Q11206 (SIA4C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
Short name=Alpha 2,3-ST 4
Short name=Beta-galactoside alpha-2,3-sialyltransferase 4
EC=2.4.99.-

Alternative name(s):
Alpha 2,3-sialyltransferase IV
Gal-NAc6S
Gal-beta-1,4-GalNAc-alpha-2,3-sialyltransferase
SAT-3
ST-4
ST3Gal IV
Short name=ST3GalIV
ST3GalA.2
STZ
Sialyltransferase 4C
Short name=SIAT4-C

Gene names

Name:	ST3GAL4
Synonyms:	CGS23, NANTA3, SIAT4C, STZ

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	It may catalyze the formation of the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- or NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc-sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. It may be involved in the biosynthesis of the sialyl Lewis X determinant. Also acts on the corresponding 1,3-galactosyl derivative. Ref.7
Catalytic activity	CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note: Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.
Tissue specificity	Highly expressed in adult placenta, ovary and testes.
Post-translational modification	The soluble form derives from the membrane form by proteolytic processing.
Sequence similarities	Belongs to the glycosyltransferase 29 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	O-glycan processing Traceable author statement. Source: Reactome keratan sulfate biosynthetic process Traceable author statement. Source: Reactome post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome
Cellular_component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell Golgi membrane Traceable author statement. Source: Reactome extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to Golgi membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	beta-galactoside (CMP) alpha-2,3-sialyltransferase activity Traceable author statement Ref.1. Source: ProtInc monosialoganglioside sialyltransferase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q11206-1)

Also known as: B1;

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: Q11206-2)

Also known as: A1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MVSKSR → MCPAG

Isoform 3 (identifier: Q11206-3)

Also known as: A2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: Missing.

Isoform 4 (identifier: Q11206-4)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     61-61: N → KLSPLCS

Isoform 5 (identifier: Q11206-5)

The sequence of this isoform differs from the canonical sequence as follows:
     30-34: RYIEL → S

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 333	333	CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4		PRO_0000149262
Regions
	Topological domain	1 – 8	8	Cytoplasmic Potential
	Transmembrane	9 – 26	18	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	27 – 333	307	Lumenal Potential
Amino acid modifications
	Glycosylation	61	1	N-linked (GlcNAc...) Potential
	Glycosylation	131	1	N-linked (GlcNAc...) Potential
	Glycosylation	310	1	N-linked (GlcNAc...) Potential
	Glycosylation	329	1	N-linked (GlcNAc...) Potential
	Disulfide bond	120 ↔ 273		By similarity
Natural variations
	Alternative sequence	1 – 11	11	Missing in isoform 3.		VSP_001785
	Alternative sequence	1 – 6	6	MVSKSR → MCPAG in isoform 2.		VSP_001784
	Alternative sequence	30 – 34	5	RYIEL → S in isoform 5.		VSP_021104
	Alternative sequence	61	1	N → KLSPLCS in isoform 4.		VSP_001786
Experimental info
	Sequence conflict	182 – 183	2	NP → KG in AAC14162. Ref.7
	Sequence conflict	200	1	I → T in AAC14162. Ref.7
	Sequence conflict	304	1	M → I in AAC14162. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (B1) [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 15E4BCE1F4F5B3C3	FASTA	333	38,045
	10 20 30 40 50 60 MVSKSRWKLL AMLALVLVVM VWYSISREDR YIELFYFPIP EKKEPCLQGE AESKASKLFG 70 80 90 100 110 120 NYSRDQPIFL RLEDYFWVKT PSAYELPYGT KGSEDLLLRV LAITSSSIPK NIQSLRCRRC 130 140 150 160 170 180 VVVGNGHRLR NSSLGDAINK YDVVIRLNNA PVAGYEGDVG SKTTMRLFYP ESAHFDPKVE 190 200 210 220 230 240 NNPDTLLVLV AFKAMDFHWI ETILSDKKRV RKGFWKQPPL IWDVNPKQIR ILNPFFMEIA 250 260 270 280 290 300 ADKLLSLPMQ QPRKIKQKPT TGLLAITLAL HLCDLVHIAG FGYPDAYNKK QTIHYYEQIT 310 320 330 LKSMAGSGHN VSQEALAIKR MLEMGAIKNL TSF
	Isoform 2 (A1) [UniParc]. Checksum: 3FF1B2BBAF273A03	FASTA	332	37,816
	10 20 30 40 50 60 MCPAGWKLLA MLALVLVVMV WYSISREDRY IELFYFPIPE KKEPCLQGEA ESKASKLFGN 70 80 90 100 110 120 YSRDQPIFLR LEDYFWVKTP SAYELPYGTK GSEDLLLRVL AITSSSIPKN IQSLRCRRCV 130 140 150 160 170 180 VVGNGHRLRN SSLGDAINKY DVVIRLNNAP VAGYEGDVGS KTTMRLFYPE SAHFDPKVEN 190 200 210 220 230 240 NPDTLLVLVA FKAMDFHWIE TILSDKKRVR KGFWKQPPLI WDVNPKQIRI LNPFFMEIAA 250 260 270 280 290 300 DKLLSLPMQQ PRKIKQKPTT GLLAITLALH LCDLVHIAGF GYPDAYNKKQ TIHYYEQITL 310 320 330 KSMAGSGHNV SQEALAIKRM LEMGAIKNLT SF
	Isoform 3 (A2) [UniParc]. Checksum: 3AA7031A765DF2BD	FASTA	322	36,745
	10 20 30 40 50 60 MLALVLVVMV WYSISREDRY IELFYFPIPE KKEPCLQGEA ESKASKLFGN YSRDQPIFLR 70 80 90 100 110 120 LEDYFWVKTP SAYELPYGTK GSEDLLLRVL AITSSSIPKN IQSLRCRRCV VVGNGHRLRN 130 140 150 160 170 180 SSLGDAINKY DVVIRLNNAP VAGYEGDVGS KTTMRLFYPE SAHFDPKVEN NPDTLLVLVA 190 200 210 220 230 240 FKAMDFHWIE TILSDKKRVR KGFWKQPPLI WDVNPKQIRI LNPFFMEIAA DKLLSLPMQQ 250 260 270 280 290 300 PRKIKQKPTT GLLAITLALH LCDLVHIAGF GYPDAYNKKQ TIHYYEQITL KSMAGSGHNV 310 320 SQEALAIKRM LEMGAIKNLT SF
	Isoform 4 (C) [UniParc]. Checksum: F48917FF5E9CAF87	FASTA	339	38,660
	10 20 30 40 50 60 MVSKSRWKLL AMLALVLVVM VWYSISREDR YIELFYFPIP EKKEPCLQGE AESKASKLFG 70 80 90 100 110 120 KLSPLCSYSR DQPIFLRLED YFWVKTPSAY ELPYGTKGSE DLLLRVLAIT SSSIPKNIQS 130 140 150 160 170 180 LRCRRCVVVG NGHRLRNSSL GDAINKYDVV IRLNNAPVAG YEGDVGSKTT MRLFYPESAH 190 200 210 220 230 240 FDPKVENNPD TLLVLVAFKA MDFHWIETIL SDKKRVRKGF WKQPPLIWDV NPKQIRILNP 250 260 270 280 290 300 FFMEIAADKL LSLPMQQPRK IKQKPTTGLL AITLALHLCD LVHIAGFGYP DAYNKKQTIH 310 320 330 YYEQITLKSM AGSGHNVSQE ALAIKRMLEM GAIKNLTSF
	Isoform 5 [UniParc]. Checksum: 3A1C52816B5BE9E8	FASTA	329	37,458
	10 20 30 40 50 60 MVSKSRWKLL AMLALVLVVM VWYSISREDS FYFPIPEKKE PCLQGEAESK ASKLFGNYSR 70 80 90 100 110 120 DQPIFLRLED YFWVKTPSAY ELPYGTKGSE DLLLRVLAIT SSSIPKNIQS LRCRRCVVVG 130 140 150 160 170 180 NGHRLRNSSL GDAINKYDVV IRLNNAPVAG YEGDVGSKTT MRLFYPESAH FDPKVENNPD 190 200 210 220 230 240 TLLVLVAFKA MDFHWIETIL SDKKRVRKGF WKQPPLIWDV NPKQIRILNP FFMEIAADKL 250 260 270 280 290 300 LSLPMQQPRK IKQKPTTGLL AITLALHLCD LVHIAGFGYP DAYNKKQTIH YYEQITLKSM 310 320 AGSGHNVSQE ALAIKRMLEM GAIKNLTSF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic organization and chromosomal mapping of the Gal beta 1,3GalNAc/Gal beta 1,4GlcNAc alpha 2,3-sialyltransferase." Kitagawa H., Mattei M.-G., Paulson J.C. J. Biol. Chem. 271:931-938(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Cloning of a novel alpha 2,3-sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups." Kitagawa H., Paulson J.C. J. Biol. Chem. 269:1394-1401(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Placenta.
[3]	"Expression cloning of a novel Gal beta (1-3/1-4) GlcNAc alpha 2,3-sialyltransferase using lectin resistance selection." Sasaki K., Watanabe E., Kawashima K., Sekine S., Dohi T., Oshima M., Hanai N., Nishi T., Hasegawa M. J. Biol. Chem. 268:22782-22787(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[4]	"Analysis of a2,3-sialyltransferase, ST3Gal IV, transcripts in human peripheral white blood cells by RT-PCR and capillary electrophoresis." Grahn A., Larson G. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Placenta.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta.
[7]	"Characterization of two glycolipid: alpha 2-3sialyltransferases, SAT-3 (CMP-NeuAc:nLcOse4Cer alpha 2-3sialyltransferase) and SAT-4 (CMP-NeuAc:GgOse4Cer alpha 2-3sialyltransferase), from human colon carcinoma (Colo 205) cell line." Basu S.S., Basu M., Li Z., Basu S. Biochemistry 35:5166-5174(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-314, FUNCTION. Tissue: Colon carcinoma.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

