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Database: UniProt
Entry: Q6CC41_YARLI
LinkDB: Q6CC41_YARLI
Original site: Q6CC41_YARLI 
ID   Q6CC41_YARLI            Unreviewed;      1470 AA.
AC   Q6CC41;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   SubName: Full=YALI0C12661p {ECO:0000313|EMBL:CAG82081.1};
GN   ORFNames=YALI0_C12661g {ECO:0000313|EMBL:CAG82081.1};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG82081.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG82081.1, ECO:0000313|Proteomes:UP000001300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
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DR   EMBL; CR382129; CAG82081.1; -; Genomic_DNA.
DR   RefSeq; XP_501771.1; XM_501771.1.
DR   SMR; Q6CC41; -.
DR   STRING; 284591.Q6CC41; -.
DR   CAZy; GT24; Glycosyltransferase Family 24.
DR   EnsemblFungi; CAG82081; CAG82081; YALI0_C12661g.
DR   GeneID; 2909509; -.
DR   KEGG; yli:YALI0C12661g; -.
DR   VEuPathDB; FungiDB:YALI0_C12661g; -.
DR   HOGENOM; CLU_002668_1_0_1; -.
DR   InParanoid; Q6CC41; -.
DR   OMA; VYETEHE; -.
DR   OrthoDB; 1734at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001300; Chromosome C.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; 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   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   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; PF06427; UDP-g_GGTase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   4: Predicted;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1470
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004271526"
FT   DOMAIN          32..210
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18400"
FT   DOMAIN          249..377
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18401"
FT   DOMAIN          385..611
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18402"
FT   DOMAIN          1164..1432
FT                   /note="Glucosyltransferase 24 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF18404"
FT   REGION          612..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1434..1470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1434..1451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1452..1470
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1470 AA;  165685 MW;  A7B604B70D090617 CRC64;
     MKLLKYAAAA LFASSVAANV TVELKAQWQS DFLLELVETL STEHTYFDFI NHIAEQVEDG
     ANYTDKEWYD NLTAFAASKS EISDFQKSLT DAALAFRRES PLIETFYQLG DSQESECDIF
     FTYNGKKYCD SNDLFTLKTT KMPKNPSVYF FDHVARSVQA NKHLKNIPVT VLYADLRSPE
     FPLFHKILYQ EAQDGKMVYI LRYRRSDRSE RVTMTGYGAE LSLKKTDYLV LDDDANTEKL
     TDNKNPVYTK RELQNMGLNA AQFVLNHRKD PEAALKALKE VSFDFPLLSS SLNNTKPVKG
     FQKALQENTA AGDFMPGANQ MFVNGALLST SASNLQSLFD LVALEHSRLE VLAKTLKGAI
     SAEQLASILN DYPLQHALES QPQRIDYRDA DALLWLNNLA TDIQYQEWPR SVASLLQNQI
     NLAHNAQTVV MPFNMDDFAD VKVDKETGEL INMHPINRGK LTVLFTMLQR SMPIQFGVVP
     YGSTLKGKKL SQYLHYLARN VDATASLRFL FALGAGTPVE EIFTQIPAEI TQESVDEALK
     EESYEPYVTA SREWMKKLGM NEAQTQEPAF VMNGIVMPFS EKWQNLVGAR FQQDLPEMLK
     LVQKQIIKVS KEAPVGEDDE DEDDENAGNP VDKYFANHEI KDLLVEGSPT RRNLILSPAS
     FTNLQYLESD LNLKDVSTAT IAGTTASIFS NSILAGNFAS TQFVSQLLAL IEAQQEEKDR
     FAFRTQFVHI GQTDSAKGQV INGVVQKLTE LAGEEQVSLL KDALAYLEGD NASFSAKKVP
     FDKTITASEE VKYLKQFKTT ESSTLLIIDG LVNDISSKAM LLDKSEVIAL YEREAVRRLE
     LTSVALSDLK LLTKSVENNL DLAKVHIPLA KIFYGDATEQ ESTLYDVRAF HHIRWNKDVS
     SFVLGDESTS LVKIVAAVDV LSDGGQRLVS QIEAISKVTG VSVRVFPSPK APDARQEPTL
     PLKRFYRAHN SVVPEFDAEG AHKVPNLNFE GLPAQNLLTF GLDAPSSWIA MPADNTHDLD
     NILLEEDSED FVDASYSLQN ILIEGSIIDI TKNSYAPGTD LLLKSTLTGE SSDTLVMSNL
     GYFQLQAGPG LWELNLGPSA SDVYETEHEV IIPVTDVLGP HISLSMERKK GKENVVVGAS
     QDKAKLWSKL KKSTGVSTKK QADINIFTVA SGHLYERFLS IMTASVMAHT DHTVKFWLIE
     NFLSASFKAF LPHLAAHYGF EYELVTYQWP HWLRGQTEKQ RQIWGYKILF LDVLFPQDLE
     RVIFIDSDQI VRTDLYELVE MDLEGAPYGF TPMCDSRKEM DGFRFWKQGY WDTFLGDDLV
     YHISALFVVD LKVFRAQQIG DRLRVHYHQL SADPASLSNL DQDLPNNLQR QVPIFSLPQD
     WLWCETWCSD ESLKTAKTID MCNNPLTKEP KLDRARRQVP EWTKYDDEIR KLRKEAEGIE
     GKKKEEEERA GPVEVEVEID EPEADLHDEL
//
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