Q9NUD9 (PIGV_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GPI mannosyltransferase 2
EC=2.4.1.-

Alternative name(s):
GPI mannosyltransferase II
Short name=GPI-MT-II
Phosphatidylinositol-glycan biosynthesis class V protein
Short name=PIG-V

Gene names

Name:

PIGV

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

General annotation (Comments)

Function	Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly. Ref.6 Ref.7
Pathway	Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.7.
Post-translational modification	Not N-glycosylated. Ref.7
Involvement in disease	Hyperphosphatasia with mental retardation 1 (HPMRS1) [MIM:239300]: A severe syndrome characterized by elevated serum alkaline phosphatase, severe mental retardation, seizures, hypotonia, facial dysmorphism, and hypoplastic terminal phalanges. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9
Sequence similarities	Belongs to the PIGV family.
Sequence caution	The sequence CAI21625.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI21626.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI21627.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	GPI-anchor biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Disease	Disease mutation Mental retardation
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	C-terminal protein lipidation Traceable author statement. Source: Reactome preassembly of GPI anchor in ER membrane Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Inferred from direct assay Ref.7. Source: UniProtKB integral to membrane Non-traceable author statement Ref.7. Source: UniProtKB
Molecular_function	mannosyltransferase activity Inferred from mutant phenotype Ref.7. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 493	493	GPI mannosyltransferase 2		PRO_0000246234
Regions
	Topological domain	1 – 13	13	Cytoplasmic Potential
	Transmembrane	14 – 34	21	Helical; Potential
	Topological domain	35 – 77	43	Lumenal Potential
	Transmembrane	78 – 98	21	Helical; Potential
	Topological domain	99 – 113	15	Cytoplasmic Potential
	Transmembrane	114 – 134	21	Helical; Potential
	Topological domain	135 – 136	2	Lumenal Potential
	Transmembrane	137 – 157	21	Helical; Potential
	Topological domain	158 – 161	4	Cytoplasmic Potential
	Transmembrane	162 – 182	21	Helical; Potential
	Topological domain	183 – 192	10	Lumenal Potential
	Transmembrane	193 – 213	21	Helical; Potential
	Topological domain	214 – 234	21	Cytoplasmic Potential
	Transmembrane	235 – 255	21	Helical; Potential
	Topological domain	256 – 327	72	Lumenal Potential
	Transmembrane	328 – 348	21	Helical; Potential
	Topological domain	349 – 378	30	Cytoplasmic Potential
	Transmembrane	379 – 399	21	Helical; Potential
	Topological domain	400 – 469	70	Lumenal Potential
	Transmembrane	470 – 490	21	Helical; Potential
	Topological domain	491 – 493	3	Cytoplasmic Potential
Natural variations
	Natural variant	256	1	Q → K in HPMRS1. Ref.9		VAR_064190
	Natural variant	341	1	A → E in HPMRS1. Ref.9		VAR_064191
	Natural variant	341	1	A → V in HPMRS1. Ref.9		VAR_064192
	Natural variant	385	1	H → P in HPMRS1. Ref.9		VAR_064193
Experimental info
	Mutagenesis	66	1	W → L: Loss of function. Ref.7
	Mutagenesis	67	1	D → A: Loss of function. Ref.7
	Mutagenesis	293 – 294	2	PP → TA: N-glycosylated due to the creation of an acceptor site for N-glycosylation.
	Mutagenesis	308	1	Q → A: Induces a reduces enzyme activity. Ref.7
	Mutagenesis	312	1	W → L: Loss of function. Ref.7
	Sequence conflict	33	1	I → T in BAA91196. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9NUD9 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 087AE31E51BDD519	FASTA	493	55,713
	10 20 30 40 50 60 MWPQDPSRKE VLRFAVSCRI LTLMLQALFN AIIPDHHAEA FSPPRLAPSG FVDQLVEGLL 70 80 90 100 110 120 GGLSHWDAEH FLFIAEHGYL YEHNFAFFPG FPLALLVGTE LLRPLRGLLS LRSCLLISVA 130 140 150 160 170 180 SLNFLFFMLA AVALHDLGCL VLHCPHQSFY AALLFCLSPA NVFLAAGYSE ALFALLTFSA 190 200 210 220 230 240 MGQLERGRVW TSVLLFAFAT GVRSNGLVSV GFLMHSQCQG FFSSLTMLNP LRQLFKLMAS 250 260 270 280 290 300 LFLSVFTLGL PFALFQYYAY TQFCLPGSAR PIPEPLVQLA VDKGYRIAEG NEPPWCFWDV 310 320 330 340 350 360 PLIYSYIQDV YWNVGFLKYY ELKQVPNFLL AAPVAILVAW ATWTYVTTHP WLCLTLGLQR 370 380 390 400 410 420 SKNNKTLEKP DLGFLSPQVF VYVVHAAVLL LFGGLCMHVQ VLTRFLGSST PIMYWFPAHL 430 440 450 460 470 480 LQDQEPLLRS LKTVPWKPLA EDSPPGQKVP RNPIMGLLYH WKTCSPVTRY ILGYFLTYWL 490 LGLLLHCNFL PWT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]. Tissue: Lung.
