Q9EQY6 (PIGM_RAT) 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

Gene names

Name:

Pigm

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	423 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-acyl-PI during GPI precursor assembly By similarity.
Pathway	Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
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 Reference proteome
Gene Ontology (GO)
Biological_process	GPI anchor biosynthetic process Inferred from direct assay Ref.1. Source: RGD
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	mannosyltransferase activity Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 423	423	GPI mannosyltransferase 1		PRO_0000246217
Regions
	Topological domain	1 – 17	17	Cytoplasmic Potential
	Transmembrane	18 – 38	21	Helical; Potential
	Topological domain	39 – 89	51	Lumenal Potential
	Transmembrane	90 – 110	21	Helical; Potential
	Topological domain	111 – 169	59	Cytoplasmic Potential
	Transmembrane	170 – 190	21	Helical; Potential
	Topological domain	191 – 224	34	Lumenal Potential
	Transmembrane	225 – 245	21	Helical; Potential
	Topological domain	246 – 287	42	Cytoplasmic Potential
	Transmembrane	288 – 308	21	Helical; Potential
	Topological domain	309 – 329	21	Lumenal Potential
	Transmembrane	330 – 350	21	Helical; Potential
	Topological domain	351 – 357	7	Cytoplasmic Potential
	Transmembrane	358 – 378	21	Helical; Potential
	Topological domain	379 – 384	6	Lumenal Potential
	Transmembrane	385 – 405	21	Helical; Potential
	Topological domain	406 – 423	18	Cytoplasmic Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9EQY6 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 7FC172B5DF98992D	FASTA	423	49,594
	10 20 30 40 50 60 MSYTKHWGEW FLNLRVPPAG VFGVAFLARV ALVFYGVFQD RTLLVRYTDI DYHVFTDAAR 70 80 90 100 110 120 FVTEGRSPYL RATYRYTPLL SWLLTPNVYL SELFGKFLFI SCDLLTAFLL YRLLLLKGLG 130 140 150 160 170 180 RRQACGYCVF WLLNPLPMAV SSRGNADSIV ASLVLTTLYL IEKRLIACAA VFYGFAVHMK 190 200 210 220 230 240 MYPVTYILPI ALHLRPERDS DEGLRLARYS FQARLYDFLK RLCSWAVLLF VAIAGLTFLA 250 260 270 280 290 300 LSFGFYYKYG WEFLEHTYLY HLTRRDIRHN FSPYFYMLYL TAESKWSFTL GIAAFLPQFI 310 320 330 340 350 360 LLSAASFAYY RDLVFCCFLH TSIFVTFNKV CTSQYFLWYL CLLPLVMPLV RMPWKRAVVL 370 380 390 400 410 420 LMLWFIGQAL WLAPAYVLEF QGKNTFLFIW LAGLFFLLIN CSILIQIISH YKEDRLTERI KYD

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB028126 mRNA. Translation: BAB18566.1.
IPI	IPI00190580.
RefSeq	NP_077058.1. NM_024144.1.
UniGene	Rn.163231.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000010551.
Protein family/group databases
CAZy	GT50. Glycosyltransferase Family 50.
Proteomic databases
PRIDE	Q9EQY6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000010551; ENSRNOP00000010551; ENSRNOG00000007735.
GeneID	79112.
KEGG	rno:79112.
UCSC	RGD:71041. rat.
Organism-specific databases
CTD	93183.
RGD	71041. Pigm.
Phylogenomic databases
eggNOG	NOG268708.
GeneTree	ENSGT00390000017728.
HOGENOM	HOG000186884.
HOVERGEN	HBG082137.
InParanoid	Q9EQY6.
KO	K05284.
OMA	EFLEHTY.
OrthoDB	EOG4Q2DG6.
Enzyme and pathway databases
UniPathway	UPA00196.
Gene expression databases
Genevestigator	Q9EQY6.
GermOnline	ENSRNOG00000007735. Rattus norvegicus.
Family and domain databases
InterPro	IPR007704. Mannosyltransferase_DXD. [Graphical view]
PANTHER	PTHR12886. PTHR12886. 1 hit.
Pfam	PF05007. Mannosyl_trans. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	614510.

Entry information

Entry name

PIGM_RAT

Accession

Primary (citable) accession number: Q9EQY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	March 1, 2001
Last modified:	April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program