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.

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

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acyltransferase; Calcium; Cell membrane; Lipoprotein; Membrane; Metal-binding; Palmitate; Transferase.

Features

Feature table viewer

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