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Q8C2R7 (PIGM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processGPI-anchor biosynthesis
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processGPI anchor biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 423423GPI mannosyltransferase 1
PRO_0000246215

Regions

Topological domain1 – 1717Cytoplasmic Potential
Transmembrane18 – 3821Helical; Potential
Topological domain39 – 8951Lumenal Potential
Transmembrane90 – 11021Helical; Potential
Topological domain111 – 16959Cytoplasmic Potential
Transmembrane170 – 19021Helical; Potential
Topological domain191 – 22434Lumenal Potential
Transmembrane225 – 24521Helical; Potential
Topological domain246 – 28742Cytoplasmic Potential
Transmembrane288 – 30821Helical; Potential
Topological domain309 – 32921Lumenal Potential
Transmembrane330 – 35021Helical; Potential
Topological domain351 – 3577Cytoplasmic Potential
Transmembrane358 – 37821Helical; Potential
Topological domain379 – 3846Lumenal Potential
Transmembrane385 – 40521Helical; Potential
Topological domain406 – 42318Cytoplasmic Potential

Experimental info

Sequence conflict2061Q → H in BAC40156. Ref.1
Sequence conflict2061Q → H in AAH05650. Ref.2
Sequence conflict3471M → I in BAC40156. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8C2R7 [UniParc].

Last modified July 25, 2006. Version 2.
Checksum: 0862F05F69894FEE

FASTA42349,789
        10         20         30         40         50         60 
MSYPMHWGEW ILNFRVPPAG 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 ASLVLSTLYF IEKRLIACAA VFYGFAVHMK 

       190        200        210        220        230        240 
MYPVTYILPI ALHLRPERDD DERLRQARFS FQARLYDFLR RLCSWAVLLF VAVAGLTFVA 

       250        260        270        280        290        300 
LSFGFYYKYG WEFLEHTYFY HLTRRDIRHN FSPYFYMLYL TAESKWSFTL GIAAFLPQFI 

       310        320        330        340        350        360 
LLSAASFAYY RDLVFCCFLH TSIFVTFNKV CTSQYFLWYL CLLPLVMPLV RMPWKRAVVL 

       370        380        390        400        410        420 
LLFWFIGQAL WLAPAYVLEF QGKNTFLFIW LAGLFFLLIN CSILIQIISH YKEDRLTERI 


KYD

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Aorta, Cerebellum, Colon, Thymus and Vein.
[2]"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].
Strain: NMRI.
Tissue: Eye and Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK018560 mRNA. Translation: BAB31275.1.
AK040397 mRNA. Translation: BAC30585.1.
AK043216 mRNA. Translation: BAC31497.1.
AK080242 mRNA. Translation: BAC37857.1.
AK088117 mRNA. Translation: BAC40156.1.
BC005650 mRNA. Translation: AAH05650.1.
BC083115 mRNA. Translation: AAH83115.1.
IPIIPI00458715.
RefSeqNP_080510.1. NM_026234.4.
UniGeneMm.26612.

3D structure databases

ProteinModelPortalQ8C2R7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8C2R7.

Protein family/group databases

CAZyGT50. Glycosyltransferase Family 50.

PTM databases

PhosphoSiteQ8C2R7.

Proteomic databases

PRIDEQ8C2R7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000052455; ENSMUSP00000052838; ENSMUSG00000050229.
GeneID67556.
KEGGmmu:67556.
UCSCuc007dqk.2. mouse.

Organism-specific databases

CTD93183.
MGIMGI:1914806. Pigm.

Phylogenomic databases

eggNOGmaNOG18045.
GeneTreeENSGT00390000017728.
HOGENOMHBG559139.
HOVERGENHBG082137.
InParanoidQ8C2R7.
OMAEFLEHTY.
OrthoDBEOG4Q2DG6.
PhylomeDBQ8C2R7.

Gene expression databases

ArrayExpressQ8C2R7.
BgeeQ8C2R7.
GenevestigatorQ8C2R7.
GermOnlineENSMUSG00000050229. Mus musculus.

Family and domain databases

InterProIPR007704. Mannosyltransferase_DXD.
[Graphical view]
KOK05284.
PANTHERPTHR12886. Mannos_trans_DXD. 1 hit.
PfamPF05007. Mannosyl_trans. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio324913.
SOURCESearch...

Entry information

Entry namePIGM_MOUSE
AccessionPrimary (citable) accession number: Q8C2R7
Secondary accession number(s): Q8C917, Q99J22, Q9D315
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: November 16, 2011
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents