ID V5HFN7_IXORI Unreviewed; 369 AA.
AC V5HFN7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative selenoprotein i pediculus us corporis selenoprotein i {ECO:0000313|EMBL:JAB82420.1};
DE Flags: Fragment;
OS Ixodes ricinus (Common tick) (Acarus ricinus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB82420.1};
RN [1] {ECO:0000313|EMBL:JAB82420.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB82420.1};
RX PubMed=25765539;
RA Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT and midguts when blood feeding on the vertebrate host.";
RL Sci. Rep. 5:9103-9103(2015).
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000256|ARBA:ARBA00010441, ECO:0000256|RuleBase:RU003750}.
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DR EMBL; GANP01002048; JAB82420.1; -; mRNA.
DR AlphaFoldDB; V5HFN7; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR InterPro; IPR014472; CHOPT.
DR PANTHER; PTHR10414; ETHANOLAMINEPHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR10414:SF71; FI05338P; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF015665; CHOPT; 2.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 2: Evidence at transcript level;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023209};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003750};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 139..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB82420.1"
SQ SEQUENCE 369 AA; 41251 MW; 66A45FCDAB791EA1 CRC64;
YTSKDTSPLS NYVMHPFWDQ AVKLVPRNRG PQRADLLGLC PDGGERGAAL HVRLRLLCVE
RPAPRGAPRA PLGLAWSAPS TSSSPTTLDG IDGKHARHTG SSGPLGELFD HGLDSWATLF
MPVCLYSVFG RAELSCSTWR FFLILCNVHF CFILSHWEKY NTGILYLPWG YDISQMILLS
SFVLTYLKSY QFWKFTVLGF GAGECLELML HGGSFFMTIP MCLYNIHCAR VEGRLRQRSL
LEVVRPMGSV LALFLLSLTW VLASRDSILE REPRIFYLVL GTVFSNISCR LIISQMTSTR
CEAFNLLLLP VAASLAASVY LDVDEALLLK VLAAAVTLAH IHYGVCVVQQ MCSHFRIHCF
SLKKKPPIE
//
