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P52183 (ANNU_SCHAM) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Annulin
Alternative name(s):
Protein-glutamine gamma-glutamyltransferase
EC=2.3.2.13
Transglutaminase
OrganismSchistocerca americana (American grasshopper)
Taxonomic identifier7009 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraOrthopteroideaOrthopteraCaeliferaAcridomorphaAcridoideaAcrididaeCyrtacanthacridinaeSchistocerca

Protein attributes

Sequence length772 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Participates in morphogenetic activities of the cells, maybe by stabilizing the membrane or subcortical structures of cells that are under mechanical stress. Probably catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.

Catalytic activity

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

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Note: Intracellular and peripherally associated with the inner leaflet of the cell membrane, using a fatty acid linkage.

Tissue specificity

Has an annular, or ring-like expression pattern in epithelial annuli of developing limb segment boundary cells. In embryos, it is seen in gastrulating cells, in cells surrounding rapidly dividing neuroblasts, and in muscle pioneer cells invaginating to form apodemes.

Developmental stage

Expression of this protein in embryos and limbs is associated with areas undergoing movements, morphogenetic rearrangements, or rapid cell division. Expression of annulin precedes the first morphological signs of segmentation in the developing limbs.

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   LigandCalcium
Metal-binding
   Molecular functionAcyltransferase
Transferase
   PTMLipoprotein
Palmitate
Gene Ontology (GO)
   Biological_processpeptide cross-linking

Inferred from electronic annotation. Source: InterPro

   Cellular_componentplasma membrane

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

Chain1 – 772772Annulin
PRO_0000213718

Sites

Active site4001 By similarity
Active site4271 By similarity
Metal binding4671Calcium By similarity
Metal binding4691Calcium By similarity
Metal binding5171Calcium By similarity
Metal binding5221Calcium By similarity

Amino acid modifications

Lipidation41S-palmitoyl cysteine Potential
Lipidation51S-palmitoyl cysteine Potential

Sequences

Sequence LengthMass (Da)Tools
P52183 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: FA5A3CE6A7C4E394

FASTA77285,942
        10         20         30         40         50         60 
MGNCCSTFRA VFKPNEGSGG GIPLMPVRGG STRRPDSLPK PPAAVVPSPP SPGDVPDAGV 

        70         80         90        100        110        120 
APEVASVKEV DVLLAENGDA HRTRHYELMD REKEPRLVVR RGQPFAVSVT LSRPYNPDID 

       130        140        150        160        170        180 
AISFVFTVED AEKPSYGQGT LVAVPLLAKG AESGAAWNAV LDSSADDILR IQITPAADAI 

       190        200        210        220        230        240 
VGKWKMDIDT KLKNDGAVSY SYKDPFYILY NPWCRQDQVF LEGEELLQEY VLNDTGLIWR 

       250        260        270        280        290        300 
GSYNRLRPCV WKYAQFEKEI LDCALYLVSK IGGVRPSECG DPVRVCRAIS AAVNSPDDNG 

       310        320        330        340        350        360 
AVMGNWSNDY GGGTPPTKWI GSMKILQQFY KNKKPVKYGQ CWVFAGVLTT VCRALGLPAR 

       370        380        390        400        410        420 
TVTTYSAAHD TQNSLTVDYF VDDKGEIMEE MNSDSIWNFH VWTEVWMERP DLMPGDGAHY 

       430        440        450        460        470        480 
GGWQAVDSTP QELSDNMYRC GPAPVVAVKQ GEVLRPYDSA YVFAEVNADK VFWRYSGPTQ 

       490        500        510        520        530        540 
PLKLIRKDML GIGQNISTKA VGRFQREDIT NTYKYPEKSV EERAAMLKAL RQSESLFSRY 

       550        560        570        580        590        600 
YLNEDFNDIH FNFELRDDIV IGSPFSVVVV MKNRSNQQDY TVTVLLRVDT VLYTGHVKDG 

       610        620        630        640        650        660 
VKKEKVERLI KAGAVEEVRI DVSYEDYYKH LVDQCAFNIA CLATVHDTNY EYFAQDDFRV 

       670        680        690        700        710        720 
RKPDIKIKLE GEPVQGQEMS AVATLKNPLP IPVKKGQFLI EGPGIAKTQK IKLSQNIAPG 

       730        740        750        760        770 
EEASVNFKFT PKYDGRATIA AKFSSKELDD VDGFLNFMVE PKKEVNGTGN AA 

« Hide

References

[1]"Annulin, a protein expressed at limb segment boundaries in the grasshopper embryo, is homologous to protein cross-linking transglutaminases."
Singer M.A., Hortsch M., Goodman C.S., Bentley D.
Dev. Biol. 154:143-159(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M92291 mRNA. Translation: AAA29806.1.
PIRA48822.

3D structure databases

ProteinModelPortalP52183.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameANNU_SCHAM
AccessionPrimary (citable) accession number: P52183
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families