; -.
DR KEGG; mmu:68018; -.
DR UCSC; uc007rni.2; mouse. [Q9EQG9-3]
DR UCSC; uc007rnk.2; mouse. [Q9EQG9-1]
DR UCSC; uc007rnl.2; mouse. [Q9EQG9-2]
DR CTD; 10087; -.
DR MGI; MGI:1915268; Cert1.
DR VEuPathDB; HostDB:ENSMUSG00000021669; -.
DR eggNOG; KOG1739; Eukaryota.
DR GeneTree; ENSGT00940000155123; -.
DR HOGENOM; CLU_017289_0_0_1; -.
DR InParanoid; Q9EQG9; -.
DR OMA; EDQSKKF; -.
DR OrthoDB; 959972at2759; -.
DR PhylomeDB; Q9EQG9; -.
DR TreeFam; TF106160; -.
DR BRENDA; 2.7.11.9; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR BioGRID-ORCS; 68018; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Col4a3bp; mouse.
DR PRO; PR:Q9EQG9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9EQG9; protein.
DR Bgee; ENSMUSG00000021669; Expressed in substantia nigra and 234 other tissues.
DR Genevisible; Q9EQG9; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
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:0097001; F:ceramide binding; ISS:UniProtKB.
DR GO; GO:0120017; F:ceramide transfer activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; IDA:MGI.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISO:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0006672; P:ceramide metabolic process; IMP:MGI.
DR GO; GO:0035627; P:ceramide transport; IBA:GO_Central.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0120009; P:intermembrane lipid transfer; IBA:GO_Central.
DR GO; GO:0120012; P:intermembrane sphingolipid transfer; ISO:MGI.
DR GO; GO:0055088; P:lipid homeostasis; IMP:MGI.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:MGI.
DR GO; GO:0006936; P:muscle contraction; IMP:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IMP:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Endoplasmic reticulum;
KW Golgi apparatus; Lipid transport; Lipid-binding; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..624
FT /note="Ceramide transfer protein"
FT /id="PRO_0000220666"
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 REGION 202..221
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"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 311..313
FT /note="EGP -> VWT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028735"
FT VAR_SEQ 314..624
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028736"
FT VAR_SEQ 371..396
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11007769,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_006277"
FT CONFLICT 526
FT /note="W -> S (in Ref. 2; BAB31070)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="S -> P (in Ref. 2; BAB31070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 624 AA; 71111 MW; FD708AFFB25FCD31 CRC64;
MSDNQSWNSS GSEEDPETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN TLSYYKSEDE
TEYGCRGSIC LSKAVITPHD FDECRFDISV NDSVWYLRAQ DPEHRQQWVD AIEQHKTESG
YGSESSLRRH GSMVSLVSGA SGYSATSTSS FKKGHSLREK LAEMETFRDI LCRQVDTLQK
YFDVCADAVS KDELQRDKVV EDDEDDFPTT RSDGDFLHNT NGNKEKLFPH VTPKGINGID
FKGEAITFKA TTAGILATLS HCIELMVKRE ESWQKRHDRE VEKRRRVEEA YKNVMEELKK
KPRFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDKIEEQS QSEKVRLHWP TSLPSGDTFS
SVGTHRFVQK PYSRSSSMSS IDLVSASDDV HRFSSQVEEM VQNHMNYSLQ DVGGDANWQL
VVEEGEMKVY RREVEENGIV LDPLKATHAV KGVTGHEVCN YFWNVDVRND WETTIENFHV
VETLADNAII VYQTHKRVWP ASQRDVLYLS AIRKIPALTE NDPETWIVCN FSVDHDSAPL
NNRCVRAKIN IAMICQTLVS PPEGDQEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR
EYPKFLKRFT SYVQEKTAGK PILF
