ID E2BKT8_HARSA Unreviewed; 591 AA.
AC E2BKT8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 ORFNames=EAI_10223 {ECO:0000313|EMBL:EFN83687.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN83687.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN83687.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL448826; EFN83687.1; -; Genomic_DNA.
DR RefSeq; XP_011140753.1; XM_011142451.2.
DR AlphaFoldDB; E2BKT8; -.
DR STRING; 610380.E2BKT8; -.
DR EnsemblMetazoa; XM_025305700.1; XP_025161485.1; LOC105183968.
DR InParanoid; E2BKT8; -.
DR OMA; GAEAKCH; -.
DR OrthoDB; 5489052at2759; -.
DR PhylomeDB; E2BKT8; -.
DR Proteomes; UP000008237; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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 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 Collagen {ECO:0000313|EMBL:EFN83687.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Reference proteome {ECO:0000313|Proteomes:UP000008237}.
FT DOMAIN 37..132
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 382..585
FT /note="START"
FT /evidence="ECO:0000259|PROSITE:PS50848"
SQ SEQUENCE 591 AA; 67695 MW; 2442E1BE9CE0394B CRC64;
MADEVVETIR LNNEDAECID AEIDGDDEEE GSDGVIVPEL QGTLSKWTNY IHGWQTRFIV
LKDGTLSYYK SEQDSGFGCR GSISLYKANI KAHEFDECRF DVSVNDCLVW YLRARSPEEK
QRWVDVLKSY KSESGYGSEN SLKRHGSAIS LVSNTQSTAS AGSFTKRGIR GLKEKLAEIE
TFRDILIKQI DTLQKYFDNC AENAKNTSKK EKKIETMFNP AEQSVDFKGE AITFKATSEG
VLATLQHCVE LMIQREDAWR RRWEKEVEKK RKLQELYKTL KDQVAMHHTG SPRSRVLIHG
GPDYEEGPHS ALCDEEFYDA VETGLDKIEE ENQLRDRLKQ KSVSILTSPT ITASTHRLWP
EIEKITMEQL HYARLGVGGA GGWQLFAEDG DMRMYRREEE ADGLVVDPLK ACHVVKGVTG
HEVCEIFFSP EYRSGWEATL EDMTVVENIS KDTLLFLQTH KRIWPASQRD ALFWSHMRRV
SDDQDRDAHD LWIVCNHSTE HPDYPPNAGK CVRVYLTVCL VCQTCIDPPK DEEEIKRENI
TCKITYCSVV NPGGWAPASV LRAVYKREYP KFLKRFTNFC IDQCKSKPIT F
//