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Q8BH61 (F13A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coagulation factor XIII A chain

Short name=Coagulation factor XIIIa
EC=2.3.2.13
Alternative name(s):
Protein-glutamine gamma-glutamyltransferase A chain
Transglutaminase A chain
Gene names
Name:F13a1
Synonyms:F13a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length732 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (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 N(5)-alkylglutamine + NH3.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

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.

Post-translational modification

The activation peptide is released by thrombin By similarity.

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Propeptide2 – 3837Activation peptide By similarity
PRO_0000033648
Chain39 – 732694Coagulation factor XIII A chain
PRO_0000033649

Sites

Active site3151 By similarity
Active site3741 By similarity
Active site3971 By similarity
Metal binding4371Calcium By similarity
Metal binding4391Calcium By similarity
Metal binding4861Calcium By similarity
Metal binding4911Calcium By similarity
Site38 – 392Cleavage; by thrombin; to produce active factor XIII-A By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Glycosylation6141N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict51P → Q in BAC29414. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BH61 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 47B338665D40C4D9

FASTA73283,207
        10         20         30         40         50         60 
MSDTPASTFG GRRAVPPNNS NAAEVDLPTE ELQGLVPRGV NLKDYLNVTA VHLFKERWDS 

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

       130        140        150        160        170        180 
PVVKELQSGK WGAKVIMNED RSVRLSVQSS PECIVGKFRM YVAVWTPYGI LRTRRDPETD 

       190        200        210        220        230        240 
TYILFNPWCE EDAVYLDDEK EREEYVLNDI GVIFYGDFKD IKSRSWSYGQ FEDGILDTCL 

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

       310        320        330        340        350        360 
LEYRSSETPV RYGQCWVFAG VFNTFLRCLG IPARVITNYF SAHDNDANLQ MDIFLEEDGN 

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

       430        440        450        460        470        480 
GHVCFQFDAP FVFAEVNSDL VYITAKQDGT HVVEAVDATH IGKLIVTKQI GGDGMQDITD 

       490        500        510        520        530        540 
TYKFQEGQEE ERLALETALM YGAKKTLNTE GVVKSRSDVT MNFDVENAVL GKDFKVTITF 

       550        560        570        580        590        600 
QNNSSNLYTI LAYLSGNITF YTGVSKKEFK KESFEETLDP FSSKKKEVLV RAGEYMSHLL 

       610        620        630        640        650        660 
EQGFLHFFVT ARINESRDVL AKQKSIILTI PKITIKVRGA AMVGSDMVVT VEFTNPLKET 

       670        680        690        700        710        720 
LQNVWIHLDG PGVMRPKRKV FREIRPNTTV QWEEVCRPWV SGHRKLIASM TSDSLRHVYG 

       730 
ELDLQIQRRP TM 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone, Cerebellum and Spleen.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK036403 mRNA. Translation: BAC29414.1.
AK049092 mRNA. Translation: BAC33539.1.
AK165311 mRNA. Translation: BAE38130.1.
BC040274 mRNA. Translation: AAH40274.1.
CCDSCCDS26456.1.
RefSeqNP_001159863.1. NM_001166391.1.
NP_083060.2. NM_028784.3.
UniGeneMm.235105.

3D structure databases

ProteinModelPortalQ8BH61.
SMRQ8BH61. Positions 7-729.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8BH61.

Proteomic databases

MaxQBQ8BH61.
PaxDbQ8BH61.
PRIDEQ8BH61.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037491; ENSMUSP00000048667; ENSMUSG00000039109.
ENSMUST00000164727; ENSMUSP00000128316; ENSMUSG00000039109.
GeneID74145.
KEGGmmu:74145.
UCSCuc007qcn.2. mouse.

Organism-specific databases

CTD2162.
MGIMGI:1921395. F13a1.

Phylogenomic databases

eggNOGNOG80379.
GeneTreeENSGT00740000115156.
HOGENOMHOG000231695.
HOVERGENHBG004342.
InParanoidQ8BH61.
KOK03917.
OMACEEDAVY.
OrthoDBEOG7WT40M.
PhylomeDBQ8BH61.
TreeFamTF324278.

Gene expression databases

ArrayExpressQ8BH61.
BgeeQ8BH61.
CleanExMM_F13A1.
GenevestigatorQ8BH61.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProIPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
PANTHERPTHR11590. PTHR11590. 1 hit.
PfamPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFPIRSF000459. TGM_EBP42. 1 hit.
SMARTSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSF13A1. mouse.
NextBio339898.
PROQ8BH61.
SOURCESearch...

Entry information

Entry nameF13A_MOUSE
AccessionPrimary (citable) accession number: Q8BH61
Secondary accession number(s): Q3TNF9, Q8BIP2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot