Q9UKY4 (POMT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein O-mannosyl-transferase 2
EC=2.4.1.109

Alternative name(s):
Dolichyl-phosphate-mannose--protein mannosyltransferase 2

Gene names

Name:

POMT2

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	750 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. Ref.6
Catalytic activity	Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.
Cofactor	Magnesium. Manganese and calcium ions suppress enzyme activity.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Interacts with POMT1 Probable.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1 Ref.6.
Tissue specificity	Highly expressed in testis; detected at low levels in most tissues.
Post-translational modification	N-glycosylated. Ref.1
Involvement in disease	Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A2 (MDDGA2) [MIM:613150]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound mental retardation, and death usually in the first years of life. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.10 Ref.12 Ref.14 Muscular dystrophy-dystroglycanopathy congenital with mental retardation B2 (MDDGB2) [MIM:613156]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with mental retardation and mild structural brain abnormalities. Note: The disease is caused by mutations affecting the gene represented in this entry. Muscular dystrophy-dystroglycanopathy limb-girdle C2 (MDDGC2) [MIM:613158]: An autosomal recessive muscular dystrophy with onset after ambulation is achieved. MDDGC2 is characterized by increased serum creatine kinase and mild muscle weakness. Muscle biopsy shows dystrophic changes, inflammatory changes, and severely decreased alpha-dystroglycan. Cognition is normal. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10
Sequence similarities	Belongs to the glycosyltransferase 39 family. Contains 3 MIR domains.
Sequence caution	The sequence CAD62348.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Congenital muscular dystrophy Limb-girdle muscular dystrophy Lissencephaly
Domain	Repeat Transmembrane Transmembrane helix
Ligand	Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein O-linked glycosylation Inferred from electronic annotation. Source: InterPro
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	dolichyl-phosphate-mannose-protein mannosyltransferase activity Inferred from electronic annotation. Source: EC metal ion 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: Q9UKY4-1)

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: Q9UKY4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     83-750: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 750	750	Protein O-mannosyl-transferase 2		PRO_0000121488
Regions
	Transmembrane	54 – 74	21	Helical; Potential
	Transmembrane	100 – 120	21	Helical; Potential
	Transmembrane	146 – 166	21	Helical; Potential
	Transmembrane	191 – 211	21	Helical; Potential
	Transmembrane	231 – 251	21	Helical; Potential
	Transmembrane	283 – 303	21	Helical; Potential
	Transmembrane	596 – 616	21	Helical; Potential
	Transmembrane	643 – 663	21	Helical; Potential
	Transmembrane	665 – 685	21	Helical; Potential
	Transmembrane	700 – 720	21	Helical; Potential
	Domain	334 – 390	57	MIR 1
	Domain	403 – 459	57	MIR 2
	Domain	464 – 521	58	MIR 3
Amino acid modifications
	Glycosylation	98	1	N-linked (GlcNAc...) Potential
	Glycosylation	330	1	N-linked (GlcNAc...) Potential
	Glycosylation	445	1	N-linked (GlcNAc...) Potential
	Glycosylation	528	1	N-linked (GlcNAc...) Potential
	Glycosylation	583	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	83 – 750	668	Missing in isoform 2.		VSP_041457
	Natural variant	54	1	A → E. Corresponds to variant rs8177536 [ dbSNP | Ensembl ].		VAR_022083
	Natural variant	184	1	T → M in MDDGC2. Ref.9 Ref.10		VAR_065037
	Natural variant	198	1	I → N in MDDGA2. Ref.10		VAR_065038
	Natural variant	246	1	G → D in MDDGB2. Ref.13		VAR_065039
	Natural variant	353	1	G → S in MDDGA2. Ref.8 Ref.13		VAR_065040
	Natural variant	373	1	V → F in MDDGA2. Ref.10		VAR_065041
	Natural variant	413	1	R → P in MDDGA2. Ref.10		VAR_065042
	Natural variant	444 – 445	2	IN → LLWQ in MDDGA2.		VAR_065043
	Natural variant	478	1	H → R in MDDGA2. Ref.14		VAR_068968
	Natural variant	482	1	G → V in MDDGA2. Ref.12		VAR_065044
	Natural variant	666	1	Y → C in MDDGB2 and MDDGA2. Ref.10 Ref.11 Ref.12 Ref.13		VAR_065045
	Natural variant	717	1	F → S in MDDGB2.		VAR_065046
	Natural variant	726	1	G → E in MDDGA2 and MDDGB2. Ref.8 Ref.13		VAR_065047
	Natural variant	748	1	W → R in MDDGB2. Ref.11		VAR_065048
	Natural variant	748	1	W → S in MDDGC2. Ref.10		VAR_065049
Experimental info
	Sequence conflict	53	1	E → Q in AAF14118. Ref.1
	Sequence conflict	53	1	E → Q in AAM12046. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 20, 2003. Version 2. Checksum: 79732D6C4978CFB9	FASTA	750	84,214
	10 20 30 40 50 60 MPPATGGGLA ESELRPRRGR CGPQAARAAG RDVAAEAVAR SPKRPAWGSR RFEAVGWWAL 70 80 90 100 110 120 LALVTLLSFA TRFHRLDEPP HICWDETHFG KMGSYYINRT FFFDVHPPLG KMLIGLAGYL 130 140 150 160 170 180 SGYDGTFLFQ KPGDKYEHHS YMGMRGFCAF LGSWLVPFAY LTVLDLSKSL SAALLTAALL 190 200 210 220 230 240 TFDTGCLTLS QYILLDPILM FFIMAAMLSM VKYNSCADRP FSAPWWFWLS LTGVSLAGAL 250 260 270 280 290 300 GVKFVGLFII LQVGLNTIAD LWYLFGDLSL SLVTVGKHLT ARVLCLIVLP LALYTATFAV 310 320 330 340 350 360 HFMVLSKSGP GDGFFSSAFQ ARLSGNNLHN ASIPEHLAYG SVITVKNLRM AIGYLHSHRH 370 380 390 400 410 420 LYPEGIGARQ QQVTTYLHKD YNNLWIIKKH NTNSDPLDPS FPVEFVRHGD IIRLEHKETS 430 440 450 460 470 480 RNLHSHYHEA PMTRKHYQVT GYGINGTGDS NDFWRIEVVN RKFGNRIKVL RSRIRFIHLV 490 500 510 520 530 540 TGCVLGSSGK VLPKWGWEQL EVTCTPYLKE TLNSIWNVED HINPKLPNIS LDVLQPSFPE 550 560 570 580 590 600 ILLESHMVMI RGNSGLKPKD NEFTSKPWHW PINYQGLRFS GVNDTDFRVY LLGNPVVWWL 610 620 630 640 650 660 NLLSIALYLL SGSIIAVAMQ RGARLPAEVA GLSQVLLRGG GQVLLGWTLH YFPFFLMGRV 670 680 690 700 710 720 LYFHHYFPAM LFSSMLTGIL WDTLLRLCAW GLASWPLARG IHVAGILSLL LGTAYSFYLF 730 740 750 HPLAYGMVGP LAQDPQSPMA GLRWLDSWDF
	Isoform 2 [UniParc]. Checksum: FFC305699BA89C4F	FASTA	82	8,899
	10 20 30 40 50 60 MPPATGGGLA ESELRPRRGR CGPQAARAAG RDVAAEAVAR SPKRPAWGSR RFEAVGWWAL 70 80 LALVTLLSFA TRFHRLDEPP HI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of POMT2, a novel member of the PMT protein O-mannosyltransferase family specifically localized to the acrosome of mammalian spermatids." Willer T., Amselgruber W., Deutzmann R., Strahl S. Glycobiology 12:771-783(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), GLYCOSYLATION, SUBCELLULAR LOCATION. Tissue: Cerebellum.
[2]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Neuroblastoma.
[3]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 612-750. Tissue: Testis.
[6]	"Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity." Manya H., Chiba A., Yoshida A., Wang X., Chiba Y., Jigami Y., Margolis R.U., Endo T. Proc. Natl. Acad. Sci. U.S.A. 101:500-505(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"POMT2 mutations cause alpha-dystroglycan hypoglycosylation and Walker-Warburg syndrome." van Reeuwijk J., Janssen M., van den Elzen C., Beltran-Valero de Bernabe D., Sabatelli P., Merlini L., Boon M., Scheffer H., Brockington M., Muntoni F., Huynen M.A., Verrips A., Walsh C.A., Barth P.G., Brunner H.G., van Bokhoven H. J. Med. Genet. 42:907-912(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MDDGA2.
[8]	"POMT2 mutation in a patient with 'MEB-like' phenotype." Mercuri E., D'Amico A., Tessa A., Berardinelli A., Pane M., Messina S., van Reeuwijk J., Bertini E., Muntoni F., Santorelli F.M. Neuromuscul. Disord. 16:446-448(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MDDGA2 SER-353 AND GLU-726.
[9]	"POMT2 gene mutation in limb-girdle muscular dystrophy with inflammatory changes." Biancheri R., Falace A., Tessa A., Pedemonte M., Scapolan S., Cassandrini D., Aiello C., Rossi A., Broda P., Zara F., Santorelli F.M., Minetti C., Bruno C. Biochem. Biophys. Res. Commun. 363:1033-1037(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MDDGC2 MET-184.
[10]	"Refining genotype phenotype correlations in muscular dystrophies with defective glycosylation of dystroglycan." Godfrey C., Clement E., Mein R., Brockington M., Smith J., Talim B., Straub V., Robb S., Quinlivan R., Feng L., Jimenez-Mallebrera C., Mercuri E., Manzur A.Y., Kinali M., Torelli S., Brown S.C., Sewry C.A., Bushby K. , Topaloglu H., North K., Abbs S., Muntoni F. Brain 130:2725-2735(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MDDGA2 ASN-198; PHE-373; PRO-413 AND CYS-666, VARIANTS MDDGC2 MET-184 AND SER-748.
[11]	"New POMT2 mutations causing congenital muscular dystrophy: identification of a founder mutation." Yanagisawa A., Bouchet C., Van den Bergh P.Y., Cuisset J.M., Viollet L., Leturcq F., Romero N.B., Quijano-Roy S., Fardeau M., Seta N., Guicheney P. Neurology 69:1254-1260(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MDDGB2 CYS-666 AND ARG-748.
[12]	"POMT2 intragenic deletions and splicing abnormalities causing congenital muscular dystrophy with mental retardation." Yanagisawa A., Bouchet C., Quijano-Roy S., Vuillaumier-Barrot S., Clarke N., Odent S., Rodriguez D., Romero N.B., Osawa M., Endo T., Taratuto A.L., Seta N., Guicheney P. Eur. J. Med. Genet. 52:201-206(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MDDGA2 VAL-482; 444-ILE-ASN-445 DELINS LEU-LEU-TRP-GLN AND CYS-666.
[13]	"Congenital muscular dystrophies with defective glycosylation of dystroglycan: a population study." Mercuri E., Messina S., Bruno C., Mora M., Pegoraro E., Comi G.P., D'Amico A., Aiello C., Biancheri R., Berardinelli A., Boffi P., Cassandrini D., Laverda A., Moggio M., Morandi L., Moroni I., Pane M., Pezzani R. , Pichiecchio A., Pini A., Minetti C., Mongini T., Mottarelli E., Ricci E., Ruggieri A., Saredi S., Scuderi C., Tessa A., Toscano A., Tortorella G., Trevisan C.P., Uggetti C., Vasco G., Santorelli F.M., Bertini E. Neurology 72:1802-1809(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MDDGB2 ASP-246; SER-353; CYS-666 AND GLU-726.
[14]	"Exome sequencing and functional validation in zebrafish identify GTDC2 mutations as a cause of Walker-Warburg syndrome." Manzini M.C., Tambunan D.E., Hill R.S., Yu T.W., Maynard T.M., Heinzen E.L., Shianna K.V., Stevens C.R., Partlow J.N., Barry B.J., Rodriguez J., Gupta V.A., Al-Qudah A.K., Eyaid W.M., Friedman J.M., Salih M.A., Clark R., Moroni I. , Mora M., Beggs A.H., Gabriel S.B., Walsh C.A. Am. J. Hum. Genet. 91:541-547(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MDDGA2 ARG-478.
+	Additional computationally mapped references.

