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Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase (EC 2.4.1.260) (Asparagine-linked glycosylation protein 12 homolog) (hALG12) (Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase) (Mannosyltransferase ALG12 homolog) (Membrane protein SB87)

 ALG12_HUMAN             Reviewed;         488 AA.
Q9BV10; A6PWM1; Q4KMH4; Q8NG10; Q96AA4;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
28-FEB-2018, entry version 149.
RecName: Full=Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase;
EC=2.4.1.260;
AltName: Full=Asparagine-linked glycosylation protein 12 homolog;
Short=hALG12;
AltName: Full=Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase;
AltName: Full=Mannosyltransferase ALG12 homolog;
AltName: Full=Membrane protein SB87;
Name=ALG12; ORFNames=PP14673;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT CDG1G VAL-142.
TISSUE=Skin;
PubMed=11983712; DOI=10.1074/jbc.M203285200;
Chantret I., Dupre T., Delenda C., Bucher S., Dancourt J., Barnier A.,
Charollais A., Heron D., Bader-Meunier B., Danos O., Seta N.,
Durand G., Oriol R., Codogno P., Moore S.E.H.;
"Congenital disorders of glycosylation type Ig is defined by a
deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl
mannosyltransferase.";
J. Biol. Chem. 277:25815-25822(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Zhang W., Li N., Wan T., Cao X.;
"Identification of novel membrane proteins.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-393.
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
CHARACTERIZATION OF VARIANTS CDG1G MET-67 AND GLN-146.
PubMed=12217961; DOI=10.1093/hmg/11.19.2331;
Grubenmann C.E., Frank C.G., Kjaergaard S., Berger E.G., Aebi M.,
Hennet T.;
"ALG12 mannosyltransferase defect in congenital disorder of
glycosylation type Ig.";
Hum. Mol. Genet. 11:2331-2339(2002).
[9]
CHARACTERIZATION OF VARIANT CDG1G PRO-158.
PubMed=12093361; DOI=10.1042/BJ20020794;
Thiel C., Schwarz M., Hasilik M., Grieben U., Hanefeld F., Lehle L.,
von Figura K., Koerner C.;
"Deficiency of dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl
mannosyltransferase causes congenital disorder of glycosylation type
Ig.";
Biochem. J. 367:195-201(2002).
[10]
INVOLVEMENT IN CDG1G.
PubMed=12736397; DOI=10.1203/01.PDR.0000072327.55955.F7;
Zdebska E., Bader-Meunier B., Schischmanoff P.-O., Dupre T., Seta N.,
Tchernia G., Koscielak J., Delaunay J.;
"Abnormal glycosylation of red cell membrane band 3 in the congenital
disorder of glycosylation Ig.";
Pediatr. Res. 54:224-229(2003).
[11]
VARIANTS CDG1G ARG-101 AND GLN-146.
PubMed=17506107; DOI=10.1002/ajmg.a.31791;
Kranz C., Basinger A.A., Guecsavas-Calikoglu M., Sun L., Powell C.M.,
Henderson F.W., Aylsworth A.S., Freeze H.H.;
"Expanding spectrum of congenital disorder of glycosylation Ig (CDG-
Ig): sibs with a unique skeletal dysplasia, hypogammaglobulinemia,
cardiomyopathy, genital malformations, and early lethality.";
Am. J. Med. Genet. A 143:1371-1378(2007).
-!- FUNCTION: Adds the eighth mannose residue in an alpha-1,6 linkage
onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-
Man(7)GlcNAc(2)) required for protein glycosylation.
-!- CATALYTIC ACTIVITY: Dolichyl beta-D-mannosyl phosphate + D-Man-
alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-
(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-
GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-
(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-
D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-alpha-(1->6))-D-Man-
beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol +
dolichyl phosphate.
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in fibroblasts.
