ID   Q9DER6_CHICK            Unreviewed;       736 AA.
AC   Q9DER6;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   08-NOV-2023, entry version 112.
DE   SubName: Full=Coagulation factor XIIIA {ECO:0000313|EMBL:CAC10657.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|EMBL:CAC10657.1};
RN   [1] {ECO:0000313|EMBL:CAC10657.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=White Leghorn {ECO:0000313|EMBL:CAC10657.1};
RX   PubMed=10948196; DOI=10.1074/jbc.M005025200;
RA   Recheis B., Osanger A., Haubenwallner S., Schneider W.J., Nimpf J.;
RT   "Chicken coagulation factor XIIIA is produced by the theca externa and
RT   stabilizes the ovarian follicular wall.";
RL   J. Biol. Chem. 275:35320-35327(2000).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000459-2};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000459-2};
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000256|ARBA:ARBA00005968}.
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DR   EMBL; AJ278103; CAC10657.1; -; mRNA.
DR   RefSeq; NP_990016.1; NM_204685.1.
DR   AlphaFoldDB; Q9DER6; -.
DR   GeneID; 395420; -.
DR   KEGG; gga:395420; -.
DR   CTD; 2162; -.
DR   VEuPathDB; HostDB:geneid_395420; -.
DR   PhylomeDB; Q9DER6; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.90.260.10; Transglutaminase-like; 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   PANTHER; PTHR11590:SF42; COAGULATION FACTOR XIII A CHAIN; 1.
DR   PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
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; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2}.
FT   DOMAIN          314..407
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        322
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         444
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         446
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         493
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         498
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   736 AA;  83749 MW;  100F69C0268C0331 CRC64;
     MSEPTSTDRE KKRPPLNGRR ALPSNNSNAE ENDVPEMDAF GLIPRGFNPK DYLRVVDIHM
     FKEPNEINKQ QHHTDKYYNP KLIVRRGQPF QIQIDFSRPY DPEKDQIWLE YLIGRYPQPN
     KGTYIPILIG DVLKPGEWGA KITHRENNSI RLSIMSSATC IIGKFRLYIA IWTPYGIIRT
     HRNSATDTYI LFNPWCQLDA VYLDDEKERE EYVLNDVGIV FHGDVNEVKL RSWSYGQFEE
     NILDACLFLM DKAELELSGR GNPIKICRVA SAMINSKDDN GVLAGSWDNL YDYGVPPSAW
     TGSVDILLEY YSSKQPVRYG QCWVFAGVFN TFLRCLGIPA RLITNYSSAH DNNANLQLDF
     FLDDEGQVDN RLTKDSVWNY HCWNEAWMTR PDLPVGFGGW QAVDGTPQET SDGMYRCGPA
     SVQAIKHGHV CFQFDAPFVY AEVNSDIIYS RMGKNGSQVI EKIDTTHIGK LIVTKGVGND
     DMVDITENYK FQEGSAEERL ALETAVMYGV KKQTTQPTTY QPQKDIEMDL QVQKVVLGSD
     FKVTIILRNK SRNSYTATTY LSGNIVFYTG VTKSEFKKHS FSAKLEPLLS NTFDVMITSA
     EYLNDLLDQA SFHFFVTARI NETGKVLAMQ KAVVLEIPTL KIKTKGQMVV DRETSVVVEF
     TNPLKQTLEN ATLRLEGPGV LRTMKKEFRQ IPAMSTLIWD VKCIPKRPGL RKLIASLNCD
     ALRHVYGELN IQVQKP
//