ID V5HC06_IXORI Unreviewed; 721 AA.
AC V5HC06;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative carnitine o-palmitoyltransferase 1 {ECO:0000313|EMBL:JAB70758.1};
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:JAB70758.1};
RN [1] {ECO:0000313|EMBL:JAB70758.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB70758.1};
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 carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232}.
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DR EMBL; GANP01013710; JAB70758.1; -; mRNA.
DR AlphaFoldDB; V5HC06; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR22589:SF112; CHOLINE_CARNITINE ACYLTRANSFERASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:JAB70758.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..721
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004737881"
FT TRANSMEM 53..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 125..710
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 420
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 721 AA; 82689 MW; 6EA009247D4334AD CRC64;
MWPTSVQNIG ILCVIVFLFM LSEIDVAESI KEFFWDTGDT LHVPHALPST VRAVIVACFI
SIVLSVVFMK VRQIILRGLL AYRGWMYEAR KPGEKYLTLM WCMAVRVVSG YQPSLYSCQR
CLPRLPVPPL HDTIVRLLDS LKAVCTEDEM KVLSEQAEKF EKTLGPTLQR LLYLRSWYAS
NYVTDWWEKY IYLSSRSSLA VNSNYYCFDQ SYYHPSDIQS SRTAVIIHNC LVFKRLIDRE
ELQPLVLRGT VPICMSQYER LFSTTRVPGI DVDEICHFCT SESKHVILQH KGMFYKLEVY
DSTNQILFPT TLEHQIEWIM KDAEQHTPTE AETSLAALTS LDRPTWARIR NKYFLAGVNK
ESLDAIEKAT FFVSMNDLEP SGLNERGKYL LHGDGKSIWF DKSLNVQVFK NAHAGMNCEH
SMADAPAMAH MWEYALTREV LEKVYDESGR CMPPGKKLKQ GSIRRPQRLV WDISPELERE
IAGALANARK NNEDLDLYVR DHDSWGKGVI KKCKVSPDAF IQMALQLTYY KENKKFVQTY
EASMTRLYLN GRTETVRSCT LEAVDFVKAM VENSVSNEEK IRLLRRAANK HQMLYRDAMS
GKGVDRHLFA LFVACKGLKY ESEFLTNAIM RPWTLSTSQT PHTQLDYSPD ADLEVFTNKI
CPGGGFGPVS DDGYGVSYII PNNSKIFFHV SSKKSCPNTN SERFVKTLDE SMDEMKALFS
F
//