O75352 (MPU1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mannose-P-dolichol utilization defect 1 protein

Alternative name(s):
Suppressor of Lec15 and Lec35 glycosylation mutation homolog
Short name=SL15

Gene names

Name:

MPDU1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	247 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for normal utilization of mannose-dolichol phosphate (Dol-P-Man) in the synthesis of N-linked and O-linked oligosaccharides and GPI anchors By similarity.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Involvement in disease	Defects in MPDU1 are the cause of congenital disorder of glycosylation type 1F (CDG1F) [MIM:609180]. CDGs are a family of severe inherited diseases caused by a defect in protein N-glycosylation. They are characterized by under-glycosylated serum proteins. These multisystem disorders present with a wide variety of clinical features, such as disorders of the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. Ref.8 Ref.9
Sequence similarities	Belongs to the MPDU1 family. Contains 2 PQ-loop domains.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Congenital disorder of glycosylation Disease mutation
Domain	Repeat Transmembrane Transmembrane helix
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	dolichol-linked oligosaccharide biosynthetic process Traceable author statement Ref.9. Source: UniProtKB protein folding Non-traceable author statement. Source: UniProtKB
Cellular component	endoplasmic reticulum membrane Non-traceable author statement. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from direct assay. Source: HPA
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HERC2	O95714	1	EBI-1046501,EBI-1058922
MORF4L2	Q15014	1	EBI-1046501,EBI-399257
PMVK	Q15126	1	EBI-1046501,EBI-1055562
QRICH2	Q9H0J4	1	EBI-1046501,EBI-1053637
RPS3A	P61247	1	EBI-1046501,EBI-352378
SLC1A5	Q15758	1	EBI-1046501,EBI-356576

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 247	246	Mannose-P-dolichol utilization defect 1 protein		PRO_0000221034
Regions
	Transmembrane	74 – 94	21	Helical; Potential
	Transmembrane	100 – 120	21	Helical; Potential
	Transmembrane	131 – 151	21	Helical; Potential
	Transmembrane	185 – 205	21	Helical; Potential
	Transmembrane	213 – 233	21	Helical; Potential
	Domain	39 – 105	67	PQ-loop 1
	Domain	159 – 216	58	PQ-loop 2
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.6
Natural variations
	Natural variant	73	1	G → E in CDG1F. Ref.9		VAR_021388
	Natural variant	74	1	L → S in CDG1F. Ref.8		VAR_021389
	Natural variant	119	1	L → P in CDG1F. Ref.9		VAR_021390
	Natural variant	225	1	G → S. Corresponds to variant rs16956808 [ dbSNP | Ensembl ].		VAR_047757
	Natural variant	229	1	A → T. Ref.5 Corresponds to variant rs10852891 [ dbSNP | Ensembl ].		VAR_047758
Experimental info
	Sequence conflict	66	1	L → R in AAC39875. Ref.1
	Sequence conflict	181	1	H → Y in AAC39875. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O75352 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 8C840B26F06DFD9B	FASTA	247	26,638
	10 20 30 40 50 60 MAAEADGPLK RLLVPILLPE KCYDQLFVQW DLLHVPCLKI LLSKGLGLGI VAGSLLVKLP 70 80 90 100 110 120 QVFKILGAKS AEGLSLQSVM LELVALTGTM VYSITNNFPF SSWGEALFLM LQTITICFLV 130 140 150 160 170 180 MHYRGQTVKG VAFLACYGLV LLVLLSPLTP LTVVTLLQAS NVPAVVVGRL LQAATNYHNG 190 200 210 220 230 240 HTGQLSAITV FLLFGGSLAR IFTSIQETGD PLMAGTFVVS SLCNGLIAAQ LLFYWNAKPP HKQKKAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning." Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z. Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed: 9653160] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[2]	"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].
[3]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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].
[5]	"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], VARIANT THR-229. Tissue: Lung.
[6]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"A mutation in the human MPDU1 gene causes congenital disorder of glycosylation type If (CDG-If)." Kranz C., Denecke J., Lehrman M.A., Ray S., Kienz P., Kreissel G., Sagi D., Peter-Katalinic J., Freeze H.H., Schmid T., Jackowski-Dohrmann S., Harms E., Marquardt T. J. Clin. Invest. 108:1613-1619(2001) [PubMed: 11733556] [Abstract] Cited for: VARIANT CDG1F SER-74.
[9]	"MPDU1 mutations underlie a novel human congenital disorder of glycosylation, designated type If." Schenk B., Imbach T., Frank C.G., Grubenmann C.E., Raymond G.V., Hurvitz H., Raas-Rotschild A., Luder A.S., Jaeken J., Berger E.G., Matthijs G., Hennet T., Aebi M. J. Clin. Invest. 108:1687-1695(2001) [PubMed: 11733564] [Abstract] Cited for: VARIANTS CDG1F GLU-73 AND PRO-119.
[10]	Erratum Schenk B., Imbach T., Frank C.G., Grubenmann C.E., Raymond G.V., Hurvitz H., Korn-Lubetzki I., Revel-Vik S., Raas-Rotschild A., Luder A.S., Jaeken J., Berger E.G., Matthijs G., Hennet T., Aebi M. J. Clin. Invest. 111:925-925(2001)
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF038961 mRNA. Translation: AAC39875.1. AK075299 mRNA. Translation: BAG52103.1. AC016876 Genomic DNA. No translation available. CH471108 Genomic DNA. Translation: EAW90161.1. BC001898 mRNA. Translation: AAH01898.1.
IPI	IPI00025292.
RefSeq	NP_004861.2. NM_004870.3.
UniGene	Hs.246381.
3D structure databases
ProteinModelPortal	O75352.
ModBase	Search...
Protein-protein interaction databases
STRING	O75352.
Proteomic databases
PRIDE	O75352.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000250124; ENSP00000250124; ENSG00000129255.
GeneID	9526.
KEGG	hsa:9526.
Organism-specific databases
CTD	9526.
GeneCards	GC17P007486.
H-InvDB	HIX0013504.
HGNC	HGNC:7207. MPDU1.
HPA	HPA014845.
MIM	604041. gene. 609180. phenotype.
neXtProt	NX_O75352.
Orphanet	79323. CDG syndrome type If.
PharmGKB	PA30913.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13569.
HOVERGEN	HBG000421.
OrthoDB	EOG4BK54W.
PhylomeDB	O75352.
Gene expression databases
ArrayExpress	O75352.
Bgee	O75352.
CleanEx	HS_MPDU1.
Genevestigator	O75352.
GermOnline	ENSG00000129255. Homo sapiens.
Family and domain databases
InterPro	IPR006603. CTNS. IPR016817. MannP-dilichol_defect-1. [Graphical view]
KO	K09660.
PANTHER	PTHR12226. PTHR12226. 1 hit.
PIRSF	PIRSF023381. MannP-dilichol_defect-1p. 1 hit.
SMART	SM00679. CTNS. 2 hits. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

MPU1_HUMAN

Accession

Primary (citable) accession number: O75352
Secondary accession number(s): B3KQP1, Q9BUU8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	November 25, 2008
Last modified:	January 25, 2012
This is version 88 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.