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Database: UniProt
Entry: U3JFA8_FICAL
LinkDB: U3JFA8_FICAL
Original site: U3JFA8_FICAL 
ID   U3JFA8_FICAL            Unreviewed;       370 AA.
AC   U3JFA8;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Hexosyltransferase {ECO:0000256|RuleBase:RU363063};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363063};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000001462.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000001462.2, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000001462.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a globoside Gb3Cer (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC         galactosamine = a globoside Gb4Cer (d18:1(4E)) + H(+) + UDP;
CC         Xref=Rhea:RHEA:22252, ChEBI:CHEBI:15378, ChEBI:CHEBI:18259,
CC         ChEBI:CHEBI:18313, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.79;
CC         Evidence={ECO:0000256|ARBA:ARBA00043819};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22253;
CC         Evidence={ECO:0000256|ARBA:ARBA00043819};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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   AlphaFoldDB; U3JFA8; -.
DR   STRING; 59894.ENSFALP00000001462; -.
DR   Ensembl; ENSFALT00000001471.2; ENSFALP00000001462.2; ENSFALG00000001402.2.
DR   eggNOG; KOG2287; Eukaryota.
DR   GeneTree; ENSGT00940000162252; -.
DR   HOGENOM; CLU_036849_2_4_1; -.
DR   Proteomes; UP000016665; Chromosome 9.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047273; F:galactosylgalactosylglucosylceramide beta-D-acetylgalactosaminyltransferase 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:SF153; UDP-GALNAC:BETA-1,3-N-ACETYLGALACTOSAMINYLTRANSFERASE 1; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   REGION          67..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..105
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   370 AA;  41481 MW;  E1332DF1D317AB58 CRC64;
     GTPAPPDHDS GSDRRPVREA LAVDFPAAAA LFPAHHVVRH PLLQGRPGEP QPALLLRVRA
     RLPAGAAVRA ARAPPLRPPP PPPPPPPPPP PPPPPPPPPP PPPPLRERRR CAEARPFLVI
     LVASSPGELR ARQAIRVSWG SRGSWWGQRV LTLFLLGRAG RGERGPAALS VEDESVLYGD
     IIRQDFLDTY DNLTLKTIMA FQWFSEFCPG ARFFMKTDVD VFINTPNLVK LLLRLNSSEN
     VFTGFPLIQN FAYRGFDRKR FISYEEYPFR LYPPYCSGLG YILDGKLALR VYELMGHVKP
     LKFEDVYVGI CLNLLKVNVT LPEDAEQYFL YKIDFDICKY RHLIAVHGLT SSELVQFWQD
     LSSDTSKTCL
//
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