NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
DOI=10.1002/yea.678; PubMed=11255248 [NCBI, ExPASy, EBI, Israel, Japan]
Agaphonov M.O., Packeiser A.N., Chechenova M.B., Choi E.-S., Ter-Avanesyan M.D.;
"Mutation of the homologue of GDP-mannose pyrophosphorylase alters cell wall structure, protein glycosylation and secretion in Hansenula polymorpha.";
Yeast 18:391-402(2001).

Comments

FUNCTION: Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint.
CATALYTIC ACTIVITY: GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose.
PATHWAY: Protein modification; protein glycosylation .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the transferase hexapeptide repeat family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF234177; AAF60300.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q97R46; 1HM0. [HSSP ENTRY / PDB]

ModBase

Q9P8N0.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004475;	Molecular function: mannose-1-phosphate guanylyltransferase activity (inferred from electronic annotation from EC).
GO:0009058;	Biological process: biosynthetic process (inferred from electronic annotation from InterPro).
GO:0007049;	Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001451; Hexapep_transf.
IPR005835; NTP_transferase.
Graphical view of domain structure.

Pfam

PF00132; Hexapep; 4.
PF00483; NTP_transferase; 1.
Pfam graphical view of domain structure.

PROSITE

PS00101; HEXAPEP_TRANSFERASES; 1.

ProtoNet

Q9P8N0.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell cycle; Cytoplasm; Nucleotidyltransferase; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 364`	`364`		`Mannose-1-phosphate guanyltransferase.`	`PRO_0000238492`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 40065 Da [This is the MW of the unprocessed precursor]

CRC64: 1700BCA9AF0308FD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKGLILVGGY GTRLRPLTLS LPKPLVEFGN RPMILHQIEA LANAGCTDIV LAVNYKPEVM 

        70         80         90        100        110        120 
VGALKQYEKE YGVSITFSVE EEPLGTAGPL KLAEKILKKD NTPIFVLNSD VICEYPLRDL 

       130        140        150        160        170        180 
LEFHTAHGGE ATIVATKVDE PSKYGVIVHD RDVPNLIERF VEKPVEFVGN RINAGIYVLN 

       190        200        210        220        230        240 
PSVIDLIEMR PTSIEHETFP ILVEQKKLYS FDLPGYWMDV GQPKDFLSGM CLYLSALTKK 

       250        260        270        280        290        300 
NSNLLTSTSE EYVNGGNVLI DPSAKIGKGC KIGPNVVIGP NCIIGDGVRI QRSTILKNSQ 

       310        320        330        340        350        360 
IKDHAWVKST IVGWNSTVGK WARLEGVTVL GEDVTVKDEV YVNGGKVLPH KSIKDNVETP 


QIIM

Q9P8N0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools