ID   ALG3_MOUSE              Reviewed;         438 AA.
AC   Q8K2A8;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 44.
DE   RecName: Full=Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase;
DE            EC=2.4.1.130;
DE   AltName: Full=Dol-P-Man-dependent alpha(1-3)-mannosyltransferase;
DE   AltName: Full=Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase;
DE   AltName: Full=Asparagine-linked glycosylation protein 3;
DE   AltName: Full=Not56-like protein;
GN   Name=Alg3; Synonyms=Not, Not56l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Adds the first Dol-P-Man derived mannose in an alpha-1,3
CC       linkage to Man5GlcNAc2-PP-Dol.
CC   -!- CATALYTIC ACTIVITY: Transfers an alpha-D-mannosyl residue from
CC       dolichyl-phosphate D-mannose into membrane lipid-linked
CC       oligosaccharide.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (Probable).
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 58 family.
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DR   EMBL; BC031893; AAH31893.1; -; mRNA.
DR   IPI; IPI00322103; -.
DR   RefSeq; NP_666051.1; -.
DR   UniGene; Mm.24950; -.
DR   CAZy; GT58; Glycosyltransferase Family 58.
DR   PhosphoSite; Q8K2A8; -.
DR   Ensembl; ENSMUSG00000033809; Mus musculus.
DR   GeneID; 208624; -.
DR   KEGG; mmu:208624; -.
DR   MGI; MGI:1098592; Alg3.
DR   HOGENOM; Q8K2A8; -.
DR   HOVERGEN; Q8K2A8; -.
DR   BRENDA; 2.4.1.130; 244.
DR   NextBio; 372337; -.
DR   Bgee; Q8K2A8; -.
DR   GermOnline; ENSMUSG00000033809; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004584; F:dolichyl-phosphate-mannose-glycolipid alpha...; IEA:EC.
DR   InterPro; IPR007873; Glycosyltransferase_ALG3.
DR   PANTHER; PTHR12646; ALG3; 1.
DR   Pfam; PF05208; ALG3; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycosyltransferase; Membrane; Phosphoprotein;
KW   Transferase; Transmembrane.
FT   CHAIN         1    438       Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-
FT                                dolichyl mannosyltransferase.
FT                                /FTId=PRO_0000080567.
FT   TRANSMEM     41     61       Potential.
FT   TRANSMEM     95    115       Potential.
FT   TRANSMEM    123    143       Potential.
FT   TRANSMEM    149    169       Potential.
FT   TRANSMEM    172    192       Potential.
FT   TRANSMEM    203    223       Potential.
FT   TRANSMEM    231    251       Potential.
FT   TRANSMEM    289    309       Potential.
FT   TRANSMEM    332    352       Potential.
FT   TRANSMEM    356    376       Potential.
FT   TRANSMEM    407    427       Potential.
FT   MOD_RES      13     13       Phosphoserine (By similarity).
SQ   SEQUENCE   438 AA;  50166 MW;  99297B2F51F6330F CRC64;
     MAAGLRKRGQ PASVGQPAGI WKQWLQRAWQ ERYLLLREPR YTLLVASCLC IAEVGITFWV
     IHRVAYTEID WKAYMAQVEG FINGTYDYTQ LQGDTGPLVY PAGFLYIFTG LFYATDRGTD
     IPMAQNIFAV LYLVTLVLVF LIYHQTSKVP PFVFFFMCCA SYRVHSIFVL RLFNDPVAMA
     LLFLSINLFL AQCWSWGCCC FSLAVSVKMN VLLFAPGLLF LLLTQFGFRG ALPKLAICAA
     LQVVLGLPFL LENPIGYLSR SFDLGRQFLF QWTVNWRFLP ETIFLHRAFH LALLAAHLSL
     LLLFALCRWH RTGESILALL KDPSKRKVPP QALTPNQIVS ILFTSNFIGI CFSHSLHYQF
     YVWYFHTLPY LLWAMPARWL THLLRLLVLG LIELSWNTYP STSFSSAALH LCHAVVLLQL
     WLSPESFPKS IQPSRKTH
//