ANNU_SCHAM
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 03-AUG-2022, entry version 112.
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; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
OX NCBI_TaxID=7009;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX 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 grasshopper
RT embryo, is homologous to protein cross-linking transglutaminases.";
RL Dev. Biol. 154:143-159(1992).
CC -!- FUNCTION: Participates in morphogenetic activities of the cells, maybe
CC by stabilizing the membrane or subcortical structures of cells that are
CC under mechanical stress. Probably catalyzes the cross-linking of
CC proteins and the conjugation of polyamines to proteins.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-
CC lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011,
CC ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10024};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side.
CC Note=Intracellular and peripherally associated with the inner leaflet
CC of the cell membrane, using a fatty acid linkage.
CC -!- TISSUE SPECIFICITY: Has an annular, or ring-like expression pattern in
CC epithelial annuli of developing limb segment boundary cells. In
CC embryos, it is seen in gastrulating cells, in cells surrounding rapidly
CC dividing neuroblasts, and in muscle pioneer cells invaginating to form
CC apodemes.
CC -!- DEVELOPMENTAL STAGE: Expression of this protein in embryos and limbs is
CC associated with areas undergoing movements, morphogenetic
CC rearrangements, or rapid cell division. Expression of annulin precedes
CC the first morphological signs of segmentation in the developing limbs.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000305}.
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DR EMBL; M92291; AAA29806.1; -; mRNA.
DR PIR; A48822; A48822.
DR AlphaFoldDB; P52183; -.
DR SMR; P52183; -.
DR PRIDE; P52183; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.90.260.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR InterPro; IPR023608; Transglutaminase_animal.
DR InterPro; IPR013808; Transglutaminase_AS.
DR InterPro; IPR008958; Transglutaminase_C.
DR InterPro; IPR036238; Transglutaminase_C_sf.
DR InterPro; IPR001102; Transglutaminase_N.
DR Pfam; PF00927; Transglut_C; 2.
DR Pfam; PF01841; Transglut_core; 1.
DR Pfam; PF00868; Transglut_N; 1.
DR PIRSF; PIRSF000459; TGM_EBP42; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF49309; SSF49309; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF81296; SSF81296; 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
FT /note="Annulin"
FT /id="PRO_0000213718"
FT REGION 15..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
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
