ID   UGGG_DICDI              Reviewed;        1681 AA.
AC   Q8T191; Q555Q8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 2.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Probable UDP-glucose:glycoprotein glucosyltransferase A;
DE            EC=2.4.1.-;
DE   AltName: Full=Developmental gene 1109 protein;
DE   Flags: Precursor;
GN   Name=ggtA; Synonyms=DG1109; ORFNames=DDB_G0274103;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15352238; DOI=10.1002/pmic.200300788;
RA   Secko D.M., Insall R.H., Spiegelman G.B., Weeks G.;
RT   "The identification of Dictyostelium phosphoproteins altered in response to
RT   the activation of RasG.";
RL   Proteomics 4:2629-2639(2004).
CC   -!- FUNCTION: Recognizes glycoproteins with minor folding defects.
CC       Reglucosylates single N-glycans near the misfolded part of the protein,
CC       thus providing quality control for protein folding in the endoplasmic
CC       reticulum (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Endoplasmic
CC       reticulum-Golgi intermediate compartment {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR   EMBL; AAFI02000012; EAL69944.1; -; Genomic_DNA.
DR   RefSeq; XP_644005.1; XM_638913.1.
DR   AlphaFoldDB; Q8T191; -.
DR   SMR; Q8T191; -.
DR   STRING; 44689.DDB0220030; -.
DR   CAZy; GT24; Glycosyltransferase Family 24.
DR   PaxDb; Q8T191; -.
DR   EnsemblProtists; EAL69944; EAL69944; DDB_G0274103.
DR   GeneID; 8619433; -.
DR   KEGG; ddi:DDB_G0274103; -.
DR   dictyBase; DDB_G0274103; ggtA.
DR   eggNOG; KOG1879; Eukaryota.
DR   HOGENOM; CLU_002668_1_0_1; -.
DR   InParanoid; Q8T191; -.
DR   OMA; EFAIDIR; -.
DR   PhylomeDB; Q8T191; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q8T191; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR   GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR   Gene3D; 3.90.550.10; -; 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   PANTHER; PTHR11226; PTHR11226; 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; PF06427; UDP-g_GGTase; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW   Reference proteome; Signal; Transferase.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..1681
FT                   /note="Probable UDP-glucose:glycoprotein
FT                   glucosyltransferase A"
FT                   /id="PRO_0000327469"
FT   REGION          566..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1346..1657
FT                   /note="Glucosyltransferase"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        391
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1681 AA;  192629 MW;  946F082CE2E58B18 CRC64;
     MARIFKFFVF LLIVFISNVL LLVESNEGDN SFSSKSIQLS LVSNWGETPS YLEAAEFLHN
     QDKSLFWKFI EEFNKIDFST NYSDKIYYES TISLMKSVLS SNTQFLSEFL SIDLAMRTYS
     PRVETYRQLA ISNMKLNNIE HSITTADNKT ITLFNSGGWV QIKNKIITDV NEINESLFKD
     VAVVDDEENE FIRLYDFDHI FPTLANTVSS SSSSPSSIPI VILYVDIKSE FFKLVHPKLK
     QFSQMGKIKY CLRYVVQESN QKLNLQGYGY ELSIKNLEYK VMDDSAIKKD IIIDGVKSKT
     IINIPNEDVQ GFNFHKLQKR KPELTSKLST FRSYLMAKSQ EAKELKVWEL KDLGIQSAQK
     IIQSGDPLRS LEYISQKFPT LSNSLSKITL NESLKSVIES NQKIIPSTTD QTLLLNGRLI
     DTNELSPIEL SRIILEEYEH STTIQQQGPL SSKTVQDIIS AQLPIRIQLL PTKEELELNG
     GNEPFVSLNN LELDYIYRQW EPKLQSSVLD KPVTSPQDIF IRKNLLTTVI VLDWNNINTF
     EIIPEIQEMV QGNSLIPTRI QLLFNTKSNN NNNNNNNNND QNSQTSNFIQ GKDLAKVFLT
     IKNSNLGNRG AFFFITALNY FKKMYIPNEL GITRSVLSSS FQAVLQQMGG SVRSLQHALT
     NTDFDNLLES SNQLIERLEL LDTTTSQSTT TTTTTKILPK VFVNGVQVKY SNIDQLSFDL
     LVSLYDEFDN LKPLFKESIL STTTAQYYET ILTSSYWKDN NLPFLKKLNS MISNEKYSHL
     ITNSKNRNQE VDAQNVLKNL LYFRNNENKD EQNLLNLIVI GDFDHYNTRD ISLELLRQLE
     KGELKNCKLT FISNPIDINS VVNTAGNENQ ILGKLITILK HYGKILTPQL VIGLFEKVQS
     DPTIIDSFKT MKQIIELSGF DIAANDIWVA QSVNLFKQSS KVCKQYLGIQ STNKSPLSIL
     VNGRIITPPL SYDDAASFIQ SDFKLLLEIE MIKAKKTFEL LNSDPILKDK SNLKISDLLN
     KVQSLVGYYY NGNNQLDSNI KRKRIPNSLS ISFSHKPPTL SSSSSSSSSN SNDVPLKFLM
     IINPFNKVSQ KLVPMVREFS NKLNIPVDVI LNPPVSLSEL PLKTYYTYVI KLSSEFNNEN
     VLYNQPLGIA TDIPEDRVVT LALDIPSSWL VQPIIAKYDL DNIRLKDLGD EQVLTAVYEL
     ENIVIEGSAN DMTTDNAPAG LELLLNPIST QTNKTQDTIV MNNFGYYQLK SNPGIWKLTI
     APGRSSDIMD MVDHPNQKEK ETFVIVPHRL VVIDSLYQSL SSLSVVRKAG QELRPILQPI
     DEYEKQKEQE KEQKLKQNSS GFFSNLFSSK NDATDSVATH QKKSNLDTIH IFSVASGHLY
     ERFLKIMMLS VVKNTESPIK FWFLKNYLSP AFKEFIPEMA KEYGFQYELV TYKWPWWLRK
     QTEKQRIIWS YKILFLDVLF PLDVPKIIFV DADQVVRTDL KELWDMDLHG ASLGYTPFCD
     SNKDTEGFRF WKSGYWRQHL AGRSYHISAL YVVDLVRFRR LAAGDQLRAT YDQLSRDPNS
     LANLDQDLPN YLQHYVRIHS LPQEWLWCET WCDQESKSKA KTIDLCNNPL TKTPKLENAV
     RIIDEWTTLD NEAKEFELKI DQSKHHRQIE LDHQNQLPNS KPIENIDDIL LNLAESQKDL
     F