P52183 (ANNU_SCHAM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Annulin Alternative name(s): Protein-glutamine gamma-glutamyltransferase EC=2.3.2.13 Transglutaminase
Organism	Schistocerca americana (American grasshopper)
Taxonomic identifier	7009 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Orthopteroidea › Orthoptera › Caelifera › Acridomorpha › Acridoidea › Acrididae › Cyrtacanthacridinae › Schistocerca

Protein attributes

Sequence length	772 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cell membrane Membrane
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
PTM	Lipoprotein Palmitate
Gene Ontology (GO)
Biological_process	peptide cross-linking Inferred from electronic annotation. Source: InterPro
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein-glutamine gamma-glutamyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 772	772	Annulin		PRO_0000213718
Sites
	Active site	400	1	By similarity
	Active site	427	1	By similarity
	Metal binding	467	1	Calcium By similarity
	Metal binding	469	1	Calcium By similarity
	Metal binding	517	1	Calcium By similarity
	Metal binding	522	1	Calcium By similarity
Amino acid modifications
	Lipidation	4	1	S-palmitoyl cysteine Potential
	Lipidation	5	1	S-palmitoyl cysteine Potential

Sequences

	Sequence		Length	Mass (Da)
	P52183 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: FA5A3CE6A7C4E394	FASTA	772	85,942
	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

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.
PIR	A48822.
3D structure databases
ProteinModelPortal	P52183.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	2.60.40.10. 3 hits.
InterPro	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]
PANTHER	PTHR11590. PTHR11590. 1 hit.
Pfam	PF00927. Transglut_C. 2 hits. PF01841. Transglut_core. 1 hit. PF00868. Transglut_N. 1 hit. [Graphical view]
PIRSF	PIRSF000459. TGM_EBP42. 1 hit.
SMART	SM00460. TGc. 1 hit. [Graphical view]
SUPFAM	SSF81296. Ig_E-set. 1 hit. SSF49309. Transglut_C. 2 hits.
PROSITE	PS00547. TRANSGLUTAMINASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ANNU_SCHAM

Accession

Primary (citable) accession number: P52183

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)