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Q9D7I9 (TGM5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Protein-glutamine gamma-glutamyltransferase 5

EC=2.3.2.13
Alternative name(s):
Transglutaminase-5
Short name=TGase-5
Gene names
Name:Tgm5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length724 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Contributes to the formation of the cornified cell envelope of keratinocytes By similarity.

Catalytic activity

Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Cytoplasm By similarity. Note: Associated with intermediate filaments By similarity.

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCalcium
Metal-binding
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptide cross-linking

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein-glutamine gamma-glutamyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 724723Protein-glutamine gamma-glutamyltransferase 5
PRO_0000213714

Sites

Active site2831 By similarity
Active site3421 By similarity
Active site3651 By similarity
Metal binding4051Calcium By similarity
Metal binding4071Calcium By similarity
Metal binding4531Calcium By similarity
Metal binding4581Calcium By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9D7I9 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: FB6A22FDEB5F8329

FASTA72481,014
        10         20         30         40         50         60 
MAQGCPITGL EVALTDLQSS QNNVRHHTEE ISVDRLVVRR GQAFSITLYF KNRGFQPGMD 

        70         80         90        100        110        120 
SIMFVAETGP LPDLAKGTRA VFSFTGSGGP SPWIASLEAN RANSLEVSLC APPIAAVGRY 

       130        140        150        160        170        180 
LLKIRIDSYQ GFVTAYQLGE FILLFNPWCP ADSVYLESEP QRQEYVVNDY GFIYQGSKSW 

       190        200        210        220        230        240 
IRPCPWNYGQ FEENIIDICL ELLEKSLNFQ VDPSTDCALR GSPVYTSRVV CAMINSNDDN 

       250        260        270        280        290        300 
GVLNGNWSEN YVDGINPAEW TGSVAILKQW HATGCQPVRY GQCWVFAAVM CTVMRCLGIP 

       310        320        330        340        350        360 
TRVITNFDSG HDTDGNLIID EYYDNTGRIL ENMKKDTVWN FHVWNECWMA RKDLPPGYGG 

       370        380        390        400        410        420 
WQVLDATPQE TSNGLYCCGP ASVKAIKEGE IDLNYDTRFA FSMVNADCMS WLVYGGKEQK 

       430        440        450        460        470        480 
LHQDTATVGN FISTKSIQSD ERDDITESYK YEEGSLQERE VFLKALQKLQ ATRSQGPHQA 

       490        500        510        520        530        540 
NSNPFSSVPP RHNSARSPDS PSLQPSDVLQ VSLKFELLDS PKMGQDINFV LLAVNMSPQF 

       550        560        570        580        590        600 
KDLKLNLSAQ SLLHDGSPLV PFWQDTAFIT LFPEEEKSYP CKILYSQYSQ YLSTDKLIRI 

       610        620        630        640        650        660 
SALGEEKNSP EKILVNKIIT LTFPGIMINV LGAAFVNQPL TVQVVFSNPL SEPVEDCVLT 

       670        680        690        700        710        720 
LEGSGLFRKQ QRVLIGVLKP HHKASITLKT VPFKSGQRQI QANLRSNRFK DIKGYKNVYV 


DIGL 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Skin and Tongue.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK009196 mRNA. Translation: BAB26133.1.
AK132482 mRNA. Translation: BAE21192.1.
AL844548 Genomic DNA. Translation: CAM19018.1.
RefSeqNP_083075.1. NM_028799.2.
UniGeneMm.20187.

3D structure databases

ProteinModelPortalQ9D7I9.
SMRQ9D7I9. Positions 9-720.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9D7I9.

Proteomic databases

PRIDEQ9D7I9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028721; ENSMUSP00000028721; ENSMUSG00000053675.
GeneID74176.
KEGGmmu:74176.
UCSCuc008lxl.1. mouse.

Organism-specific databases

CTD9333.
MGIMGI:1921426. Tgm5.

Phylogenomic databases

eggNOGNOG293974.
GeneTreeENSGT00740000115034.
HOGENOMHOG000231695.
HOVERGENHBG004342.
InParanoidA2AQ62.
KOK05622.
OMAGVLNGNW.
OrthoDBEOG7WT40M.
PhylomeDBQ9D7I9.
TreeFamTF324278.

Gene expression databases

BgeeQ9D7I9.
CleanExMM_TGM5.
GenevestigatorQ9D7I9.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProIPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
PANTHERPTHR11590. PTHR11590. 1 hit.
PfamPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFPIRSF000459. TGM_EBP42. 1 hit.
SMARTSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio339996.
PROQ9D7I9.
SOURCESearch...

Entry information

Entry nameTGM5_MOUSE
AccessionPrimary (citable) accession number: Q9D7I9
Secondary accession number(s): A2AQ62, Q3V1F9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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