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Database: UniProt
Entry: A0A3L8SU89_CHLGU
LinkDB: A0A3L8SU89_CHLGU
Original site: A0A3L8SU89_CHLGU 
ID   A0A3L8SU89_CHLGU        Unreviewed;       475 AA.
AC   A0A3L8SU89;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Glycosyl transferase CAP10 domain-containing protein {ECO:0000259|SMART:SM00672};
GN   ORFNames=DV515_00003319 {ECO:0000313|EMBL:RLW08408.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW08408.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLW08408.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLW08408.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLW08408.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[EGF-like domain protein] + UDP-alpha-D-glucose = 3-O-
CC         (beta-D-glucosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP;
CC         Xref=Rhea:RHEA:58116, Rhea:RHEA-COMP:14610, Rhea:RHEA-COMP:16010,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885, ChEBI:CHEBI:140576;
CC         Evidence={ECO:0000256|ARBA:ARBA00000570};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[EGF-like domain protein] + UDP-alpha-D-xylose = 3-O-
CC         (beta-D-xylosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP;
CC         Xref=Rhea:RHEA:62016, Rhea:RHEA-COMP:16010, Rhea:RHEA-COMP:16011,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57632,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:132085;
CC         Evidence={ECO:0000256|ARBA:ARBA00000273};
CC   -!- SIMILARITY: Belongs to the KDELC family.
CC       {ECO:0000256|ARBA:ARBA00006063}.
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:RLW08408.1}.
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DR   EMBL; QUSF01000006; RLW08408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8SU89; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR006598; CAP10.
DR   InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR   InterPro; IPR001298; Filamin/ABP280_rpt.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR12203; KDEL LYS-ASP-GLU-LEU CONTAINING - RELATED; 1.
DR   PANTHER; PTHR12203:SF18; PROTEIN O-GLUCOSYLTRANSFERASE 3; 1.
DR   Pfam; PF00630; Filamin; 1.
DR   Pfam; PF05686; Glyco_transf_90; 1.
DR   SMART; SM00672; CAP10; 1.
DR   SMART; SM00557; IG_FLMN; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   PROSITE; PS50194; FILAMIN_REPEAT; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..475
FT                   /note="Glycosyl transferase CAP10 domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018224791"
FT   REPEAT          24..134
FT                   /note="Filamin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT   DOMAIN          217..443
FT                   /note="Glycosyl transferase CAP10"
FT                   /evidence="ECO:0000259|SMART:SM00672"
FT   REGION          451..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  55142 MW;  6DEB2EEBA37DC20D CRC64;
     MGSCGLLLLL LLGAAGPLLQ AEPAEPVSAE RSLAWGPGLE AGIAVPVRYF YIQAVSAAGR
     NFSRSPPGIK QFKVVIKALS PKEVTRIYTP RPLDRNDGTF LMRYRMYGSV TKGLKIEIFY
     GDQHVAQSPY ILKEPVYHEY CDCPEEDPEV WQDMMSCPSQ EPQITEDFIS FPTIDLQRML
     KEIPAKFSQA RGAIVHYTIR DNHIYRRSLG KYTDFKMFSD EMFVFLTWSF ISMLETGQLS
     IGKLMIHLGL YLSSPGVALW IPEISSCRRP FWENKTEKAL FRGRDSREER LHLVKLSKEN
     PELLDAGITG YFFFREKEKE LGKAQLMGFF DFFKYKYQVN IDGTVAAYRF PYLLLGDSLV
     LKQDSQYYEH FYIGLKPWKH YVPVKRNLED LLEKIKWAKE NDEEARKIAK EGQLTARELL
     QPHRFYCYYY KVLQKYAERQ ASKPEIRDGM ELVPQPDDRD SVCSCHRKKP LREDL
//
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