位置:首页 > 蛋白库 > ALG3_CRYNJ
ALG3_CRYNJ
ID   ALG3_CRYNJ              Reviewed;         447 AA.
AC   P0CN92; Q55M08; Q5K8R1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase;
DE            EC=2.4.1.258;
DE   AltName: Full=Asparagine-linked glycosylation protein 6;
DE   AltName: Full=Dol-P-Man-dependent alpha(1-3)-mannosyltransferase;
DE   AltName: Full=Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase;
GN   Name=ALG3; OrderedLocusNames=CNL04800;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: Adds the first Dol-P-Man derived mannose in an alpha-1,3
CC       linkage to Man(5)GlcNAc(2)-PP-Dol. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC         alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-
CC         Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a
CC         dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC         beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+);
CC         Xref=Rhea:RHEA:29527, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC         Rhea:RHEA-COMP:12627, Rhea:RHEA-COMP:12628, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132515,
CC         ChEBI:CHEBI:132516; EC=2.4.1.258;
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ALG3 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017352; AAW46504.1; -; Genomic_DNA.
DR   RefSeq; XP_568021.1; XM_568021.1.
DR   AlphaFoldDB; P0CN92; -.
DR   STRING; 5207.AAW46504; -.
DR   CAZy; GT58; Glycosyltransferase Family 58.
DR   PaxDb; P0CN92; -.
DR   EnsemblFungi; AAW46504; AAW46504; CNL04800.
DR   GeneID; 3254774; -.
DR   KEGG; cne:CNL04800; -.
DR   VEuPathDB; FungiDB:CNL04800; -.
DR   eggNOG; KOG2762; Eukaryota.
DR   HOGENOM; CLU_035382_3_0_1; -.
DR   InParanoid; P0CN92; -.
DR   OMA; DWETYMI; -.
DR   OrthoDB; 774318at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000002149; Chromosome 12.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0052925; F:dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR   InterPro; IPR007873; Glycosyltransferase_ALG3.
DR   PANTHER; PTHR12646; PTHR12646; 1.
DR   Pfam; PF05208; ALG3; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..447
FT                   /note="Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-
FT                   mannosyltransferase"
FT                   /id="PRO_0000350925"
FT   TOPO_DOM        1..34
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..83
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..118
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..204
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..232
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        254..296
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        318..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        365..379
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..411
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        433..447
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   447 AA;  50713 MW;  5D466EAF24A77013 CRC64;
     MSRQSLFTPA LGQRKGLISH TVDLVRALLF DRRYFWHTAF LLFLGEVALS LLVIWKIPYT
     KIDWPAYMQQ VDMFLAGERD YSKIEGETGP LVYPALHLYI YTAFHRLLPS IENVRPAQFV
     FLGFYLATYL AISTIYYLAG RPSNGGHHFP QVLLIPLTLS KRAHSIFLLR LFNDPIAMLI
     FYLSVIAFQI GGRKGWRLGC VLFSLALGVK MNILNFLPGL LVLLFQYRGI VGTVEGLSII
     GLIQFLLPAP FFFSKSNPYL IRAYFTSAFD FSRQFLYEWT VNWRFISEET FLSRERAVTL
     LAGHLTVLGL FAAFKWSPVP GGTLRVLRKG FSDPLNQALE VSQVPAYHIP LVLFSANLIG
     MLFARSLHYQ FHSWYFHQLP FLLYSGAGWG NMLTSVLIWV TVQYAWETAP STISTSAALL
     AGHGAMVFGL FFHGMKRPSS SQKSKAK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024