GenomeNet

Database: UniProt
Entry: C4WX87_ACYPI
LinkDB: C4WX87_ACYPI
Original site: C4WX87_ACYPI 
ID   C4WX87_ACYPI            Unreviewed;       396 AA.
AC   C4WX87;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
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=ACYPI005896 {ECO:0000313|EMBL:BAH72507.1};
GN   Synonyms=100164916 {ECO:0000313|EnsemblMetazoa:NP_001155645.1};
OS   Acyrthosiphon pisum (Pea aphid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC   Aphidoidea; Aphididae; Macrosiphini; Acyrthosiphon.
OX   NCBI_TaxID=7029 {ECO:0000313|EMBL:BAH72507.1};
RN   [1] {ECO:0000313|EMBL:BAH72507.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LSR1 {ECO:0000313|EMBL:BAH72507.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:BAH72507.1};
RA   Shigenobu S., Nakabachi A., Richards S.;
RT   "A full-length cDNA resource of the pea aphid, Acyrthosiphon pisum.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSR1 {ECO:0000313|Proteomes:UP000007819};
RA   Jiang H., Abraham K., Ali S., Alsbrooks S.L., Anim B.N., Anosike U.S.,
RA   Attaway T., Bandaranaike D.P., Battles P.K., Bell S.N., Bell A.V.,
RA   Beltran B., Bickham C., Bustamante Y., Caleb T., Canada A., Cardenas V.,
RA   Carter K., Chacko J., Chandrabose M.N., Chavez D., Chavez A., Chen L.,
RA   Chu H.-S., Claassen K.J., Cockrell R., Collins M., Cooper J.A., Cree A.,
RA   Curry S.M., Da Y., Dao M.D., Das B., Davila M.-L., Davy-Carroll L.,
RA   Denson S., Dinh H., Ebong V.E., Edwards J.R., Egan A., El-Daye J.,
RA   Escobedo L., Fernandez S., Fernando P.R., Flagg N., Forbes L.D.,
RA   Fowler R.G., Fu Q., Gabisi R.A., Ganer J., Garbino Pronczuk A.,
RA   Garcia R.M., Garner T., Garrett T.E., Gonzalez D.A., Hamid H.,
RA   Hawkins E.S., Hirani K., Hogues M.E., Hollins B., Hsiao C.-H., Jabil R.,
RA   James M.L., Jhangiani S.N., Johnson B., Johnson Q., Joshi V., Kalu J.B.,
RA   Kam C., Kashfia A., Keebler J., Kisamo H., Kovar C.L., Lago L.A.,
RA   Lai C.-Y., Laidlaw J., Lara F., Le T.-K., Lee S.L., Legall F.H.,
RA   Lemon S.J., Lewis L.R., Li B., Liu Y., Liu Y.-S., Lopez J., Lozado R.J.,
RA   Lu J., Madu R.C., Maheshwari M., Maheshwari R., Malloy K., Martinez E.,
RA   Mathew T., Mercado I.C., Mercado C., Meyer B., Montgomery K., Morgan M.B.,
RA   Munidasa M., Nazareth L.V., Nelson J., Ng B.M., Nguyen N.B., Nguyen P.Q.,
RA   Nguyen T., Obregon M., Okwuonu G.O., Onwere C.G., Orozco G., Parra A.,
RA   Patel S., Patil S., Perez A., Perez Y., Pham C., Primus E.L., Pu L.-L.,
RA   Puazo M., Qin X., Quiroz J.B., Reese J., Richards S., Rives C.M.,
RA   Robberts R., Ruiz S.J., Ruiz M.J., Santibanez J., Schneider B.W.,
RA   Sisson I., Smith M., Sodergren E., Song X.-Z., Song B.B., Summersgill H.,
RA   Thelus R., Thornton R.D., Trejos Z.Y., Usmani K., Vattathil S.,
RA   Villasana D., Walker D.L., Wang S., Wang K., White C.S., Williams A.C.,
RA   Williamson J., Wilson K., Woghiren I.O., Woodworth J.R., Worley K.C.,
RA   Wright R.A., Wu W., Young L., Zhang L., Zhang J., Zhu Y., Muzny D.M.,
RA   Weinstock G., Gibbs R.A.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:NP_001155645.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2022) 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; AK342507; BAH72507.1; -; mRNA.
DR   RefSeq; NP_001155645.1; NM_001162173.2.
DR   AlphaFoldDB; C4WX87; -.
DR   STRING; 7029.C4WX87; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblMetazoa; NM_001162173.2; NP_001155645.1; LOC100164916.
DR   GeneID; 100164916; -.
DR   KEGG; api:100164916; -.
DR   eggNOG; KOG0853; Eukaryota.
DR   HOGENOM; CLU_030619_1_0_1; -.
DR   InParanoid; C4WX87; -.
DR   OMA; ENVQYHR; -.
DR   OrthoDB; 1377at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000007819; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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; PF13439; Glyco_transf_4; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU367136};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007819};
KW   Transferase {ECO:0000256|RuleBase:RU367136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          14..190
FT                   /note="Glycosyltransferase subfamily 4-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13439"
FT   DOMAIN          207..371
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
SQ   SEQUENCE   396 AA;  44987 MW;  31C140096E8D2CC6 CRC64;
     MKLNVVFLHP DLGIGGAERL VVDAAVAMKQ SGHAVRFVTN HHSVSHCFEE TRDGTLPVTV
     VGDWLPRTVF GKCYALCSYA RMVYAALYLT FFSSINPDVV FVDQISACIP ILNWMPCKVL
     FYCHYPDQLL AAHDDALKRY YRLPLDWLEE KTTACAHMIL VNSNFTLDIF RSTFKSIKTL
     PTVVYPSINT VFFDNTETVQ LKDLINVENC KYILSINRFE RKKNLGLAIH SFSMLSDKKI
     KLVLAGGYDP LNLENIEYFH ELVSLVQDMK LNERVIFLKS PSDAIKISLL RHCLCLVYTP
     SFEHFGIVPL EAMYCCKPVV AVNNGGPKET IENDHNGYLR NAEPEDFADA IKQLVEIEGK
     AELFGNHGKK RFDDIFSFGA FKNKIDSILE NVYKTE
//
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