ID W5MDW7_LEPOC Unreviewed; 624 AA.
AC W5MDW7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Ceramide transfer protein {ECO:0000256|ARBA:ARBA00021440};
DE AltName: Full=Collagen type IV alpha-3-binding protein {ECO:0000256|ARBA:ARBA00031527};
GN Name=CERT1 {ECO:0000313|Ensembl:ENSLOCP00000006576.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000006576.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000006576.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000074};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}.
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DR EMBL; AHAT01014705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01014706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006626774.1; XM_006626711.2.
DR RefSeq; XP_015220260.1; XM_015364774.1.
DR RefSeq; XP_015220270.1; XM_015364784.1.
DR AlphaFoldDB; W5MDW7; -.
DR STRING; 7918.ENSLOCP00000006576; -.
DR Ensembl; ENSLOCT00000006584.1; ENSLOCP00000006576.1; ENSLOCG00000005451.1.
DR GeneID; 102687266; -.
DR KEGG; loc:102687266; -.
DR CTD; 10087; -.
DR eggNOG; KOG1739; Eukaryota.
DR GeneTree; ENSGT00940000155123; -.
DR HOGENOM; CLU_017289_0_0_1; -.
DR InParanoid; W5MDW7; -.
DR OMA; SLFWSHM; -.
DR OrthoDB; 5489052at2759; -.
DR Proteomes; UP000018468; Linkage group LG2.
DR Bgee; ENSLOCG00000005451; Expressed in larva and 13 other cell types or 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:0035621; P:ER to Golgi ceramide transport; IBA:GO_Central.
DR CDD; cd13283; PH_GPBP; 1.
DR CDD; cd08872; START_STARD11-like; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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 PANTHER; PTHR19308:SF53; CERAMIDE TRANSFER PROTEIN; 1.
DR PANTHER; PTHR19308; PHOSPHATIDYLCHOLINE TRANSFER PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50848; START; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 23..117
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 415..618
FT /note="START"
FT /evidence="ECO:0000259|PROSITE:PS50848"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 70976 MW; E4AA2CEFB3BFE087 CRC64;
MSDNQSWNSS GSEEDLETES GPPVELGGIL SKWTNYIHGW QDRWVVLKNN TLSYYKSEDE
REYGCRGSLC LSKAVITPHE FDECRFDISV NDSVWYLRAQ DPEHRHQWMD SIEQHKAESG
YGSESSLRRH GSMLSLTSAA SGYSATSTSS FKKGHSLREK LAEMETFRDI LCRQVDTLQK
YFDACADAVS KDELQRDKVV EDDEDDFPTT RPDGEFLHNN NGSKEKLFPC VNPKGINGID
FKGEAITFKA TTAGILATLS HCIDLMVKRE DSWQKRLDKE MDKRRRVEDA YKTAMTELKK
KSHFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDKIEEQS QSEKTRIHRP TAVPSDDAYS
AVGKHRFGQK PYSRSSSMSS IDLVSASDDV HRFSTQVEDM VQNHITYSLQ DVGGDANWQL
VVEEGEMKVY RREVEENGIV LDPLKATHAV KGVTGHEVCH YFWNVEVRND WETTIENFNV
VETLSDNAII VYQTHKRVWP ASQRDVLYLS AIRKIIANNE NDPDTWIVCN FSVDHNNVPL
TNRCVRAKIN IAMICQTLVS PPEGDKEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR
EYPKFLKRFT SYVQEKTAGK PILF
//
