[1]	NUCLEOTIDE SEQUENCE [MRNA]. Diepholz D., Grundmann U., Zettlmeissl G.; "cDNA cloning for rat factor XIIIa."; Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin (By similarity).
CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N⁵-alkylglutamine + NH₃.
COFACTOR: Binds 1 calcium ion per subunit (By similarity).
SUBUNIT: Tetramer of two A chains and two B chains (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Secreted (By similarity). Note=Cytoplasmic in most tissues, but also secreted in the blood plasma (By similarity).
PTM: The activation peptide is released by thrombin (By similarity).
SIMILARITY: Belongs to the transglutaminase superfamily. Transglutaminase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y12502; CAA73104.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_067730.2; -.

UniGene

Rn.42925

3D structure databases

HSSP

P00488; 1QRK. [HSSP ENTRY / PDB]

SMR

O08619; 8-727, 9-728.

ModBase

O08619.

Organism-specific databases

RGD

621495; F13a1.

Gene expression databases

ArrayExpress

O08619; -.

GermOnline

ENSRNOG00000015957; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0008415;	Molecular function: acyltransferase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003810;	Molecular function: protein-glutamine gamma-glutamyltransferase activity (inferred from electronic annotation from InterPro).
GO:0007596;	Biological process: blood coagulation (inferred from electronic annotation from UniProtKB-KW).
GO:0018149;	Biological process: peptide cross-linking (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR008957; Fibronectin_typ-III-like_fold.
IPR013783; Ig-like_fold.
IPR008958; Transglutaminase_C.
IPR013808; Transglutaminase_CS.
IPR001102; Transglutaminase_N.
IPR002931; Trnsglumase_like.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.30; FN_III-like; 1.
G3DSA:2.60.40.10; Ig-like_fold; 1.

Pfam

PF00927; Transglut_C; 2.
PF01841; Transglut_core; 1.
PF00868; Transglut_N; 1.
Pfam graphical view of domain structure.

SMART

SM00460; TGc; 1.
SMART graphical view of domain structure.

PROSITE

PS00547; TRANSGLUTAMINASES; 1.

Proteomics databases

PRIDE

O08619; -.

Genome annotation databases

Ensembl

ENSRNOG00000015957; Rattus norvegicus. [Contig view]

GeneID

60327; -.

KEGG

rno:60327; -.

Phylogenomic databases

HOVERGEN

O08619; -.

Other

611953; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Acyltransferase; Blood coagulation; Calcium; Cytoplasm; Glycoprotein; Metal-binding; Secreted; Transferase; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`PROPEP`	`2 38`	`37`	`Activation peptide (By similarity).`	`PRO_0000033650`
`CHAIN`	`39 732`	`694`	`Coagulation factor XIII A chain.`	`PRO_0000033651`
`ACT_SITE`	`315 315`		`By similarity.`
`ACT_SITE`	`374 374`		`By similarity.`
`ACT_SITE`	`397 397`		`By similarity.`
`METAL`	`437 437`		`Calcium (By similarity).`
`METAL`	`439 439`		`Calcium (By similarity).`
`METAL`	`486 486`		`Calcium (By similarity).`
`METAL`	`491 491`		`Calcium (By similarity).`
`SITE`	`38 39`	`2`	`Cleavage; by thrombin; to produce active factor XIII-A (By similarity).`
`MOD_RES`	`2 2`		`N-acetylserine (By similarity).`
`CARBOHYD`	`614 614`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 732 AA [This is the length of the unprocessed precursor]

Molecular weight: 82659 Da [This is the MW of the unprocessed precursor]

CRC64: 22B052D3A73721ED [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDTPATTFG GRGAIPPNNS NAAGVDLPTE DLQGLVPRGV SLKDYLNVTA VHLFKERWDS 

        70         80         90        100        110        120 
NKIVHHTDKF DNNKLIVRRG QTFYIQIDFN RPYDPRKDLF RVEYVIGRYP QENKGTYIPV 

       130        140        150        160        170        180 
PVVTELQSGK WGAKVIMNED RSVRLSVQSS PECIVGKFRM YVAVWTPYGI LRTQRDPETD 

       190        200        210        220        230        240 
TYILFNPWCE EDAVYLDDEK EREEYVLNDI GGIFHGDFND IKSRSWSYGQ FEDGILDACL 

       250        260        270        280        290        300 
FVMDKAEMDL SGRGNPIKVS RVGSAMVNAK DDEGVLVGSW DNVYAYGIPP SAWTGSVDIL 

       310        320        330        340        350        360 
LEYRSSETPV RYGQCWVLAG VFNTFLRCLG IPARVITNYS SAHDNDANLQ MDIFLEEDGS 

       370        380        390        400        410        420 
VSFKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQAVDSTP QENSDGMYRC GPASVQAVKH 

       430        440        450        460        470        480 
GHVCFQFDAP FVLGEVNSDL VYITAKKDGT HVVENVDATH IGKLIVTKEI GGDGMQDITD 

       490        500        510        520        530        540 
TYKFQEGQEE ERLALETALM YGAKKTLNTE GMVKSSSDVD MNFDVENAVL GKDFRVTITF 

       550        560        570        580        590        600 
QNNSSNLYTI LAYLSGNITF YTGVSKKEFK TESFEVTLDP LSLEKKEVLI RAGEYMSYLL 

       610        620        630        640        650        660 
EQGLLHFFVT ARINETRVVL AKQKAIVLTI PKVTIKVRGT AMVGSDMVVT VEFTNPLKET 

       670        680        690        700        710        720 
LKNVWLHLEG PGVMRPKRKM FREIRPNATV QWEEVCQPWV SGHRKLNASM TSDSLRHVYG 

       730 
ELDLQIRRRP TV

O08619 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools