ID   ANNU_SCHAM              Reviewed;         772 AA.
AC   P52183;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 72.
DE   RecName: Full=Annulin;
DE   AltName: Full=Protein-glutamine gamma-glutamyltransferase;
DE            EC=2.3.2.13;
DE   AltName: Full=Transglutaminase;
OS   Schistocerca americana (American grasshopper).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Orthopteroidea; Orthoptera; Caelifera; Acridomorpha;
OC   Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
OX   NCBI_TaxID=7009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93050772; PubMed=1358727; DOI=10.1016/0012-1606(92)90055-L;
RA   Singer M.A., Hortsch M., Goodman C.S., Bentley D.;
RT   "Annulin, a protein expressed at limb segment boundaries in the
RT   grasshopper embryo, is homologous to protein cross-linking
RT   transglutaminases.";
RL   Dev. Biol. 154:143-159(1992).
CC   -!- FUNCTION: Participates in morphogenetic activities of the cells,
CC       maybe by stabilizing the membrane or subcortical structures of
CC       cells that are under mechanical stress. Probably catalyzes the
CC       cross-linking of proteins and the conjugation of polyamines to
CC       proteins.
CC   -!- CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N(5)-
CC       alkylglutamine + NH(3).
CC   -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side. Note=Intracellular and peripherally associated with the
CC       inner leaflet of the cell membrane, using a fatty acid linkage.
CC   -!- TISSUE SPECIFICITY: Has an annular, or ring-like expression
CC       pattern in epithelial annuli of developing limb segment boundary
CC       cells. In embryos, it is seen in gastrulating cells, in cells
CC       surrounding rapidly dividing neuroblasts, and in muscle pioneer
CC       cells invaginating to form apodemes.
CC   -!- DEVELOPMENTAL STAGE: Expression of this protein in embryos and
CC       limbs is associated with areas undergoing movements, morphogenetic
CC       rearrangements, or rapid cell division. Expression of annulin
CC       precedes the first morphological signs of segmentation in the
CC       developing limbs.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family.
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DR   EMBL; M92291; AAA29806.1; -; mRNA.
DR   PIR; A48822; A48822.
DR   HSSP; P00488; 1EVU.
DR   BRENDA; 2.3.2.13; 301871.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase...; IEA:EC.
DR   GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
DR   InterPro; IPR008957; Fibronectin_typ-III-like_fold.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   InterPro; IPR013808; Transglutaminase_CS.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   Gene3D; G3DSA:2.60.40.30; FN_III-like; 2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00927; Transglut_C; 2.
DR   Pfam; PF01841; Transglut_core; 1.
DR   Pfam; PF00868; Transglut_N; 1.
DR   SMART; SM00460; TGc; 1.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Calcium; Cell membrane; Lipoprotein; Membrane;
KW   Metal-binding; Palmitate; Transferase.
FT   CHAIN         1    772       Annulin.
FT                                /FTId=PRO_0000213718.
FT   ACT_SITE    400    400       By similarity.
FT   ACT_SITE    427    427       By similarity.
FT   METAL       467    467       Calcium (By similarity).
FT   METAL       469    469       Calcium (By similarity).
FT   METAL       517    517       Calcium (By similarity).
FT   METAL       522    522       Calcium (By similarity).
FT   LIPID         4      4       S-palmitoyl cysteine (Potential).
FT   LIPID         5      5       S-palmitoyl cysteine (Potential).
SQ   SEQUENCE   772 AA;  85942 MW;  FA5A3CE6A7C4E394 CRC64;
     MGNCCSTFRA VFKPNEGSGG GIPLMPVRGG STRRPDSLPK PPAAVVPSPP SPGDVPDAGV
     APEVASVKEV DVLLAENGDA HRTRHYELMD REKEPRLVVR RGQPFAVSVT LSRPYNPDID
     AISFVFTVED AEKPSYGQGT LVAVPLLAKG AESGAAWNAV LDSSADDILR IQITPAADAI
     VGKWKMDIDT KLKNDGAVSY SYKDPFYILY NPWCRQDQVF LEGEELLQEY VLNDTGLIWR
     GSYNRLRPCV WKYAQFEKEI LDCALYLVSK IGGVRPSECG DPVRVCRAIS AAVNSPDDNG
     AVMGNWSNDY GGGTPPTKWI GSMKILQQFY KNKKPVKYGQ CWVFAGVLTT VCRALGLPAR
     TVTTYSAAHD TQNSLTVDYF VDDKGEIMEE MNSDSIWNFH VWTEVWMERP DLMPGDGAHY
     GGWQAVDSTP QELSDNMYRC GPAPVVAVKQ GEVLRPYDSA YVFAEVNADK VFWRYSGPTQ
     PLKLIRKDML GIGQNISTKA VGRFQREDIT NTYKYPEKSV EERAAMLKAL RQSESLFSRY
     YLNEDFNDIH FNFELRDDIV IGSPFSVVVV MKNRSNQQDY TVTVLLRVDT VLYTGHVKDG
     VKKEKVERLI KAGAVEEVRI DVSYEDYYKH LVDQCAFNIA CLATVHDTNY EYFAQDDFRV
     RKPDIKIKLE GEPVQGQEMS AVATLKNPLP IPVKKGQFLI EGPGIAKTQK IKLSQNIAPG
     EEASVNFKFT PKYDGRATIA AKFSSKELDD VDGFLNFMVE PKKEVNGTGN AA
//