ID A0A0V1BAK8_TRISP Unreviewed; 959 AA.
AC A0A0V1BAK8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=COL4A3BP {ECO:0000313|EMBL:KRY34036.1};
GN ORFNames=T01_6113 {ECO:0000313|EMBL:KRY34036.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY34036.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY34036.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY34036.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY34036.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDH01000073; KRY34036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1BAK8; -.
DR Proteomes; UP000054776; 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:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR010876; C1orf43.
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; PF07406; NICE-3; 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, ECO:0000256|SAM:Coils};
KW Collagen {ECO:0000313|EMBL:KRY34036.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054776};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 22..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 364..458
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 751..953
FT /note="START"
FT /evidence="ECO:0000259|PROSITE:PS50848"
FT REGION 270..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 624..651
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 270..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 959 AA; 108892 MW; 8EDF287C7A7218FB CRC64;
MEYANISNAG NNSTSGYRLG QISGITLTYL IALAGQILAV VFIMAKRRVV RNNLLLPKNP
YSAAGTGASA RFRAKIQRGI LLTSSYKHFH PLLVGGSEQE RAERFRRQAV DSFATVLTKL
GSWARFRWSR HSLPTVALLR RLVDEGYIGR QQQVTDDDCE QFASLYDTAR YTSRPFGEQE
LDRFVLLYEK MFAGVESWHE KQPLEEDVTE RCAFVFASYL DVCGVVESFG WFNLKLRPTG
MYHITSLGTQ SLNLAKRTIK RALSSHQQSD NVVVTTSQQQ QHQQQSTGTA EPLVEHQHPP
ARRAQPQQQE NWICGNCASS PTQHKLCADG FFQTTSSASR NDDNSNCAET VSWSSEGEPV
ESACPILTGV LNKWTNYIHG WQPRYFVLQA GTLAYYKSEQ EIEFGCRGAI TVSKAIIQMH
DYDDCRVDIS VNDCVWYLRA DRLQDRQRWL DAIEAYRADS GYGSQGDLCR HGSLVSLTSN
KSLASSSSFK VCQGLNEKIS ELETYREIVL RQIDTLQSYF DSCAEETTST WNIPRAPREP
GEDFDDIDAD HTMVHPSPHL ITMGTAGMLN AHANGTTVHH REEPTIPNAK RAADFRSEAL
TFKATTAGIL PLLQHCTDLV QQSEDAWKRR LEQETDRRKR ADDNCRQLAL ELQKLHVDRS
SLAFGGPDYE EGPHSALKED EWHDALDAAL EKQDLEDRRV ERLLARNVGP GKLQPFDKIL
LSTDHSLFNE IEQTTMEQVK YAQQGVSDGE WQLFSEDGEM KMYRREVEIG GLVCDPLKAV
HHVKGVSALE YLHYFYEPDY KMDWDTTLEE LKVIERMSED TMILQQIHKR VWPAAQRESL
FWSHIRRVPK PTDSNALDMI VVCNHDTQHA AAPPNSRTVR VGLTIAMVCQ TIVENASVDR
NKLTRDDVSC KITYVAQVNP RGWAPSSVLR AVYKREYPKF LKRFTQYVLQ KVENSPIQL
//
