ID A0A443SIG6_9ACAR Unreviewed; 914 AA.
AC A0A443SIG6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Exostosin-3-like protein {ECO:0000313|EMBL:RWS27321.1};
GN ORFNames=B4U80_06532 {ECO:0000313|EMBL:RWS27321.1};
OS Leptotrombidium deliense.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombiculoidea; Trombiculidae; Leptotrombidium.
OX NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS27321.1, ECO:0000313|Proteomes:UP000288716};
RN [1] {ECO:0000313|EMBL:RWS27321.1, ECO:0000313|Proteomes:UP000288716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-UT {ECO:0000313|EMBL:RWS27321.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004648}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000256|ARBA:ARBA00010271}.
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:RWS27321.1}.
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DR EMBL; NCKV01002104; RWS27321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443SIG6; -.
DR STRING; 299467.A0A443SIG6; -.
DR EnsemblMetazoa; LDEU004719-RA; LDEU004719-PA; LDEU004719.
DR VEuPathDB; VectorBase:LDEU004719; -.
DR Proteomes; UP000288716; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProt.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR040911; Exostosin_GT47.
DR InterPro; IPR015338; GT64.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR48261; ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR PANTHER; PTHR48261:SF2; EXOSTOSIN-1-LIKE; 1.
DR Pfam; PF03016; Exostosin; 1.
DR Pfam; PF09258; Glyco_transf_64; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000288716};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 231..487
FT /note="Exostosin GT47"
FT /evidence="ECO:0000259|Pfam:PF03016"
FT DOMAIN 657..899
FT /note="Glycosyl transferase 64"
FT /evidence="ECO:0000259|Pfam:PF09258"
FT COILED 104..138
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 914 AA; 105076 MW; 67A1D5F375BDDF20 CRC64;
MAKICSLKIN ERTMIPLPSV RMQKVMVLLL VLLITVPFLT HYYISKVVIN SEKFGTNVVT
NPSLKSITYN EYNWNDVEAL QQIANLKLRV KEIMRIRGSV SNELKSMESK RQSLLSEINS
LSQKLDEIKG QLNRKQSELR RVHVSLEQAK FSQIEAYMKN PPFIAKPLPL LSDKVFTNEQ
DLHFSKSLDA NSEQSTDSSN ACDMHRCFDY SKCSLISGFP IFHYRSDEED YIPSDSQIFG
EHTNQVKADV FEALDNSIHT TSDASIACLF VVVLFHHRLE QSQLQSYLNN LAHWAEGRNH
VIINLMPNID LIDIGVNPRK ALVIQSQFSK HSFRNEFDIV SVVANNNEQK FPSFSPSKRS
YLASFRADFG ANSTTEYQTL ISILKTITRE SGDDIFKFEL NCSLSVCAKH EEILLESTFA
LIIPNSNSIS SQYISETLIR MLRLGAVPIL IGGDYIKLPF HEVIDWRLAV IHLPVARVTE
LHFILKSFND NDIFSMRRHG RLLYSRYLKD QKTIVNTILA VLRQKRLQIA APILSDEPSV
PLFNKSFPMK YFDPLENMLN PDSMEPDENL GPIEPPFSSI SYQRNYSLTL CHSYELWNSH
ELDPFNLYPY TPFDPILPSE AKFKGSTFGF RPIGGGSGGA GKEFSESLGG NVPKEQFTIV
ILTYEREAVL IDSLLRLKGL PHLNKILVIW NSADHLPSPD LKWPDVGVEI KVIRAQVNSL
NNRFKPYDEI ETEAVLSMDD DAHLRHDEII FGFRVWRESR DRIVGFPGRY HAWDASHSVW
LYNSNYSCEL SMVLTGAAFL HKYYTYLYTY SMPSSIRRRV DEYMNCEDIA MNFLVSHITR
KPPLKVTSRW TFRCPGCPVS LSEDDSHFQE RHRCINYFAE VYGYNPLLNT QFRADSVLFK
TRIPHDKQKC FKFI
//