Reviewed, UniProtKB/Swiss-Prot Q8IXK2 (GLT12_HUMAN)

Names and origin

Protein names

Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 12
    EC=2.4.1.41
Alternative name(s):
    Polypeptide GalNAc transferase 12
      Short name=pp-GaNTase 12
      Short name=GalNAc-T12
    Protein-UDP acetylgalactosaminyltransferase 12
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12

Gene names

Name:

GALNT12

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	581 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

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-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. Ref.1
Cofactor	Manganese By similarity. Calcium By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
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. Ref.1
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 By similarity. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity By similarity.
Sequence similarities	Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily. Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW polypeptide N-acetylgalactosaminyltransferase activity Inferred from electronic annotation. Source: EC sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8IXK2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8IXK2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-309: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 581	581	Polypeptide N-acetylgalactosaminyltransferase 12		PRO_0000059128
Regions
	Topological domain	1 – 19	19	Cytoplasmic Potential
	Transmembrane	20 – 37	18	Signal-anchor for type II membrane protein Potential
	Topological domain	38 – 581	544	Lumenal Potential
	Domain	445 – 577	133	Ricin B-type lectin
	Region	135 – 244	110	Catalytic subdomain A
	Region	304 – 366	63	Catalytic subdomain B
Amino acid modifications
	Disulfide bond	458 ↔ 479		By similarity
	Disulfide bond	506 ↔ 521		By similarity
	Disulfide bond	547 ↔ 566		By similarity
Natural variations
	Alternative sequence	1 – 309	309	Missing in isoform 2.		VSP_011217
Experimental info
	Sequence conflict	119	1	E → V in BAC07181. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 20, 2005. Version 3. Checksum: 8C001D58E103A523	FASTA	581	66,938
	10 20 30 40 50 60 MWGRTARRRC PRELRRGREA LLVLLALLAL AGLGSVLRAQ RGAGAGAAEP GPPRTPRPGR 70 80 90 100 110 120 REPVMPRPPV PANALGARGE AVRLQLQGEE LRLQEESVRL HQINIYLSDR ISLHRRLPER 130 140 150 160 170 180 WNPLCKEKKY DYDNLPRTSV IIAFYNEAWS TLLRTVYSVL ETSPDILLEE VILVDDYSDR 190 200 210 220 230 240 EHLKERLANE LSGLPKVRLI RANKREGLVR ARLLGASAAR GDVLTFLDCH CECHEGWLEP 250 260 270 280 290 300 LLQRIHEEES AVVCPVIDVI DWNTFEYLGN SGEPQIGGFD WRLVFTWHTV PERERIRMQS 310 320 330 340 350 360 PVDVIRSPTM AGGLFAVSKK YFEYLGSYDT GMEVWGGENL EFSFRIWQCG GVLETHPCSH 370 380 390 400 410 420 VGHVFPKQAP YSRNKALANS VRAAEVWMDE FKELYYHRNP RARLEPFGDV TERKQLRDKL 430 440 450 460 470 480 QCKDFKWFLE TVYPELHVPE DRPGFFGMLQ NKGLTDYCFD YNPPDENQIV GHQVILYLCH 490 500 510 520 530 540 GMGQNQFFEY TSQKEIRYNT HQPEGCIAVE AGMDTLIMHL CEETAPENQK FILQEDGSLF 550 560 570 580 HEQSKKCVQA ARKESSDSFV PLLRDCTNSD HQKWFFKERM L
	Isoform 2. Checksum: 6E78ADD3FC84390F	FASTA	272	31,726
	10 20 30 40 50 60 MAGGLFAVSK KYFEYLGSYD TGMEVWGGEN LEFSFRIWQC GGVLETHPCS HVGHVFPKQA 70 80 90 100 110 120 PYSRNKALAN SVRAAEVWMD EFKELYYHRN PRARLEPFGD VTERKQLRDK LQCKDFKWFL 130 140 150 160 170 180 ETVYPELHVP EDRPGFFGML QNKGLTDYCF DYNPPDENQI VGHQVILYLC HGMGQNQFFE 190 200 210 220 230 240 YTSQKEIRYN THQPEGCIAV EAGMDTLIMH LCEETAPENQ KFILQEDGSL FHEQSKKCVQ 250 260 270 AARKESSDSF VPLLRDCTNS DHQKWFFKER ML

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of a novel member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, pp-GalNAc-T12(1)." Guo J.-M., Zhang Y., Cheng L., Iwasaki H., Wang H., Kubota T., Tachibana K., Narimatsu H. FEBS Lett. 524:211-218(2002) [PubMed: 12135769] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY. Tissue: Lung.
[2]	Bennett E.P. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Bone marrow.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-581 (ISOFORM 1). Tissue: Colon.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 12

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB078146 mRNA. Translation: BAC07181.1. AJ132365 mRNA. Translation: CAC80100.2. AL136084 Genomic DNA. Translation: CAI17042.1. BC013945 mRNA. Translation: AAH13945.1. AK024865 mRNA. Translation: BAB15027.1. Different initiation.
IPI	IPI00456149. IPI00456150.
RefSeq	NP_078918.3.
UniGene	Hs.47099
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8IXK2.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Proteomic databases
PRIDE	Q8IXK2.
Genome annotation databases
Ensembl	ENST00000375011; ENSP00000364150; ENSG00000119514; Homo sapiens. [Genome view]
GeneID	79695.
KEGG	hsa:79695.
UCSC	uc004ayz.1. human.
Organism-specific databases
CTD	79695.
GeneCards	GC09P100609.
HGNC	HGNC:19877. GALNT12.
MIM	610290. gene.
PharmGKB	PA134929192.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG715048.
HOVERGEN	Q8IXK2.
InParanoid	Q8IXK2.
OMA	WNPLCKE.
OrthoDB	EOG9STVQ9.
PhylomeDB	Q8IXK2.
Enzyme and pathway databases
BRENDA	2.4.1.41. 247.
Gene expression databases
ArrayExpress	Q8IXK2.
Bgee	Q8IXK2.
CleanEx	HS_GALNT12.
Genevestigator	Q8IXK2.
GermOnline	ENSG00000119514. Homo sapiens.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. IPR008997. Ricin_B-rel_lectin. IPR000772. Ricin_B_lectin. [Graphical view]
Pfam	PF00535. Glycos_transf_2. 1 hit. PF00652. Ricin_B_lectin. 1 hit. [Graphical view]
SMART	SM00458. RICIN. 1 hit. [Graphical view]
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	68982.
SOURCE	Search...

Entry information

Entry name

GLT12_HUMAN

Accession

Primary (citable) accession number: Q8IXK2
Secondary accession number(s): Q5TCF7 , Q8NG54, Q96CT9, Q9H771

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	December 20, 2005
Last modified:	January 19, 2010
This is version 74 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.