ID   F13A_BOVIN              Reviewed;         198 AA.
AC   P12260; Q1JPK3;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 2.
DT   08-NOV-2023, entry version 136.
DE   RecName: Full=Coagulation factor XIII A chain;
DE            Short=Coagulation factor XIIIa;
DE            EC=2.3.2.13 {ECO:0000250|UniProtKB:P00488};
DE   AltName: Full=Protein-glutamine gamma-glutamyltransferase A chain;
DE   AltName: Full=Transglutaminase A chain;
DE   Flags: Precursor; Fragment;
GN   Name=F13A1; Synonyms=F13A;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-38.
RX   PubMed=4831071; DOI=10.1016/0006-291x(74)90919-x;
RA   Nakamura S., Iwanaga S., Suzuki T., Mikuni Y., Konishi K.;
RT   "Amino acid sequence of the peptide released from bovine factor XIII
RT   following activation by thrombin.";
RL   Biochem. Biophys. Res. Commun. 58:250-256(1974).
CC   -!- FUNCTION: Factor XIII is activated by thrombin and calcium ion to a
CC       transglutaminase that catalyzes the formation of gamma-glutamyl-
CC       epsilon-lysine cross-links between fibrin chains, thus stabilizing the
CC       fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin,
CC       to the alpha chains of fibrin. {ECO:0000250|UniProtKB:P00488}.
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;
CC         Evidence={ECO:0000250|UniProtKB:P00488};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P00488};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00488};
CC   -!- SUBUNIT: Tetramer of two A chains (F13A1) and two B (F13B) chains.
CC       {ECO:0000250|UniProtKB:P00488}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00488}.
CC       Secreted {ECO:0000250|UniProtKB:P00488}. Note=Secreted into the blood
CC       plasma. Cytoplasmic in most tissues, but also secreted in the blood
CC       plasma. {ECO:0000250|UniProtKB:P00488}.
CC   -!- PTM: The activation peptide is released by thrombin.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
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DR   EMBL; BT025350; ABF57306.1; -; mRNA.
DR   PIR; A10933; A10933.
DR   AlphaFoldDB; P12260; -.
DR   SMR; P12260; -.
DR   STRING; 9913.ENSBTAP00000009559; -.
DR   PaxDb; 9913-ENSBTAP00000009559; -.
DR   eggNOG; ENOG502QQ46; Eukaryota.
DR   HOGENOM; CLU_013435_0_2_1; -.
DR   InParanoid; P12260; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0072378; P:blood coagulation, fibrin clot formation; ISS:UniProtKB.
DR   GO; GO:0018149; P:peptide cross-linking; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
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; PF00868; Transglut_N; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Blood coagulation; Calcium; Cytoplasm;
KW   Direct protein sequencing; Hemostasis; Reference proteome; Secreted;
KW   Transferase; Zymogen.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00488,
FT                   ECO:0000269|PubMed:4831071"
FT   PROPEP          2..38
FT                   /note="Activation peptide"
FT                   /id="PRO_0000033645"
FT   CHAIN           39..>198
FT                   /note="Coagulation factor XIII A chain"
FT                   /id="PRO_0000351119"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            38..39
FT                   /note="Cleavage; by thrombin; to produce active factor
FT                   XIII-A"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00488"
FT   CONFLICT        25
FT                   /note="N -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         198
SQ   SEQUENCE   198 AA;  22745 MW;  A47F7B33469B89A2 CRC64;
     MSESSGTAFG GRRAIPPNTS NAAENDPPTV ELQGLVPRGF NPQDYLNVTN VHLFKERWDS
     NKVDHHTDKY SNDKLIVRRG QSFYIQIDFN RPYDPTRDLF RVEYVIGLYP QENKGTYIPV
     PLVSELQSGK WGAKVVMRED RSVRLSVQSS ADCIVGKFRM YVAVWTPYGV IRTSRNPETD
     TYILFNPWCE EDAVYLEN
//