Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

GPI mannosyltransferase 1

Gene

Pigm

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly (By similarity).By similarity

Pathwayi: glycosylphosphatidylinositol-anchor biosynthesis

This protein is involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis, which is part of Glycolipid biosynthesis.
View all proteins of this organism that are known to be involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis and in Glycolipid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

GPI-anchor biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-162710. Synthesis of glycosylphosphatidylinositol (GPI).
UniPathwayiUPA00196.

Protein family/group databases

CAZyiGT50. Glycosyltransferase Family 50.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Pigm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1914806. Pigm.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1717CytoplasmicSequence analysisAdd
BLAST
Transmembranei18 – 3821HelicalSequence analysisAdd
BLAST
Topological domaini39 – 8951LumenalSequence analysisAdd
BLAST
Transmembranei90 – 11021HelicalSequence analysisAdd
BLAST
Topological domaini111 – 16959CytoplasmicSequence analysisAdd
BLAST
Transmembranei170 – 19021HelicalSequence analysisAdd
BLAST
Topological domaini191 – 22434LumenalSequence analysisAdd
BLAST
Transmembranei225 – 24521HelicalSequence analysisAdd
BLAST
Topological domaini246 – 28742CytoplasmicSequence analysisAdd
BLAST
Transmembranei288 – 30821HelicalSequence analysisAdd
BLAST
Topological domaini309 – 32921LumenalSequence analysisAdd
BLAST
Transmembranei330 – 35021HelicalSequence analysisAdd
BLAST
Topological domaini351 – 3577CytoplasmicSequence analysis
Transmembranei358 – 37821HelicalSequence analysisAdd
BLAST
Topological domaini379 – 3846LumenalSequence analysis
Transmembranei385 – 40521HelicalSequence analysisAdd
BLAST
Topological domaini406 – 42318CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423GPI mannosyltransferase 1PRO_0000246215Add
BLAST

Proteomic databases

EPDiQ8C2R7.
MaxQBiQ8C2R7.
PaxDbiQ8C2R7.
PRIDEiQ8C2R7.

PTM databases

iPTMnetiQ8C2R7.
PhosphoSiteiQ8C2R7.

Expressioni

Gene expression databases

BgeeiQ8C2R7.
GenevisibleiQ8C2R7. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000052838.

Structurei

3D structure databases

ProteinModelPortaliQ8C2R7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PIGM family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3893. Eukaryota.
ENOG410XRDY. LUCA.
GeneTreeiENSGT00390000017728.
HOGENOMiHOG000186884.
HOVERGENiHBG082137.
InParanoidiQ8C2R7.
KOiK05284.
OMAiEFLEHTY.
OrthoDBiEOG7SBNQM.
PhylomeDBiQ8C2R7.
TreeFamiTF314752.

Family and domain databases

InterProiIPR007704. Mannosyltransferase_DXD.
[Graphical view]
PANTHERiPTHR12886. PTHR12886. 1 hit.
PfamiPF05007. Mannosyl_trans. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8C2R7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYPMHWGEW ILNFRVPPAG VFGVAFLARV ALVFYGVFQD RTLLVRYTDI
60 70 80 90 100
DYHVFTDAAR FVTEGRSPYL RATYRYTPLL SWLLTPNVYL SELFGKFLFI
110 120 130 140 150
SCDLLTAFLL YRLLLLKGLG RRQACGYCVF WLLNPLPMAV SSRGNADSIV
160 170 180 190 200
ASLVLSTLYF IEKRLIACAA VFYGFAVHMK MYPVTYILPI ALHLRPERDD
210 220 230 240 250
DERLRQARFS FQARLYDFLR RLCSWAVLLF VAVAGLTFVA LSFGFYYKYG
260 270 280 290 300
WEFLEHTYFY HLTRRDIRHN FSPYFYMLYL TAESKWSFTL GIAAFLPQFI
310 320 330 340 350
LLSAASFAYY RDLVFCCFLH TSIFVTFNKV CTSQYFLWYL CLLPLVMPLV
360 370 380 390 400
RMPWKRAVVL LLFWFIGQAL WLAPAYVLEF QGKNTFLFIW LAGLFFLLIN
410 420
CSILIQIISH YKEDRLTERI KYD
Length:423
Mass (Da):49,789
Last modified:July 25, 2006 - v2
Checksum:i0862F05F69894FEE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061Q → H in BAC40156 (PubMed:16141072).Curated
Sequence conflicti206 – 2061Q → H in AAH05650 (PubMed:15489334).Curated
Sequence conflicti347 – 3471M → I in BAC40156 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15513.1.
RefSeqiNP_080510.1. NM_026234.4.
UniGeneiMm.26612.

Genome annotation databases

EnsembliENSMUST00000052455; ENSMUSP00000052838; ENSMUSG00000050229.
GeneIDi67556.
KEGGimmu:67556.
UCSCiuc007dqk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15513.1.
RefSeqiNP_080510.1. NM_026234.4.
UniGeneiMm.26612.

3D structure databases

ProteinModelPortaliQ8C2R7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000052838.

Protein family/group databases

CAZyiGT50. Glycosyltransferase Family 50.

PTM databases

iPTMnetiQ8C2R7.
PhosphoSiteiQ8C2R7.

Proteomic databases

EPDiQ8C2R7.
MaxQBiQ8C2R7.
PaxDbiQ8C2R7.
PRIDEiQ8C2R7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052455; ENSMUSP00000052838; ENSMUSG00000050229.
GeneIDi67556.
KEGGimmu:67556.
UCSCiuc007dqk.2. mouse.

Organism-specific databases

CTDi93183.
MGIiMGI:1914806. Pigm.

Phylogenomic databases

eggNOGiKOG3893. Eukaryota.
ENOG410XRDY. LUCA.
GeneTreeiENSGT00390000017728.
HOGENOMiHOG000186884.
HOVERGENiHBG082137.
InParanoidiQ8C2R7.
KOiK05284.
OMAiEFLEHTY.
OrthoDBiEOG7SBNQM.
PhylomeDBiQ8C2R7.
TreeFamiTF314752.

Enzyme and pathway databases

UniPathwayiUPA00196.
ReactomeiR-MMU-162710. Synthesis of glycosylphosphatidylinositol (GPI).

Miscellaneous databases

PROiQ8C2R7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C2R7.
GenevisibleiQ8C2R7. MM.

Family and domain databases

InterProiIPR007704. Mannosyltransferase_DXD.
[Graphical view]
PANTHERiPTHR12886. PTHR12886. 1 hit.
PfamiPF05007. Mannosyl_trans. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NMRI.
    Tissue: Eye and Mammary tumor.

Entry informationi

Entry nameiPIGM_MOUSE
AccessioniPrimary (citable) accession number: Q8C2R7
Secondary accession number(s): Q8C917, Q99J22, Q9D315
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: June 8, 2016
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.