ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P52183


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ANNU_SCHAM
Primary accession number P52183
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 70)
Name and origin of the protein
Protein name Annulin
Synonyms Protein-glutamine gamma-glutamyltransferase
EC 2.3.2.13
Transglutaminase
Gene name None
From
Schistocerca americana (American grasshopper) [TaxID: 7009] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Orthopteroidea; Orthoptera; Caelifera; Acridomorpha; Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0012-1606(92)90055-L; PubMed=1358727 [NCBI, ExPASy, EBI, Israel, Japan]
Singer M.A., Hortsch M., Goodman C.S., Bentley D.;
"Annulin, a protein expressed at limb segment boundaries in the grasshopper embryo, is homologous to protein cross-linking transglutaminases.";
Dev. Biol. 154:143-159(1992).
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 N5-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.
  • SIMILARITY: Belongs to the transglutaminase superfamily. Transglutaminase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M92291; AAA29806.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A48822; A48822.
3D structure databases
HSSP P00488; 1EVU. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P52183.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0008415; Molecular function: acyltransferase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003810; Molecular function: protein-glutamine gamma-glutamyltransferase activity (inferred from electronic annotation from InterPro).
GO:0018149; Biological process: peptide cross-linking (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR008957; Fibronectin_typ-III-like_fold.
IPR013783; Ig-like_fold.
IPR008958; Transglutaminase_C.
IPR013808; Transglutaminase_CS.
IPR001102; Transglutaminase_N.
IPR002931; Trnsglumase_like.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.30; FN_III-like; 2.
G3DSA:2.60.40.10; Ig-like_fold; 1.
Pfam PF00927; Transglut_C; 2.
PF01841; Transglut_core; 1.
PF00868; Transglut_N; 1.
Pfam graphical view of domain structure.
SMART SM00460; TGc; 1.
SMART graphical view of domain structure.
PROSITE PS00547; TRANSGLUTAMINASES; 1.
Other
ProtoNet P52183.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acyltransferase; Calcium; Cell membrane; Lipoprotein; Membrane; Metal-binding; Palmitate; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   772  772     Annulin. PRO_0000213718
ACT_SITE   400   400        By similarity. 
ACT_SITE   427   427        By similarity. 
METAL   467   467        Calcium (By similarity). 
METAL   469   469        Calcium (By similarity). 
METAL   517   517        Calcium (By similarity). 
METAL   522   522        Calcium (By similarity). 
LIPID   4     4        S-palmitoyl cysteine (Potential). 
LIPID   5     5        S-palmitoyl cysteine (Potential). 
Sequence information
Length: 772 AA [This is the length of the unprocessed precursor] Molecular weight: 85942 Da [This is the MW of the unprocessed precursor] CRC64: FA5A3CE6A7C4E394 [This is a checksum on the sequence]
        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 

P52183 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!