GLT12_HUMAN » Polypeptide N-acetylgalactosaminyltransferase 12

GLT12_HUMAN » Polypeptide N-acetylgalactosaminyltransferase 12
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Topology in Golgi apparatus membrane
TopologyGolgi lumenal side
cytoplasmic side
GLT12_HUMAN » Polypeptide N-acetylgalactosaminyltransferase 12 » Polypeptide GalNAc transferase 12;GalNAc-T12; pp-GaNTase 12; Protein-UDP acetylgalactosaminyltransferase 12;UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12;
Hydrophobic Thickness 34.4 ± 3.1 Å
Tilt Angle 3 ± 3°
ΔGtransfer -19.1 kcal/mol
ΔGfold -15.6 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology In
TM Segments 16-38 (11-41)
Pathways

Mucin type O-Glycan biosynthesis (KEGG)

PDB none
OPM none
Complexes none
Interactions

A4, Complex: A4:GLT12, PubMed

BMR1A, Complex: BMR1A:GLT12

CADH1, Complex: CADH1:GLT12

MUC1, Complex: GLT12:MUC1, PubMed

Domains

AA: 139-322, PDBID: 2D7I, Subunit A, Seq Identity:60%, Glycosyl transferase family 2

AA: 445-574, PDBID: 1XHB, Subunit A, Seq Identity:35%, Ricin-type beta-trefoil lectin domain

UniProt annotation for GLT12_HUMAN » Polypeptide N-acetylgalactosaminyltransferase 12
FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with Muc2 and Muc7. Displays enzymatic activity toward the Gal-NAc- Muc5AC glycopeptide, but no detectable activity to mono-GalNAc- glycosylated Muc1a, Muc2, Muc7 and EA2. May play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs.

CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.

TISSUE SPECIFICITY: Widely expressed at different levels of expression. Highly expressed in digestive organs such as small intestine, stomach, pancreas and colon. Expressed at intermediate level in testis, thyroid gland and spleen. Weakly expressed in whole brain, cerebral cortex, cerebellum, fetal brain, bone marrow, thymus, leukocytes, heart, skeletal muscle, liver, lung, esophagus, kidney, adrenal gland, mammary gland, uterus, placenta, ovary and prostate.

DOMAIN: There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.

DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

DISEASE: Colorectal cancer 1 (CRCS1) OMIM: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history. associated with variations affecting the gene represented in this entry. The role of GALNT12 in colon cancer susceptibility is however subject to discussion: studies on 103 probants with colorectal cancer 1 (CRCS1) suggest that it does not act as a major contributor of CRCS1 (PubMed).

UniProt features for GLT12_HUMAN » Polypeptide N-acetylgalactosaminyltransferase 12
CHAIN 1 581 Polypeptide N- acetylgalactosaminyltransferase 12.
DOMAIN 445 577 Ricin B-type lectin.
REGION 135 244 Catalytic subdomain A.
REGION 304 366 Catalytic subdomain B.
DISULFID 458 479 By similarity.
DISULFID 506 521 By similarity.
DISULFID 547 566 By similarity.
Amino Acid Sequence for GLT12_HUMAN » Polypeptide N-acetylgalactosaminyltransferase 12
MWGRTARRRC PRELRRGREA LLVLLALLAL AGLGSVLRAQ RGAGAGAAEP GPPRTPRPGR REPVMPRPPV PANALGARGE AVRLQLQGEE LRLQEESVRL HQINIYLSDR ISLHRRLPER WNPLCKEKKY DYDNLPRTSV IIAFYNEAWS TLLRTVYSVL ETSPDILLEE VILVDDYSDR EHLKERLANE LSGLPKVRLI RANKREGLVR ARLLGASAAR GDVLTFLDCH CECHEGWLEP LLQRIHEEES AVVCPVIDVI DWNTFEYLGN SGEPQIGGFD WRLVFTWHTV PERERIRMQS PVDVIRSPTM AGGLFAVSKK YFEYLGSYDT GMEVWGGENL EFSFRIWQCG GVLETHPCSH VGHVFPKQAP YSRNKALANS VRAAEVWMDE FKELYYHRNP RARLEPFGDV TERKQLRDKL QCKDFKWFLE TVYPELHVPE DRPGFFGMLQ NKGLTDYCFD YNPPDENQIV GHQVILYLCH GMGQNQFFEY TSQKEIRYNT HQPEGCIAVE AGMDTLIMHL CEETAPENQK FILQEDGSLF HEQSKKCVQA ARKESSDSFV PLLRDCTNSD HQKWFFKERM L