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P52183

- ANNU_SCHAM

UniProt

P52183 - ANNU_SCHAM

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Protein

Annulin

Gene
N/A
Organism
Schistocerca americana (American grasshopper)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Binds 1 calcium ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei400 – 4001 By similarity
Active sitei427 – 4271 By similarity
Metal bindingi467 – 4671Calcium By similarity
Metal bindingi469 – 4691Calcium By similarity
Metal bindingi517 – 5171Calcium By similarity
Metal bindingi522 – 5221Calcium By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. peptide cross-linking Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Annulin
Alternative name(s):
Protein-glutamine gamma-glutamyltransferase (EC:2.3.2.13)
Transglutaminase
OrganismiSchistocerca americana (American grasshopper)
Taxonomic identifieri7009 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraOrthopteroideaOrthopteraCaeliferaAcridomorphaAcridoideaAcrididaeCyrtacanthacridinaeSchistocerca

Subcellular locationi

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

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 772772AnnulinPRO_0000213718Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi4 – 41S-palmitoyl cysteine Reviewed prediction
Lipidationi5 – 51S-palmitoyl cysteine Reviewed prediction

Keywords - PTMi

Lipoprotein, Palmitate

Expressioni

Tissue specificityi

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 stagei

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.

Structurei

3D structure databases

ProteinModelPortaliP52183.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProiIPR023608. 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]
PANTHERiPTHR11590. PTHR11590. 1 hit.
PfamiPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
SMARTiSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52183-1 [UniParc]FASTAAdd to Basket

« Hide

MGNCCSTFRA VFKPNEGSGG GIPLMPVRGG STRRPDSLPK PPAAVVPSPP    50
SPGDVPDAGV APEVASVKEV DVLLAENGDA HRTRHYELMD REKEPRLVVR 100
RGQPFAVSVT LSRPYNPDID AISFVFTVED AEKPSYGQGT LVAVPLLAKG 150
AESGAAWNAV LDSSADDILR IQITPAADAI VGKWKMDIDT KLKNDGAVSY 200
SYKDPFYILY NPWCRQDQVF LEGEELLQEY VLNDTGLIWR GSYNRLRPCV 250
WKYAQFEKEI LDCALYLVSK IGGVRPSECG DPVRVCRAIS AAVNSPDDNG 300
AVMGNWSNDY GGGTPPTKWI GSMKILQQFY KNKKPVKYGQ CWVFAGVLTT 350
VCRALGLPAR TVTTYSAAHD TQNSLTVDYF VDDKGEIMEE MNSDSIWNFH 400
VWTEVWMERP DLMPGDGAHY GGWQAVDSTP QELSDNMYRC GPAPVVAVKQ 450
GEVLRPYDSA YVFAEVNADK VFWRYSGPTQ PLKLIRKDML GIGQNISTKA 500
VGRFQREDIT NTYKYPEKSV EERAAMLKAL RQSESLFSRY YLNEDFNDIH 550
FNFELRDDIV IGSPFSVVVV MKNRSNQQDY TVTVLLRVDT VLYTGHVKDG 600
VKKEKVERLI KAGAVEEVRI DVSYEDYYKH LVDQCAFNIA CLATVHDTNY 650
EYFAQDDFRV RKPDIKIKLE GEPVQGQEMS AVATLKNPLP IPVKKGQFLI 700
EGPGIAKTQK IKLSQNIAPG EEASVNFKFT PKYDGRATIA AKFSSKELDD 750
VDGFLNFMVE PKKEVNGTGN AA 772
Length:772
Mass (Da):85,942
Last modified:October 1, 1996 - v1
Checksum:iFA5A3CE6A7C4E394
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M92291 mRNA. Translation: AAA29806.1.
PIRiA48822.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M92291 mRNA. Translation: AAA29806.1 .
PIRi A48822.

3D structure databases

ProteinModelPortali P52183.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProi IPR023608. 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 ]
PANTHERi PTHR11590. PTHR11590. 1 hit.
Pfami PF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000459. TGM_EBP42. 1 hit.
SMARTi SM00460. TGc. 1 hit.
[Graphical view ]
SUPFAMi SSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEi PS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiANNU_SCHAM
AccessioniPrimary (citable) accession number: P52183
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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