Web resources

GeneReviews

GGDB

GlycoGene database

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF105020 mRNA. Translation: AAF14118.1. AY090480 mRNA. Translation: AAM12046.1. BX248027 mRNA. Translation: CAD62348.1. Sequence problems. AC007954 Genomic DNA. Translation: AAF62558.1. AC007375 Genomic DNA. Translation: AAF63184.1. BC031651 mRNA. Translation: AAH31651.1. AL353956 mRNA. Translation: CAB89256.1.
IPI	IPI00329648. IPI00329649.
PIR	T48691.
RefSeq	NP_037514.2. NM_013382.5.
UniGene	Hs.132989.
3D structure databases
ProteinModelPortal	Q9UKY4.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000261534.
Protein family/group databases
CAZy	GT39. Glycosyltransferase Family 39.
PTM databases
PhosphoSite	Q9UKY4.
Polymorphism databases
DMDM	32171723.
Proteomic databases
PaxDb	Q9UKY4.
PRIDE	Q9UKY4.
Protocols and materials databases
DNASU	29954.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261534; ENSP00000261534; ENSG00000009830. ENST00000556326; ENSP00000450630; ENSG00000009830.
GeneID	29954.
KEGG	hsa:29954.
UCSC	uc001xth.1. human.
Organism-specific databases
CTD	29954.
GeneCards	GC14M077741.
H-InvDB	HIX0011845.
HGNC	HGNC:19743. POMT2.
HPA	HPA003663.
MIM	607439. gene. 613150. phenotype. 613156. phenotype. 613158. phenotype.
neXtProt	NX_Q9UKY4.
Orphanet	206559. Autosomal recessive limb-girdle muscular dystrophy type 2N. 588. Muscle eye brain disease. 899. Walker-Warburg syndrome.
PharmGKB	PA134980627.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1928.
HOGENOM	HOG000157526.
HOVERGEN	HBG096391.
InParanoid	Q9UKY4.
KO	K00728.
OMA	WPINYRG.
OrthoDB	EOG4J3WGD.
PhylomeDB	Q9UKY4.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q9UKY4.
Bgee	Q9UKY4.
CleanEx	HS_POMT2.
Genevestigator	Q9UKY4.
GermOnline	ENSG00000009830. Homo sapiens.
Family and domain databases
InterPro	IPR027005. GlyclTrfase_39_like. IPR003342. Glyco_trans_39. IPR016093. MIR_motif. [Graphical view]
PANTHER	PTHR10050. PTHR10050. 1 hit.
Pfam	PF02815. MIR. 1 hit. PF02366. PMT. 1 hit. [Graphical view]
SMART	SM00472. MIR. 3 hits. [Graphical view]
SUPFAM	SSF82109. MIR. 1 hit.
PROSITE	PS50919. MIR. 3 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	POMT2. human.
GenomeRNAi	29954.
NextBio	52659.
SOURCE	Search...

Entry information

Entry name

POMT2_HUMAN

Accession

Primary (citable) accession number: Q9UKY4
Secondary accession number(s): Q9NSG6, Q9P1W0, Q9P1W2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	June 20, 2003
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 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.