[5]	"Familial hyperphosphatase with mental retardation, seizures, and neurologic deficits." Mabry C.C., Bautista A., Kirk R.F., Dubilier L.D., Braunstein H., Koepke J.A. J. Pediatr. 77:74-85(1970) [PubMed] [Europe PMC] [Abstract] Cited for: DESCRIPTION OF HYPERPHOSPHATASIA WITH MENTAL RETARDATION SYNDROME.
[6]	"Saccharomyces cerevisiae Ybr004c and its human homologue are required for addition of the second mannose during glycosylphosphatidylinositol precursor assembly." Fabre A.-L., Orlean P., Taron C.H. FEBS J. 272:1160-1168(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol." Kang J.Y., Hong Y., Ashida H., Shishioh N., Murakami Y., Morita Y.S., Maeda Y., Kinoshita T. J. Biol. Chem. 280:9489-9497(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, LACK OF GLYCOSYLATION, MUTAGENESIS OF TRP-66; ASP-67; 293-PRO-PRO-294; GLN-308 AND TRP-312.
[8]	"Hyperphosphatasia with seizures, neurologic deficit, and characteristic facial features: Five new patients with Mabry syndrome." Thompson M.D., Nezarati M.M., Gillessen-Kaesbach G., Meinecke P., Mendoza R., Mornet E., Brun-Heath I., Squarcioni C.P., Legeai-Mallet L., Munnich A., Cole D.E. Am. J. Med. Genet. A 152:1661-1669(2010) [PubMed] [Europe PMC] [Abstract] Cited for: DESCRIPTION OF HYPERPHOSPHATASIA WITH MENTAL RETARDATION SYNDROME.
[9]	"Identity-by-descent filtering of exome sequence data identifies PIGV mutations in hyperphosphatasia mental retardation syndrome." Krawitz P.M., Schweiger M.R., Rodelsperger C., Marcelis C., Kolsch U., Meisel C., Stephani F., Kinoshita T., Murakami Y., Bauer S., Isau M., Fischer A., Dahl A., Kerick M., Hecht J., Kohler S., Jager M., Grunhagen J. , de Condor B.J., Doelken S., Brunner H.G., Meinecke P., Passarge E., Thompson M.D., Cole D.E., Horn D., Roscioli T., Mundlos S., Robinson P.N. Nat. Genet. 42:827-829(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HPMRS1 LYS-256; VAL-341; GLU-341 AND PRO-385.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK000484 mRNA. Translation: BAA91196.1. AL034380 Genomic DNA. Translation: CAB92120.1. AL034380 Genomic DNA. Translation: CAI21625.1. Sequence problems. AL034380 Genomic DNA. Translation: CAI21626.1. Sequence problems. AL034380 Genomic DNA. Translation: CAI21627.1. Sequence problems. CH471059 Genomic DNA. Translation: EAX07790.1. CH471059 Genomic DNA. Translation: EAX07791.1. CH471059 Genomic DNA. Translation: EAX07792.1. BC013568 mRNA. Translation: AAH13568.1.
IPI	IPI00100298.
RefSeq	NP_001189483.1. NM_001202554.1. NP_060307.2. NM_017837.3.
UniGene	Hs.259605. Hs.732254.
3D structure databases
ProteinModelPortal	Q9NUD9.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000078527.
Protein family/group databases
CAZy	GT76. Glycosyltransferase Family 76.
PTM databases
PhosphoSite	Q9NUD9.
Polymorphism databases
DMDM	74752975.
Proteomic databases
PaxDb	Q9NUD9.
PRIDE	Q9NUD9.
Protocols and materials databases
DNASU	55650.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000078527; ENSP00000078527; ENSG00000060642. ENST00000374145; ENSP00000363260; ENSG00000060642. ENST00000430292; ENSP00000399067; ENSG00000060642. ENST00000431541; ENSP00000388425; ENSG00000060642. ENST00000455364; ENSP00000406080; ENSG00000060642.
GeneID	55650.
KEGG	hsa:55650.
UCSC	uc001bmz.3. human.
Organism-specific databases
CTD	55650.
GeneCards	GC01P027113.
H-InvDB	HIX0159960.
HGNC	HGNC:26031. PIGV.
MIM	239300. phenotype. 610274. gene.
neXtProt	NX_Q9NUD9.
Orphanet	247262. Hyperphosphatasia intellectual deficiency syndrome.
PharmGKB	PA134952230.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5542.
HOGENOM	HOG000232162.
HOVERGEN	HBG080592.
InParanoid	Q9NUD9.
KO	K07542.
OMA	AYTQFCL.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00196.
Gene expression databases
ArrayExpress	Q9NUD9.
Bgee	Q9NUD9.
CleanEx	HS_PIGV.
Genevestigator	Q9NUD9.
GermOnline	ENSG00000060642. Homo sapiens.
Family and domain databases
InterPro	IPR007315. GPI_Mannosyltransferase_2-like. [Graphical view]
PANTHER	PTHR12468. PTHR12468. 1 hit.
Pfam	PF04188. Mannosyl_trans2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	55650.
NextBio	60346.
SOURCE	Search...

Entry information

Entry name

PIGV_HUMAN

Accession

Primary (citable) accession number: Q9NUD9
Secondary accession number(s): D3DPL2 , Q5JYG7, Q5JYG8, Q5JYG9, Q9NX26

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 90 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.