ST3Gal IV

Cross-references

Sequence databases
EMBL GenBank DDBJ	L23767 mRNA. Translation: AAA16460.1. X74570 mRNA. Translation: CAA52662.1. AY040826 mRNA. Translation: AAK93790.1. AF035249 mRNA. Translation: AAC14162.1. AK291577 mRNA. Translation: BAF84266.1. BC010645 mRNA. Translation: AAH10645.1.
IPI	IPI00009631. IPI00216273. IPI00216274. IPI00216275. IPI00795122.
PIR	A48715. A49879.
RefSeq	NP_001241686.1. NM_001254757.1. NP_001241687.1. NM_001254758.1. NP_001241688.1. NM_001254759.1. NP_006269.1. NM_006278.2.
UniGene	Hs.591947.
3D structure databases
ProteinModelPortal	Q11206.
SMR	Q11206. Positions 42-331.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000227495.
Protein family/group databases
CAZy	GT29. Glycosyltransferase Family 29.
PTM databases
PhosphoSite	Q11206.
Polymorphism databases
DMDM	1705565.
Proteomic databases
PaxDb	Q11206.
PRIDE	Q11206.
Protocols and materials databases
DNASU	6484.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000227495; ENSP00000227495; ENSG00000110080. ENST00000356132; ENSP00000348451; ENSG00000110080. ENST00000392669; ENSP00000376437; ENSG00000110080. ENST00000444328; ENSP00000394354; ENSG00000110080. ENST00000449406; ENSP00000399444; ENSG00000110080. ENST00000526727; ENSP00000436047; ENSG00000110080. ENST00000530591; ENSP00000433989; ENSG00000110080. ENST00000532243; ENSP00000434349; ENSG00000110080. ENST00000534083; ENSP00000433318; ENSG00000110080.
GeneID	6484.
KEGG	hsa:6484.
UCSC	uc001qds.3. human. uc001qdw.3. human.
Organism-specific databases
CTD	6484.
GeneCards	GC11P126225.
HGNC	HGNC:10864. ST3GAL4.
HPA	HPA049827.
MIM	104240. gene.
neXtProt	NX_Q11206.
PharmGKB	PA35766.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG284110.
HOGENOM	HOG000000682.
HOVERGEN	HBG056676.
KO	K03494.
OMA	IHYYEQI.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_116125. Disease. REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q11206.
Bgee	Q11206.
CleanEx	HS_ST3GAL4.
Genevestigator	Q11206.
GermOnline	ENSG00000110080. Homo sapiens.
Family and domain databases
InterPro	IPR001675. Glyco_trans_29. IPR012163. Sialyl_trans. [Graphical view]
Pfam	PF00777. Glyco_transf_29. 1 hit. [Graphical view]
PIRSF	PIRSF005557. Sialyl_trans. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	ST3GAL4. human.
GenomeRNAi	6484.
NextBio	25191.
SOURCE	Search...

Entry information

Entry name

SIA4C_HUMAN

Accession

Primary (citable) accession number: Q11206
Secondary accession number(s): A8K6B2, O60497, Q96QQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.