-!- DISEASE: Congenital disorder of glycosylation 1G (CDG1G)
[MIM:607143]: A form of congenital disorder of glycosylation, a
multisystem disorder caused by a defect in glycoprotein
biosynthesis and characterized by under-glycosylated serum
glycoproteins. Congenital disorders of glycosylation result in a
wide variety of clinical features, such as defects in the nervous
system development, psychomotor retardation, dysmorphic features,
hypotonia, coagulation disorders, and immunodeficiency. The broad
spectrum of features reflects the critical role of N-glycoproteins
during embryonic development, differentiation, and maintenance of
cell functions. {ECO:0000269|PubMed:11983712,
ECO:0000269|PubMed:12093361, ECO:0000269|PubMed:12217961,
ECO:0000269|PubMed:12736397, ECO:0000269|PubMed:17506107}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM94900.1; Type=Frameshift; Positions=468; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AJ290427; CAC83681.1; -; mRNA.
EMBL; AJ303120; CAC67488.1; -; mRNA.
EMBL; AF311904; AAM94900.1; ALT_FRAME; mRNA.
EMBL; AF318343; AAL55850.1; -; mRNA.
EMBL; CR456369; CAG30255.1; -; mRNA.
EMBL; AL671710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471138; EAW73480.1; -; Genomic_DNA.
EMBL; BC001729; AAH01729.1; -; mRNA.
EMBL; BC098562; AAH98562.1; -; mRNA.
CCDS; CCDS14081.1; -.
RefSeq; NP_077010.1; NM_024105.3.
UniGene; Hs.526711; -.
ProteinModelPortal; Q9BV10; -.
BioGrid; 122535; 9.
IntAct; Q9BV10; 2.
STRING; 9606.ENSP00000333813; -.
CAZy; GT22; Glycosyltransferase Family 22.
iPTMnet; Q9BV10; -.
PhosphoSitePlus; Q9BV10; -.
BioMuta; ALG12; -.
DMDM; 45476971; -.
EPD; Q9BV10; -.
MaxQB; Q9BV10; -.
PaxDb; Q9BV10; -.
PeptideAtlas; Q9BV10; -.
PRIDE; Q9BV10; -.
DNASU; 79087; -.
Ensembl; ENST00000330817; ENSP00000333813; ENSG00000182858.
GeneID; 79087; -.
KEGG; hsa:79087; -.
UCSC; uc003biy.4; human.
CTD; 79087; -.
DisGeNET; 79087; -.
EuPathDB; HostDB:ENSG00000182858.13; -.
GeneCards; ALG12; -.
GeneReviews; ALG12; -.
H-InvDB; HIX0175449; -.
HGNC; HGNC:19358; ALG12.
HPA; HPA003076; -.
HPA; HPA051665; -.
MalaCards; ALG12; -.
MIM; 607143; phenotype.
MIM; 607144; gene.
neXtProt; NX_Q9BV10; -.
OpenTargets; ENSG00000182858; -.
Orphanet; 79324; ALG12-CDG.
PharmGKB; PA134987771; -.
eggNOG; KOG2516; Eukaryota.
eggNOG; ENOG410XR38; LUCA.
GeneTree; ENSGT00550000075005; -.
HOGENOM; HOG000265945; -.
HOVERGEN; HBG050486; -.
InParanoid; Q9BV10; -.
KO; K03847; -.
OMA; AIYSLQP; -.
OrthoDB; EOG091G07LQ; -.
PhylomeDB; Q9BV10; -.
TreeFam; TF314453; -.
BRENDA; 2.4.1.260; 2681.
Reactome; R-HSA-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
Reactome; R-HSA-4720489; Defective ALG12 causes ALG12-CDG (CDG-1g).
UniPathway; UPA00378; -.
ChiTaRS; ALG12; human.
GeneWiki; ALG12; -.
GenomeRNAi; 79087; -.
PRO; PR:Q9BV10; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000182858; -.
CleanEx; HS_ALG12; -.
ExpressionAtlas; Q9BV10; baseline and differential.
