ID A0A401H3A9_9APHY Unreviewed; 1597 AA.
AC A0A401H3A9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=UDP-glucose:glycoprotein {ECO:0000313|EMBL:GBE88925.1};
GN ORFNames=SCP_1403330 {ECO:0000313|EMBL:GBE88925.1};
OS Sparassis crispa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Sparassidaceae; Sparassis.
OX NCBI_TaxID=139825 {ECO:0000313|EMBL:GBE88925.1, ECO:0000313|Proteomes:UP000287166};
RN [1] {ECO:0000313|EMBL:GBE88925.1, ECO:0000313|Proteomes:UP000287166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30375506; DOI=10.1038/s41598-018-34415-6;
RA Kiyama R., Furutani Y., Kawaguchi K., Nakanishi T.;
RT "Genome sequence of the cauliflower mushroom Sparassis crispa
RT (Hanabiratake) and its association with beneficial usage.";
RL Sci. Rep. 8:16053-16053(2018).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC {ECO:0000256|ARBA:ARBA00006351}.
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:GBE88925.1}.
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DR EMBL; BFAD01000014; GBE88925.1; -; Genomic_DNA.
DR STRING; 139825.A0A401H3A9; -.
DR InParanoid; A0A401H3A9; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000287166; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd06432; GT8_HUGT1_C_like; 1.
DR InterPro; IPR040497; Glyco_transf_24.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR InterPro; IPR040693; UGGT_TRXL_1.
DR InterPro; IPR040694; UGGT_TRXL_2.
DR InterPro; IPR040692; UGGT_TRXL_3.
DR InterPro; IPR040525; UGGT_TRXL_4.
DR PANTHER; PTHR11226; UDP-GLUCOSE GLYCOPROTEIN:GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11226:SF0; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF18404; Glyco_transf_24; 1.
DR Pfam; PF18400; Thioredoxin_12; 1.
DR Pfam; PF18401; Thioredoxin_13; 1.
DR Pfam; PF18402; Thioredoxin_14; 1.
DR Pfam; PF18403; Thioredoxin_15; 1.
DR Pfam; PF06427; UDP-g_GGTase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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:UP000287166};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1597
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019248045"
FT DOMAIN 36..243
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 309..437
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 445..707
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 721..948
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1277..1542
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 1572..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1597 AA; 178180 MW; E4CA4DC6B04A791D CRC64;
MKAPLSFASL ITLLFVYKSY ALNPPVKVEL RSSWPAPPVL LECIEAIATE NDEAFFPLLD
TLTNPEVPIP SPHTPEVVHR SAFEAAISEG FLSRPGEYAS VQMDLALHTA TPKIEAVYQY
YTDRHAARTA SVHNDDCGSW VDWYGQVACD VQTLVHLAGV ETIDPAVPST VNASFPRPKL
LPFDHVQPSP ARVLARPPRT AIFYASLSSS NFRELHSYLY ATSSAPNPHI EYVFRAIPPE
NRDLSLRTYL SGYGVALDLK KMDYLALDDR RQGSSGQTAE SDGAVESISD VDSVMVLVQQ
YPANTDVNAS TPLTDDELLN IGLQATQLIY DADEPLPALK QLSQNFPKYA APLARRITVD
PALLDEVEEN QVKVPGGANI AWLNGVNIGE KDMNPFALLR LLRKERGTML SLTSLGLSPE
QAIRLLTHPS ISAAQSEPDA VSELFDASDR PEEGGVIVWW NDLEKDSRYA RWSRSLRILL
RPMYPGQFPN VKANLFNVVL AVDLSQSSSL HFISTSVSNI ISRSFPARFG IVPIVETEEG
ARMARLFYYL IENFGRAKTM SFLKSLSQID IPIQRLTPTV NWGLVRSEFG NLLTESKQPG
EGVITNLDTI LHGGTESPGF GLDKARAYAA RLGVTLTSAS QGHAFVNGKH LVLNDDFLRQ
LQLELGQQLQ YLQEQIATGH LRDNDIETIS TYFYDLPTTA KRRNTYIHTG KSGMNMINLP
DLLSRVKYPS GSFVYPSDLE QIPLSAYIVA DFDTDGGRTL MKEALISTKV GSASRVSFIH
NPATPWSAST RRPPTSSLLA HLITKDTLHR VSPSRLLKVL GLSEPSVPIH SPQVVISPEG
SLDDILGGTL LEDAGQETYE DFVQASRLLV RELGLAAGEQ AVIVNGRVVG PLLPGGFVAE
DFETLMTYEL RKRVEPVVEA LENIFGSLES FDRGSYAEMV ALTSSVVSAI QVPDPSEVGL
FNAPYKPRKL SYQLLSGKYT SFMFGENSTA LFHFGIVVDP LSESAQKWSS LIEWLLNIPE
VFVELHINPA RYRELPLRRF YRYNLQPRLL YDDNGEEIRA ETEFSGLAVE PIYTLAMDVP
QSWLVRPREA LHDLDNIQLS TLSARDRAHG VHAIFELDYL VIEGHARDVL TSAPPRGVQL
QLATSQGVPI ADTLVVANLG YLQFRTKPGV FKLEIRPGRG REIFKMESVG NEGWDSPHVD
VDGDEITLTN FEGLTLYPRL ARLPGMDRAD VLAEAPPKAP TAKEVLEDIV SWVSSLFSSS
KGSENNTLSS PSDQADINIF TVASGLLYER FVSIMVLSVL RNTNSTVKFW FIENFLSPSF
LEFIPHLAEA YGFKYELVTY KWPSWLRAQK EKQRIIWAYK ILFLDVLFPM DLKKVIFVDA
DQIVRADLKE LVDLDLHGAP YGYTPMGDDN EEMEGFRFWK TGYWKEFLRG LPYHISALYV
VDLVRFRQIA AGDILRGHYQ QLSADPNSLA NLDQDLPNNL QREVPIFSLP EDWLWCETWC
SKDRLNRAKT IDLCQNPLTK EPKLARARHI PEWEEYDSEI ARFARRLAEE GCIRSEIVAA
DSNVLADAGA EHRTHGTAVD KQSEGVEGKA EYVRDEL
//
