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Database: UniProt
Entry: A0A093HST5_STRCA
LinkDB: A0A093HST5_STRCA
Original site: A0A093HST5_STRCA 
ID   A0A093HST5_STRCA        Unreviewed;       380 AA.
AC   A0A093HST5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Hexosyltransferase {ECO:0000256|RuleBase:RU363063};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363063};
DE   Flags: Fragment;
GN   ORFNames=N308_11019 {ECO:0000313|EMBL:KFV82555.1};
OS   Struthio camelus australis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV82555.1, ECO:0000313|Proteomes:UP000053584};
RN   [1] {ECO:0000313|EMBL:KFV82555.1, ECO:0000313|Proteomes:UP000053584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV82555.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-N-
CC         acetyl-alpha-D-glucosamine = a beta-D-GlcNAc-(1->3)-beta-D-Gal-
CC         (1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + H(+) + UDP;
CC         Xref=Rhea:RHEA:13905, ChEBI:CHEBI:15378, ChEBI:CHEBI:17103,
CC         ChEBI:CHEBI:17950, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223;
CC         EC=2.4.1.206; Evidence={ECO:0000256|ARBA:ARBA00036283};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13906;
CC         Evidence={ECO:0000256|ARBA:ARBA00036283};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a neolactoside nLc4Cer(d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC         glucosamine = a neolactoside IV(3)-beta-GlcNAc-nLc4Cer(d18:1(4E)) +
CC         H(+) + UDP; Xref=Rhea:RHEA:23004, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17006, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:142448; Evidence={ECO:0000256|ARBA:ARBA00036580};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23005;
CC         Evidence={ECO:0000256|ARBA:ARBA00036580};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane protein
CC       {ECO:0000256|RuleBase:RU363063}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000256|ARBA:ARBA00008661, ECO:0000256|RuleBase:RU363063}.
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DR   EMBL; KL206459; KFV82555.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093HST5; -.
DR   STRING; 441894.ENSSCUP00000018830; -.
DR   Proteomes; UP000053584; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008457; F:beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase activity; IEA:RHEA.
DR   GO; GO:0047256; F:lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase activity; IEA:RHEA.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   Gene3D; 3.90.550.50; -; 1.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11214:SF21; LACTOSYLCERAMIDE 1,3-N-ACETYL-BETA-D-GLUCOSAMINYLTRANSFERASE; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363063};
KW   Golgi apparatus {ECO:0000256|RuleBase:RU363063};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW   ECO:0000256|RuleBase:RU363063};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFV82555.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU363063};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363063}.
FT   TRANSMEM        15..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363063"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV82555.1"
FT   NON_TER         380
FT                   /evidence="ECO:0000313|EMBL:KFV82555.1"
SQ   SEQUENCE   380 AA;  44416 MW;  441908AE62415C33 CRC64;
     IRMFVSPRRV RKCQFLQIFA TCFILCLMIF WGPFDNHIVS HMKSYSYRYL INSYNFVNNS
     LSVNRDNLDR VASYQYLINH KEKCQQQDVL LLLFVKTSPE NRHRRDAIRH TWGNEKYVRS
     QLNATIKTVF ALGRPADHPQ RAQLQKKLQL EDQKYNDLIQ QDFLDTFHNL TLKLLLQFSW
     VNAYCPHAKF IMSADDDIFI HMPNLVAYLQ SLAQMGVQDL WIGRVHRGSP PVRDKTSKYY
     VPYEMYQWPS YPDYTAGAAY VISNDVAAKV YEASQTLNTS LYIDDVFMGL CANKMGIVPQ
     YHVFFSGEGK APYHPCIYNK MMTSHGHVDD LHQLWKQATD PKVKRFSSGF FGRIYCKIVN
     IVLLCKLYYE DTYPCSAAFS
//
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