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Q7TPN3 (PIGV_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 72. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GPI mannosyltransferase 2
EC=2.4.1.-
Alternative name(s):
GPI mannosyltransferase II
Short name=GPI-MT-II
Phosphatidylinositol-glycan biosynthesis class V protein
Short name=PIG-V
Gene names
Name:Pigv
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly By similarity.

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Post-translational modification

Not N-glycosylated By similarity.

Sequence similarities

Belongs to the PIGV family.

Sequence caution

The sequence BAC33023.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGPI-anchor biosynthesis
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   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-UniPathway

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmannosyltransferase activity

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7TPN3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q7TPN3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     27-400: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493GPI mannosyltransferase 2
PRO_0000246235

Regions

Topological domain1 – 1313Cytoplasmic Potential
Transmembrane14 – 3421Helical; Potential
Topological domain35 – 7743Lumenal Potential
Transmembrane78 – 9821Helical; Potential
Topological domain99 – 11315Cytoplasmic Potential
Transmembrane114 – 13421Helical; Potential
Topological domain135 – 1362Lumenal Potential
Transmembrane137 – 15721Helical; Potential
Topological domain158 – 1614Cytoplasmic Potential
Transmembrane162 – 18221Helical; Potential
Topological domain183 – 19210Lumenal Potential
Transmembrane193 – 21321Helical; Potential
Topological domain214 – 23421Cytoplasmic Potential
Transmembrane235 – 25521Helical; Potential
Topological domain256 – 32772Lumenal Potential
Transmembrane328 – 34821Helical; Potential
Topological domain349 – 37830Cytoplasmic Potential
Transmembrane379 – 39921Helical; Potential
Topological domain400 – 46970Lumenal Potential
Transmembrane470 – 49021Helical; Potential
Topological domain491 – 4933Cytoplasmic Potential

Natural variations

Alternative sequence27 – 400374Missing in isoform 2.
VSP_019840

Experimental info

Sequence conflict2181C → F in BAC34995. Ref.1
Sequence conflict4601D → N in AAH55060. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 25, 2006. Version 2.
Checksum: 8A176D43F3CB7F4C

FASTA49355,026
        10         20         30         40         50         60 
MGLLDPSQKE VLRFAVNCRI LTLVLQALFN LIIPDHHADA FCPPRLAPSG SADQLVEGLL 

        70         80         90        100        110        120 
GGLSRWDAEH FLFIAEHGYL YEHNFAFFPG FPLALLMGTE LLRPLQGLLS QRSCLLVSVA 

       130        140        150        160        170        180 
LLNLLFSVLA AVALHDLGCL VLHCPRQALC AALLFCISPA NVFLAAGYSE ALFAFLTFSA 

       190        200        210        220        230        240 
MGQLERGRGW ASGLLFALAA GVRSNGLVSL GFLLHSQCRG FCSSLAVLSP WKPLVKLMAS 

       250        260        270        280        290        300 
VCLSVLIVSL PFALFQYRAY IQFCSPGSAP SIPEPLLQLA ADKGYRLAGE NAPPWCSWDL 

       310        320        330        340        350        360 
PLIYNYIQDV YWNVGLLRYY ELKQVPNFLL ATPVTVLVVW ATWTYVTTHP WLCLTLGLQR 

       370        380        390        400        410        420 
TKDRENPEKP HRGFLSPKVF VYLVHAAALL VFGGLCMHVQ VLTRFLASST PIMYWFPAHL 

       430        440        450        460        470        480 
LQDQEPLLRC VDTEPGKLPQ EKSPPGQKAP RNCLMKLFYD WKRCSPVTRC VLVYFLTYWL 

       490 
LGLILHCNFL PWT

« Hide

Isoform 2 [UniParc].

Checksum: 0B052659B20754C8
Show »

FASTA11913,882

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Adrenal gland, Cerebellum, Corpora quadrigemina and Lung.
[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] (ISOFORM 1).
Strain: FVB/N.
Tissue: Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK046527 mRNA. Translation: BAC32773.1.
AK047322 mRNA. Translation: BAC33023.1. Different initiation.
AK052446 mRNA. Translation: BAC34995.1.
AK080590 mRNA. Translation: BAC37950.1.
AK080858 mRNA. Translation: BAC38047.1.
AK148285 mRNA. Translation: BAE28458.1.
BC055060 mRNA. Translation: AAH55060.1.
IPIIPI00226659.
IPI00403376.
RefSeqNP_001139427.1. NM_001145955.1.
NP_001139428.1. NM_001145956.1.
NP_848813.3. NM_178698.5.
UniGeneMm.217004.

3D structure databases

ProteinModelPortalQ7TPN3.
ModBaseSearch...

Protein family/group databases

CAZyGT76. Glycosyltransferase Family 76.

PTM databases

PhosphoSiteQ7TPN3.

Proteomic databases

PRIDEQ7TPN3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000062118; ENSMUSP00000050647; ENSMUSG00000043257.
ENSMUST00000067902; ENSMUSP00000065601; ENSMUSG00000043257.
GeneID230801.
KEGGmmu:230801.

Organism-specific databases

CTD55650.
MGIMGI:2442480. Pigv.

Phylogenomic databases

eggNOGCOG5542.
GeneTreeENSGT00390000013174.
HOGENOMHOG000232162.
HOVERGENHBG080592.
InParanoidQ7TPN3.
KOK07542.
OMAAYTQFCL.
OrthoDBEOG48D0V8.

Enzyme and pathway databases

UniPathwayUPA00196.

Gene expression databases

ArrayExpressQ7TPN3.
BgeeQ7TPN3.
GenevestigatorQ7TPN3.
GermOnlineENSMUSG00000043257. Mus musculus.

Family and domain databases

InterProIPR007315. GPI_Mannosyltransferase_2-like.
[Graphical view]
PANTHERPTHR12468. PTHR12468. 1 hit.
PfamPF04188. Mannosyl_trans2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPIGV. mouse.
NextBio380172.
SOURCESearch...

Entry information

Entry namePIGV_MOUSE
AccessionPrimary (citable) accession number: Q7TPN3
Secondary accession number(s): Q8BGL2 expand/collapse secondary AC list , Q8BJR5, Q8BWH9, Q8BXF5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: April 3, 2013
This is version 72 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents