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ALG1_DICDI
ID   ALG1_DICDI              Reviewed;         493 AA.
AC   P90522; Q54MD7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase;
DE            EC=2.4.1.142;
DE   AltName: Full=Asparagine-linked glycosylation protein 1 homolog;
DE   AltName: Full=Beta-1,4-mannosyltransferase;
DE   AltName: Full=GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase;
DE   AltName: Full=GDP-mannose-dolichol diphosphochitobiose mannosyltransferase;
GN   Name=alg1; Synonyms=mntA; ORFNames=DDB_G0286011;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=AX4;
RX   PubMed=9434191; DOI=10.1016/s0378-1119(97)00553-2;
RA   Lee S.-K., Li G., Yu S.-L., Alexander H., Alexander S.;
RT   "The Dictyostelium discoideum beta-1,4-mannosyltransferase gene, mntA, has
RT   two periods of developmental expression.";
RL   Gene 204:251-258(1997).
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).
CC   -!- FUNCTION: Participates in the formation of the lipid-linked precursor
CC       oligosaccharide for N-glycosylation. Involved in assembling the
CC       dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic
CC       surface of the ER.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl
CC         diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC         GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:13865,
CC         Rhea:RHEA-COMP:9520, Rhea:RHEA-COMP:11044, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57269, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:58472; EC=2.4.1.142;
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type II membrane protein {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: In bacterially grown celles expressed at 2 hours
CC       and 12 hours of development. In axenically grown cells expressed at 2
CC       hours and 8/9 hours of development. {ECO:0000269|PubMed:9434191}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 33 subfamily. {ECO:0000305}.
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DR   EMBL; U65018; AAC47828.1; -; Genomic_DNA.
DR   EMBL; AAFI02000085; EAL64384.1; -; Genomic_DNA.
DR   RefSeq; XP_637897.1; XM_632805.1.
DR   AlphaFoldDB; P90522; -.
DR   STRING; 44689.DDB0191150; -.
DR   CAZy; GT33; Glycosyltransferase Family 33.
DR   PaxDb; P90522; -.
DR   PRIDE; P90522; -.
DR   EnsemblProtists; EAL64384; EAL64384; DDB_G0286011.
DR   GeneID; 8625407; -.
DR   KEGG; ddi:DDB_G0286011; -.
DR   dictyBase; DDB_G0286011; alg1.
DR   eggNOG; KOG2941; Eukaryota.
DR   HOGENOM; CLU_012079_0_0_1; -.
DR   InParanoid; P90522; -.
DR   OMA; PLKVLWQ; -.
DR   PhylomeDB; P90522; -.
DR   Reactome; R-DDI-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:P90522; -.
DR   Proteomes; UP000002195; Chromosome 4.
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:0005811; C:lipid droplet; HDA:dictyBase.
DR   GO; GO:0004578; F:chitobiosyldiphosphodolichol beta-mannosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR   InterPro; IPR026051; ALG1-like.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   PANTHER; PTHR13036; PTHR13036; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..493
FT                   /note="Chitobiosyldiphosphodolichol beta-
FT                   mannosyltransferase"
FT                   /id="PRO_0000326038"
FT   TOPO_DOM        1..71
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..493
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          462..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   493 AA;  56010 MW;  86279C007578BC02 CRC64;
     MNRVAVVVLG DIGRSPRMQY HSMSLSKLEN TKVTLIGYRE SEPHPQIVNN DSITIEPLKP
     FPISMSNSFK KIPLISIFMW PLLAICKVLF QIIQLMYVLL VKVPSPLNTI LVQSPPAIPT
     IFVMQIVCWI RGVHLVIDWH NLGYTLLKLS LSKSDNHPII RLAKFIERYF AKNAYAHLFV
     TNEMKIQLVR DWNLKGKTFV FHDKASPIFK SLTDREQEEF LKTFINKYSI KGEDKVYIES
     VISKKSIRNP KQQTSIIISS TSWTQDEDFS ILLDAIVKYD IEHAINNNNN KVEEAQDESV
     VLAENLLFII TGKGPQKEYY QEKINSLSLK KSRIITVWLD SEDYPKLLAC CDLGVSLHNS
     SSGIDLPMKV VDMFGCCLPV LAIDFKCIGE LVKVNYNGFL FKDSDQLHQL LNQLFTHPTN
     NNTITNTNNN KNLILEKMRK NLTKDRETDT WESNWLTIKP LFIPSSSSSS SSSSSSSSSS
     SSSSSSNSKS KKD
 
 
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