ID   ALG11_PONAB             Reviewed;         492 AA.
AC   Q5R7Z6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase;
DE            EC=2.4.1.131;
DE   AltName: Full=Asparagine-linked glycosylation protein 11 homolog;
DE   AltName: Full=Glycolipid 2-alpha-mannosyltransferase;
GN   Name=ALG11;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mannosyltransferase involved in the last steps of the
CC       synthesis of Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the
CC       cytoplasmic face of the endoplasmic reticulum. Catalyzes the addition
CC       of the 4th and 5th mannose residues to the dolichol-linked
CC       oligosaccharide chain (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=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 + 2 GDP-alpha-
CC         D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC         [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC         GlcNAc-diphosphodolichol + 2 GDP + 2 H(+); Xref=Rhea:RHEA:29523,
CC         Rhea:RHEA-COMP:12626, Rhea:RHEA-COMP:12627, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132511,
CC         ChEBI:CHEBI:132515; EC=2.4.1.131;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH92114.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAH92114.1; Type=Frameshift; Note=Inferred by homology to human genome.; Evidence={ECO:0000305};
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DR   EMBL; CR859960; CAH92114.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001126235.1; NM_001132763.1.
DR   AlphaFoldDB; Q5R7Z6; -.
DR   SMR; Q5R7Z6; -.
DR   STRING; 9601.ENSPPYP00000006134; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   GeneID; 100173205; -.
DR   KEGG; pon:100173205; -.
DR   CTD; 440138; -.
DR   eggNOG; KOG1387; Eukaryota.
DR   InParanoid; Q5R7Z6; -.
DR   Proteomes; UP000001595; Unplaced.
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:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03806; GT4_ALG11-like; 1.
DR   InterPro; IPR038013; ALG11.
DR   InterPro; IPR031814; ALG11_N.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   PANTHER; PTHR45919; PTHR45919; 1.
DR   Pfam; PF15924; ALG11_N; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..492
FT                   /note="GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-
FT                   mannosyltransferase"
FT                   /id="PRO_0000295618"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        273
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   492 AA;  55685 MW;  A57B4723030DD751 CRC64;
     MAAGERSWCL CKLLRFFYSL FFPGLIVCGT LCVCLVIVLW GIRLLLQRKK KLVSTSKNGK
     NQMVIAFFHP YCNAGGGGER VLWCALRALQ KKYPEAVYVV YTGDVNVNGQ QILEGAFRRF
     NIRLIHPVQF VFLRKRYLVE DSLYPHFTLL GQSLGSIFLG WEALMQCVPD VYIDSMGYAF
     TLPLFKYIGG CQVGSYVHYP TISTDMLSVV KNQNIGFNNA AFITRNPFLS KVKLIYYYLF
     AFIYGLVGSC SDVVMVNSSW TLNHILSLWK VGNCTNIVYP PCDVQTFLDI PLHEKKMTPG
     HLLVSVGQFR PEKNHPLQIR AFAKLLNKKM VESPPSLKLV FIGGCRNKDD ELRVNQLRRL
     SEDLGVQEYV EFKINIPFDE LKNYLSEATI GLHTMWNEHF GIGVVECMAA GTIILAHNSG
     GPKLDIVVPH EGDITGFLAE SEEDYAETIA HILSMSAEKR LQIRKSARAS VSRFSDQEFE
     VTFLSSVEKL FK