ID   ALG2_HUMAN              Reviewed;         416 AA.
AC   Q9H553; A2A2Y0; Q8NBX2; Q8NC39;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   02-MAR-2010, entry version 73.
DE   RecName: Full=Alpha-1,3-mannosyltransferase ALG2;
DE            EC=2.4.1.-;
DE   AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase;
DE   AltName: Full=Asparagine-linked glycosylation protein 2 homolog;
GN   Name=ALG2; ORFNames=UNQ666/PRO1298;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Takahashi T., Katoh R., Okutomi S., Suzuki Y., Mori H., Takizawa Y.,
RA   Nishikawa Y.;
RT   "Molecular cloning of the mammalian genes which complement the defect
RT   of the yeast alg2 mutation.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   MEDLINE=22887296; PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic testis carcinoma;
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).
RN   [6]
RP   FUNCTION, AND DISEASE.
RX   PubMed=12684507; DOI=10.1074/jbc.M302850200;
RA   Thiel C., Schwarz M., Peng J., Grzmil M., Hasilik M., Braulke T.,
RA   Kohlschuetter A., von Figura K., Lehle L., Koerner C.;
RT   "A new type of congenital disorders of glycosylation (CDG-Ii) provides
RT   new insights into the early steps of dolichol-linked oligosaccharide
RT   biosynthesis.";
RL   J. Biol. Chem. 278:22498-22505(2003).
CC   -!- FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and
CC       Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-
CC       dolichol diphosphate.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H553-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H553-2; Sequence=VSP_013188, VSP_013189;
CC   -!- DISEASE: Defects in ALG2 are the cause of congenital disorder of
CC       glycosylation type 1I (CDG1I) [MIM:607906]. CDGs are a family of
CC       severe inherited diseases caused by a defect in protein N-
CC       glycosylation. They are characterized by under-glycosylated serum
CC       proteins. These multisystem disorders present with a wide variety
CC       of clinical features, such as disorders of the nervous system
CC       development, psychomotor retardation, dysmorphic features,
CC       hypotonia, coagulation disorders, and immunodeficiency. The broad
CC       spectrum of features reflects the critical role of N-glycoproteins
CC       during embryonic development, differentiation, and maintenance of
CC       cell functions.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/ALG2";
CC   -!- WEB RESOURCE: Name=GGDB; Note=GlycoGene database;
CC       URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/";
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DR   EMBL; AB161356; BAD11905.1; -; mRNA.
DR   EMBL; AY358697; AAQ89060.1; -; mRNA.
DR   EMBL; AK027417; BAB55099.1; -; mRNA.
DR   EMBL; AK074704; BAC11150.1; -; mRNA.
DR   EMBL; AK074988; BAC11337.1; -; mRNA.
DR   EMBL; AK075172; BAC11449.1; -; mRNA.
DR   EMBL; AL137067; CAC07999.1; -; Genomic_DNA.
DR   EMBL; BC017876; AAH17876.1; -; mRNA.
DR   IPI; IPI00171443; -.
DR   IPI; IPI00386072; -.
DR   RefSeq; NP_149078.1; -.
DR   UniGene; Hs.40919; -.
DR   STRING; Q9H553; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PhosphoSite; Q9H553; -.
DR   PRIDE; Q9H553; -.
DR   Ensembl; ENST00000476832; ENSP00000417764; ENSG00000119523; Homo sapiens.
DR   GeneID; 85365; -.
DR   KEGG; hsa:85365; -.
DR   UCSC; uc004azf.1; human.
DR   UCSC; uc004azg.1; human.
DR   CTD; 85365; -.
DR   GeneCards; GC09M101018; -.
DR   HGNC; HGNC:23159; ALG2.
DR   MIM; 607905; gene.
DR   MIM; 607906; phenotype.
DR   Orphanet; 79326; CDG syndrome, type Ii.
DR   PharmGKB; PA134956849; -.
DR   eggNOG; prNOG12256; -.
DR   HOGENOM; HBG320579; -.
DR   HOVERGEN; HBG009445; -.
DR   InParanoid; Q9H553; -.
DR   OMA; GDWLPRS; -.
DR   OrthoDB; EOG90KBJK; -.
DR   PhylomeDB; Q9H553; -.
DR   NextBio; 75895; -.
DR   ArrayExpress; Q9H553; -.
DR   Bgee; Q9H553; -.
DR   CleanEx; HS_ALG2; -.
DR   Genevestigator; Q9H553; -.
DR   GermOnline; ENSG00000119523; Homo sapiens.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0000033; F:alpha-1,3-mannosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IMP:UniProtKB.
DR   GO; GO:0043495; F:protein anchor; IMP:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR   GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosyntheti...; IGI:UniProtKB.
DR   GO; GO:0033577; P:protein amino acid glycosylation in endopla...; IGI:UniProtKB.
DR   GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome;
KW   Congenital disorder of glycosylation; Glycosyltransferase; Membrane;
KW   Polymorphism; Transferase; Transmembrane.
FT   CHAIN         1    416       Alpha-1,3-mannosyltransferase ALG2.
FT                                /FTId=PRO_0000080260.
FT   TRANSMEM     85    105       Potential.
FT   VAR_SEQ       1     91       Missing (in isoform 2).
FT                                /FTId=VSP_013188.
FT   VAR_SEQ      92    116       VRMVFLALYVLFLADEEFDVVVCDQ -> MPLLKLVHGSPL
FT                                VFGEKFKLFTL (in isoform 2).
FT                                /FTId=VSP_013189.
FT   VARIANT      11     11       S -> P (in dbSNP:rs11545137).
FT                                /FTId=VAR_049351.
FT   VARIANT     367    367       V -> A (in dbSNP:rs35626507).
FT                                /FTId=VAR_049352.
FT   CONFLICT    178    178       Q -> R (in Ref. 2; BAC11449).
SQ   SEQUENCE   416 AA;  47092 MW;  778DB1FD069E7F29 CRC64;
     MAEEQGRERD SVPKPSVLFL HPDLGVGGAE RLVLDAALAL QARGCSVKIW TAHYDPGHCF
     AESRELPVRC AGDWLPRGLG WGGRGAAVCA YVRMVFLALY VLFLADEEFD VVVCDQVSAC
     IPVFRLARRR KKILFYCHFP DLLLTKRDSF LKRLYRAPID WIEEYTTGMA DCILVNSQFT
     AAVFKETFKS LSHIDPDVLY PSLNVTSFDS VVPEKLDDLV PKGKKFLLLS INRYERKKNL
     TLALEALVQL RGRLTSQDWE RVHLIVAGGY DERVLENVEH YQELKKMVQQ SDLGQYVTFL
     RSFSDKQKIS LLHSCTCVLY TPSNEHFGIV PLEAMYMQCP VIAVNSGGPL ESIDHSVTGF
     LCEPDPVHFS EAIEKFIREP SLKATMGLAG RARVKEKFSP EAFTEQLYRY VTKLLV
//