GenomeNet

Database: UniProt/SWISS-PROT
Entry: F13A_RAT
LinkDB: F13A_RAT
Original site: 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   20-JUN-2018, entry version 124.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
CC       a transglutaminase that catalyzes the formation of gamma-glutamyl-
CC       epsilon-lysine cross-links between fibrin chains, thus stabilizing
CC       the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or
CC       fibronectin, to the alpha chains of fibrin.
CC       {ECO:0000250|UniProtKB:P00488}.
CC   -!- CATALYTIC ACTIVITY: A protein-L-glutamine + a protein-L-lysine = a
CC       protein with an N(6)-(gamma-glutamyl)-L-lysine cross-link + NH(3).
CC       {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.
CC       {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
CC       blood plasma. Cytoplasmic in most tissues, but also secreted in
CC       the blood plasma. {ECO:0000250|UniProtKB:P00488}.
CC   -!- PTM: The activation peptide is released by thrombin.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
DR   EMBL; Y12502; CAA73104.1; -; mRNA.
DR   RefSeq; NP_067730.2; NM_021698.2.
DR   UniGene; Rn.42925; -.
DR   ProteinModelPortal; O08619; -.
DR   SMR; O08619; -.
DR   STRING; 10116.ENSRNOP00000021568; -.
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; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   HOGENOM; HOG000231695; -.
DR   HOVERGEN; HBG004342; -.
DR   InParanoid; O08619; -.
DR   KO; K03917; -.
DR   PhylomeDB; O08619; -.
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;
KW   Complete proteome; Cytoplasm; Glycoprotein; Hemostasis; Metal-binding;
KW   Reference proteome; Secreted; Transferase; Zymogen.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P00488}.
FT   PROPEP        2     38       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_0000033650.
FT   CHAIN        39    732       Coagulation factor XIII A chain.
FT                                /FTId=PRO_0000033651.
FT   ACT_SITE    315    315       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    374    374       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    397    397       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   METAL       437    437       Calcium. {ECO:0000250|UniProtKB:P00488}.
FT   METAL       439    439       Calcium. {ECO:0000250|UniProtKB:P00488}.
FT   METAL       486    486       Calcium. {ECO:0000250|UniProtKB:P00488}.
FT   METAL       491    491       Calcium. {ECO:0000250|UniProtKB:P00488}.
FT   SITE         38     39       Cleavage; by thrombin; to produce active
FT                                factor XIII-A. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000250|UniProtKB:P00488}.
FT   CARBOHYD    614    614       N-linked (GlcNAc...) asparagine.
FT                                {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
//
DBGET integrated database retrieval system