UniProt: H2PSW0

Database: UniProt
Entry: H2PSW0_PONAB

LinkDB:  H2PSW0_PONAB 
Original site:  H2PSW0_PONAB

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Ontology (10)   
   GO (10)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (3)   
   Pfam (2)   
All databases (24)   

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ID   H2PSW0_PONAB            Unreviewed;       416 AA.
AC   H2PSW0; A0A2J8WSI5; A0A663DGW5;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Alpha-1,3/1,6-mannosyltransferase ALG2 {ECO:0000256|RuleBase:RU367136};
DE            EC=2.4.1.132 {ECO:0000256|RuleBase:RU367136};
DE            EC=2.4.1.257 {ECO:0000256|RuleBase:RU367136};
DE   AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase {ECO:0000256|RuleBase:RU367136};
GN   Name=ALG2 {ECO:0000313|Ensembl:ENSPPYP00000021784.1};
GN   ORFNames=CR201_G0008216 {ECO:0000313|EMBL:PNJ72720.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000021784.1, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000021784.1, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ72720.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ72720.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000021784.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and
CC       Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol
CC       diphosphate. {ECO:0000256|ARBA:ARBA00003142,
CC       ECO:0000256|RuleBase:RU367136}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC         alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-
CC         (1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC         alpha-D-GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:29519,
CC         Rhea:RHEA-COMP:12624, Rhea:RHEA-COMP:12626, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132510,
CC         ChEBI:CHEBI:132511; EC=2.4.1.257;
CC         Evidence={ECO:0000256|ARBA:ARBA00001514,
CC         ECO:0000256|RuleBase:RU367136};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC         diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-
CC         Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol +
CC         GDP + H(+); Xref=Rhea:RHEA:29515, Rhea:RHEA-COMP:11044, Rhea:RHEA-
CC         COMP:12624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:58472, ChEBI:CHEBI:132510; EC=2.4.1.132;
CC         Evidence={ECO:0000256|ARBA:ARBA00001253,
CC         ECO:0000256|RuleBase:RU367136};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU367136}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU367136}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000256|RuleBase:RU367136}.
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DR   EMBL; NDHI03003380; PNJ72720.1; -; Genomic_DNA.
DR   RefSeq; XP_002820077.1; XM_002820031.2.
DR   STRING; 9601.ENSPPYP00000021784; -.
DR   Ensembl; ENSPPYT00000022674.2; ENSPPYP00000021784.1; ENSPPYG00000019440.2.
DR   GeneID; 100451740; -.
DR   KEGG; pon:100451740; -.
DR   CTD; 85365; -.
DR   eggNOG; KOG0853; Eukaryota.
DR   GeneTree; ENSGT00550000075033; -.
DR   HOGENOM; CLU_030619_1_0_1; -.
DR   OMA; ENVQYHR; -.
DR   OrthoDB; 1377at2759; -.
DR   TreeFam; TF106000; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001595; Chromosome 9.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0000033; F:alpha-1,3-mannosyltransferase activity; IEA:Ensembl.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0004378; F:GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102704; F:GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR   CDD; cd03805; GT4_ALG2-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR027054; ALG2.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   PANTHER; PTHR45918; ALPHA-1,3/1,6-MANNOSYLTRANSFERASE ALG2; 1.
DR   PANTHER; PTHR45918:SF1; ALPHA-1,3_1,6-MANNOSYLTRANSFERASE ALG2; 1.
DR   Pfam; PF13579; Glyco_trans_4_4; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU367136};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW   Transferase {ECO:0000256|RuleBase:RU367136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          27..184
FT                   /note="Glycosyltransferase subfamily 4-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13579"
FT   DOMAIN          218..391
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
SQ   SEQUENCE   416 AA;  47077 MW;  C2FF63CC6A353373 CRC64;
     MAEEQGRELD PVSKPSVLFL HPDLGVGGAE RLVLDAALAL QARGCSVKIW TAHYDPGHCF
     AESRELPVHC AGDWLPRGLG WGGRGAAVCA YVRMVFLALY VLFLADEEFD VVVCDQVSAC
     IPVFRLARRR KKILFYCHFP DLLLTKRDSF LKRLYRAPID WIEEYTTGMA DCILVNSQFT
     AAVFKETFKS LSHIDPDVLY PSLNVTSFDS VVPEKLDDLV PKGKKFLLLS INRYERKKNL
     TLALEALVQL RGRLTSQDWE KVHLIMAGGY DERVLENVEH YQELKKMVQQ SDLGQYVTFL
     RSFSDKQKIS LLHSCTCVLY TPSNEHFGIV PLEAMYMQCP VIAVNSGGPL ESIDHSVTGF
     LCEPDPVHFS EAIEKFIREP SLKVTMGLAG RARVKEKFSP EAFTEQLYRY VTKQLV
//

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