F13A_RAT
ID F13A_RAT Reviewed; 732 AA.
AC O08619;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 134.
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;
GN Name=F13a1; Synonyms=F13a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Diepholz D., Grundmann U., Zettlmeissl G.;
RT "cDNA cloning for rat factor XIIIa.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000305}.
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DR EMBL; Y12502; CAA73104.1; -; mRNA.
DR RefSeq; NP_067730.2; NM_021698.2.
DR AlphaFoldDB; O08619; -.
DR SMR; O08619; -.
DR STRING; 10116.ENSRNOP00000021568; -.
DR GlyGen; O08619; 1 site.
DR iPTMnet; O08619; -.
DR PhosphoSitePlus; O08619; -.
DR PaxDb; O08619; -.
DR PRIDE; O08619; -.
DR GeneID; 60327; -.
DR KEGG; rno:60327; -.
DR UCSC; RGD:621495; rat.
DR CTD; 2162; -.
DR RGD; 621495; F13a1.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR InParanoid; O08619; -.
DR OrthoDB; 297055at2759; -.
DR PhylomeDB; O08619; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-140875; Common Pathway of Fibrin Clot Formation.
DR PRO; PR:O08619; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; ISS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IDA:RGD.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; ISS:UniProtKB.
DR GO; GO:0018149; P:peptide cross-linking; ISS:UniProtKB.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.90.260.10; -; 1.
DR InterPro; IPR034810; Factor_XIII_A.
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; PTHR11590:SF42; 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; 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 Acetylation; Acyltransferase; Blood coagulation; Calcium; Cytoplasm;
KW Glycoprotein; Hemostasis; Metal-binding; Reference proteome; Secreted;
KW Transferase; Zymogen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT PROPEP 2..38
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000033650"
FT CHAIN 39..732
FT /note="Coagulation factor XIII A chain"
FT /id="PRO_0000033651"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT ACT_SITE 397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10024"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT BINDING 439
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT BINDING 486
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT BINDING 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT SITE 38..39
FT /note="Cleavage; by thrombin; to produce active factor
FT XIII-A"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P00488"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 732 AA; 82659 MW; 22B052D3A73721ED CRC64;
MSDTPATTFG GRGAIPPNNS NAAGVDLPTE DLQGLVPRGV SLKDYLNVTA VHLFKERWDS
NKIVHHTDKF DNNKLIVRRG QTFYIQIDFN RPYDPRKDLF RVEYVIGRYP QENKGTYIPV
PVVTELQSGK WGAKVIMNED RSVRLSVQSS PECIVGKFRM YVAVWTPYGI LRTQRDPETD
TYILFNPWCE EDAVYLDDEK EREEYVLNDI GGIFHGDFND IKSRSWSYGQ FEDGILDACL
FVMDKAEMDL SGRGNPIKVS RVGSAMVNAK DDEGVLVGSW DNVYAYGIPP SAWTGSVDIL
LEYRSSETPV RYGQCWVLAG VFNTFLRCLG IPARVITNYS SAHDNDANLQ MDIFLEEDGS
VSFKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQAVDSTP QENSDGMYRC GPASVQAVKH
GHVCFQFDAP FVLGEVNSDL VYITAKKDGT HVVENVDATH IGKLIVTKEI GGDGMQDITD
TYKFQEGQEE ERLALETALM YGAKKTLNTE GMVKSSSDVD MNFDVENAVL GKDFRVTITF
QNNSSNLYTI LAYLSGNITF YTGVSKKEFK TESFEVTLDP LSLEKKEVLI RAGEYMSYLL
EQGLLHFFVT ARINETRVVL AKQKAIVLTI PKVTIKVRGT AMVGSDMVVT VEFTNPLKET
LKNVWLHLEG PGVMRPKRKM FREIRPNATV QWEEVCQPWV SGHRKLNASM TSDSLRHVYG
ELDLQIRRRP TV