Genevisible; Q9BV10; HS.
GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0052917; F:dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IDA:MGI.
GO; GO:0006457; P:protein folding; NAS:UniProtKB.
GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
InterPro; IPR005599; GPI_mannosylTrfase.
PANTHER; PTHR22760; PTHR22760; 1.
Pfam; PF03901; Glyco_transf_22; 1.
1: Evidence at protein level;
Complete proteome; Congenital disorder of glycosylation;
Disease mutation; Endoplasmic reticulum; Glycosyltransferase;
Membrane; Polymorphism; Reference proteome; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 488 Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-
1,6-mannosyltransferase.
/FTId=PRO_0000215781.
TRANSMEM 11 31 Helical. {ECO:0000255}.
TRANSMEM 68 88 Helical. {ECO:0000255}.
TRANSMEM 93 113 Helical. {ECO:0000255}.
TRANSMEM 122 142 Helical. {ECO:0000255}.
TRANSMEM 145 165 Helical. {ECO:0000255}.
TRANSMEM 177 197 Helical. {ECO:0000255}.
TRANSMEM 212 232 Helical. {ECO:0000255}.
TRANSMEM 264 284 Helical. {ECO:0000255}.
TRANSMEM 290 310 Helical. {ECO:0000255}.
TRANSMEM 312 332 Helical. {ECO:0000255}.
TRANSMEM 346 366 Helical. {ECO:0000255}.
TRANSMEM 423 443 Helical. {ECO:0000255}.
VARIANT 67 67 T -> M (in CDG1G; dbSNP:rs121907931).
{ECO:0000269|PubMed:12217961}.
/FTId=VAR_017904.
VARIANT 101 101 G -> R (in CDG1G; dbSNP:rs121907933).
{ECO:0000269|PubMed:17506107}.
/FTId=VAR_038428.
VARIANT 142 142 F -> V (in CDG1G; dbSNP:rs28942090).
{ECO:0000269|PubMed:11983712}.
/FTId=VAR_017905.
VARIANT 146 146 R -> Q (in CDG1G; dbSNP:rs121907932).
{ECO:0000269|PubMed:12217961,
ECO:0000269|PubMed:17506107}.
/FTId=VAR_017906.
VARIANT 158 158 L -> P (in CDG1G; dbSNP:rs121907934).
{ECO:0000269|PubMed:12093361}.
/FTId=VAR_017907.
VARIANT 393 393 I -> V (in dbSNP:rs3922872).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_024466.
CONFLICT 267 267 A -> T (in Ref. 2; AAM94900).
{ECO:0000305}.
SEQUENCE 488 AA; 54655 MW; 8D4F921C21CBC8B6 CRC64;
MAGKGSSGRR PLLLGLLVAV ATVHLVICPY TKVEESFNLQ ATHDLLYHWQ DLEQYDHLEF
PGVVPRTFLG PVVIAVFSSP AVYVLSLLEM SKFYSQLIVR GVLGLGVIFG LWTLQKEVRR
HFGAMVATMF CWVTAMQFHL MFYCTRTLPN VLALPVVLLA LAAWLRHEWA RFIWLSAFAI
IVFRVELCLF LGLLLLLALG NRKVSVVRAL RHAVPAGILC LGLTVAVDSY FWRQLTWPEG
KVLWYNTVLN KSSNWGTSPL LWYFYSALPR GLGCSLLFIP LGLVDRRTHA PTVLALGFMA
LYSLLPHKEL RFIIYAFPML NITAARGCSY LLNNYKKSWL YKAGSLLVIG HLVVNAAYSA
TALYVSHFNY PGGVAMQRLH QLVPPQTDVL LHIDVAAAQT GVSRFLQVNS AWRYDKREDV
QPGTGMLAYT HILMEAAPGL LALYRDTHRV LASVVGTTGV SLNLTQLPPF NVHLQTKLVL
LERLPRPS


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