Q9BPQ5 (PIGM_TRYB2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GPI mannosyltransferase 1
EC=2.4.1.-

Alternative name(s):
GPI mannosyltransferase I
Short name=GPI-MT-I
Phosphatidylinositol-glycan biosynthesis class M protein
Short name=PIG-M
TbPIG-M

Gene names

Name:	PIGM
ORF Names:	Tb927.6.3300

Organism

Trypanosoma brucei brucei (strain 927/4 GUTat10.1) [Complete proteome]

Taxonomic identifier

999953 [NCBI]

Taxonomic lineage

Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-PI during GPI precursor assembly By similarity.
Pathway	Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Miscellaneous	In T.brucei, PIGM has a different substrate specificity compared to mammalian. Given that the protozoan parasite evades the immune response of mammalian hosts and digestion in the gut of the insect vector by means of its coat proteins tethered to the cell surface via GPI-anchors, it may be a good candidate for chemotherapy against African trypanosomiasis.
Sequence similarities	Belongs to the PIGM family.

Ontologies

Keywords
Biological process	GPI-anchor biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	GPI anchor biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	transferase activity, transferring hexosyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 430	430	GPI mannosyltransferase 1		PRO_0000246221
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 32	21	Helical; Potential
	Topological domain	33 – 72	40	Lumenal Potential
	Transmembrane	73 – 93	21	Helical; Potential
	Topological domain	94 – 115	22	Cytoplasmic Potential
	Transmembrane	116 – 136	21	Helical; Potential
	Topological domain	137 – 163	27	Lumenal Potential
	Transmembrane	164 – 184	21	Helical; Potential
	Topological domain	185 – 206	22	Cytoplasmic Potential
	Transmembrane	207 – 227	21	Helical; Potential
	Topological domain	228 – 360	133	Lumenal Potential
	Transmembrane	361 – 381	21	Helical; Potential
	Topological domain	382 – 388	7	Cytoplasmic Potential
	Transmembrane	389 – 409	21	Helical; Potential
	Topological domain	410 – 430	21	Lumenal Potential
Experimental info
	Sequence conflict	284	1	A → V in BAB20994. Ref.1
	Sequence conflict	391	1	Q → K in BAB20994. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9BPQ5 [UniParc]. Last modified July 25, 2006. Version 2. Checksum: B5AA67EB54A73FD6	FASTA	430	48,849
	10 20 30 40 50 60 MELQSLIDTV SLQKLLLLGA LLRLILIAYA FFHDQWFRVK YTDIDYMIVV DGARHMWNGG 70 80 90 100 110 120 SPFDRTTFRY TPLLAALVMP SIWIANPMGK LIFASSDLGA AWYCYGVLKS FAKERSAKWM 130 140 150 160 170 180 VSLFILFNPI VLSVSTRGNS DMLVTFMSLM VLSKFARRKC YQAAAVLGFA VHFKIYPIIY 190 200 210 220 230 240 ALPLTLGVWE QSVAASTNTW RRVVKTAVVV SICALMAAIS FAVPTVLCYM KYGQQYLNEA 250 260 270 280 290 300 FIYHVYREDH RHNFSPYWLL MYLNMARRHL GQGVDFSPRL VAFAPQAVVL SFVSYKLRRN 310 320 330 340 350 360 TAHACCVQTV LFVAFNKVCT VQYFVWFIPF LAFLFCEPKE VEDDESGGSG AFKFFSWVKA 370 380 390 400 410 420 LGVVLMWAAT IPLWVTTAVP LEFHGYSDFA QLWIVSCLFF LAMVVLASML ARIAYRVQCT 430 KCSAKSIKVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER." Maeda Y., Watanabe R., Harris C.L., Hong Y., Ohishi K., Kinoshita K., Kinoshita T. EMBO J. 20:250-261(2001) [PubMed: 11226175] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome of the African trypanosome Trypanosoma brucei." Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H., Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U., Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B., Alsmark U.C.M. , Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F., Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C., Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A., Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D., Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D., Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S., Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S., Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G., Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A., Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M., Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S., Walker D., Wanless D., Wang S., White B., White O., Whitehead S., Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E., Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E., Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A. Science 309:416-422(2005) [PubMed: 16020726] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 927/4 GUTat10.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB050105 mRNA. Translation: BAB20994.1. AC074258 Genomic DNA. Translation: AAX79949.1.
3D structure databases
ProteinModelPortal	Q9BPQ5.
ModBase	Search...
Protein family/group databases
CAZy	GT50. Glycosyltransferase Family 50.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOGENOM	HBG559139.
OMA	EFLEHTY.
Family and domain databases
InterPro	IPR007704. Mannosyltransferase_DXD. [Graphical view]
PANTHER	PTHR12886. Mannos_trans_DXD. 1 hit.
Pfam	PF05007. Mannosyl_trans. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PIGM_TRYB2

Accession

Primary (citable) accession number: Q9BPQ5
Secondary accession number(s): Q584X3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 25, 2006
Last modified:	December 14, 2011
This is version 38 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)