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Reviewed, UniProtKB/Swiss-Prot P00488 (F13A_HUMAN)

Last modified January 19, 2010. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

Catalytic activity

Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Tetramer of two A chains and two B chains.

Subcellular location

Cytoplasm. Secreted. Note: Secreted into the blood plasma. Cytoplasmic in most tissues, but also secreted in the blood plasma.

Post-translational modification

The activation peptide is released by thrombin.

Polymorphism

There are four main allelic forms of this protein; F13A*1A, F13A*1B, F13A*2A and F13A*2B. In addition two other intermediate forms (F13A*2A and F13A*2B) seem to exist. The sequence shown is that of F13A*2B.

Involvement in disease

Defects in F13A1 are the cause of F13A deficiency [MIM:134570]. F13A deficiency is an autosomal recessive disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women. In addition to the common presentation such as subcutaneous and intramuscular haematomas, severe bleeding such as intracranial hemorrhages may occur. Ref.16

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.9
Propeptide2 – 3837Activation peptide
PRO_0000033646
Chain39 – 732694Coagulation factor XIII A chain
PRO_0000033647

Sites

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

Amino acid modifications

Modified residue21N-acetylserine
Glycosylation6141N-linked (GlcNAc...) Ref.10

Natural variations

Natural variant351V → L Higher specific activity. dbSNP rs5985. Ref.5 Ref.17 Ref.18
VAR_013927
Natural variant401V → I
VAR_020910
Natural variant2051Y → F: dbSNP rs3024477. Ref.5
VAR_020911
Natural variant3511M → K: dbSNP rs2230848.
VAR_057350
Natural variant5511T → I: dbSNP rs5984. Ref.18
VAR_013928
Natural variant5651P → L in allele F13A*1A, allele F13A*2A and allele F13*(2)A. dbSNP rs5982. Ref.5 Ref.18 Ref.3
VAR_007471
Natural variant5891L → Q: dbSNP rs5983. Ref.18
VAR_013929
Natural variant6501T → I: dbSNP rs17852475. Ref.7
VAR_060545
Natural variant6511V → I in allele F13A*2A and allele F13A*2B. dbSNP rs5987. Ref.5 Ref.18 Ref.1
VAR_007472
Natural variant6521Q → E in allele F13A*1A and allele F13A*1B. dbSNP rs5988. Ref.5 Ref.18 Ref.7 Ref.4 Ref.6
VAR_007473
Natural variant6821R → H in F13A deficiency. Ref.16
VAR_007474

Experimental info

Sequence conflict361Missing AA sequence Ref.9
Sequence conflict891F → L in AAA52488. Ref.1

Secondary structure

............................................................................................................................. 732
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00488-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 51A83A9B8B1370D4

FASTA73283,267
        10         20         30         40         50         60 
MSETSRTAFG GRRAVPPNNS NAAEDDLPTV ELQGVVPRGV NLQEFLNVTS VHLFKERWDT 

        70         80         90        100        110        120 
NKVDHHTDKY ENNKLIVRRG QSFYVQIDFS RPYDPRRDLF RVEYVIGRYP QENKGTYIPV 

       130        140        150        160        170        180 
PIVSELQSGK WGAKIVMRED RSVRLSIQSS PKCIVGKFRM YVAVWTPYGV LRTSRNPETD 

       190        200        210        220        230        240 
TYILFNPWCE DDAVYLDNEK EREEYVLNDI GVIFYGEVND IKTRSWSYGQ FEDGILDTCL 

       250        260        270        280        290        300 
YVMDRAQMDL SGRGNPIKVS RVGSAMVNAK DDEGVLVGSW DNIYAYGVPP SAWTGSVDIL 

       310        320        330        340        350        360 
LEYRSSENPV RYGQCWVFAG VFNTFLRCLG IPARIVTNYF SAHDNDANLQ MDIFLEEDGN 

       370        380        390        400        410        420 
VNSKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQAVDSTP QENSDGMYRC GPASVQAIKH 

       430        440        450        460        470        480 
GHVCFQFDAP FVFAEVNSDL IYITAKKDGT HVVENVDATH IGKLIVTKQI GGDGMMDITD 

       490        500        510        520        530        540 
TYKFQEGQEE ERLALETALM YGAKKPLNTE GVMKSRSNVD MDFEVENAVL GKDFKLSITF 

       550        560        570        580        590        600 
RNNSHNRYTI TAYLSANITF YTGVPKAEFK KETFDVTLEP LSFKKEAVLI QAGEYMGQLL 

       610        620        630        640        650        660 
EQASLHFFVT ARINETRDVL AKQKSTVLTI PEIIIKVRGT QVVGSDMTVT VQFTNPLKET 

       670        680        690        700        710        720 
LRNVWVHLDG PGVTRPMKKM FREIRPNSTV QWEEVCRPWV SGHRKLIASM SSDSLRHVYG 

       730 
ELDVQIQRRP SM 

« Hide

References

« Hide 'large scale' references
[1]"Amino acid sequence of the a subunit of human factor XIII."
Ichinose A., Hendrickson L.E., Fujikawa K., Davie E.W.
Biochemistry 25:6900-6906(1986) [PubMed: 3026437] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-651.
[2]"Characterization of cDNA coding for human factor XIIIa."
Grundmann U., Amann E., Zettlmeissl G., Kuepper H.A.
Proc. Natl. Acad. Sci. U.S.A. 83:8024-8028(1986) [PubMed: 2877457] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Characterization of the gene for the a subunit of human factor XIII (plasma transglutaminase), a blood coagulation factor."
Ichinose A., Davie E.W.
Proc. Natl. Acad. Sci. U.S.A. 85:5829-5833(1988) [PubMed: 2901091] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-565.
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-652.
Tissue: Brain.
[5]SeattleSNPs variation discovery resource
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-35; ILE-40; PHE-205; LEU-565; ILE-651 AND GLU-652.
[6]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-652.
[7]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ILE-650 AND GLU-652.
Tissue: Pancreas.
[8]"Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta."
Takahashi N., Takahashi Y., Putnam F.W.
Proc. Natl. Acad. Sci. U.S.A. 83:8019-8023(1986) [PubMed: 2877456] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-731.
[9]"Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin."
Takagi T., Doolittle R.F.
Biochemistry 13:750-756(1974) [PubMed: 4811064] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-44.
[10]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-614, MASS SPECTROMETRY.
Tissue: Plasma.
[11]"Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII."
Yee V.C., Pedersen L.C., Trong I.L., Bishop P.D., Stenkamp R.E., Teller D.C.
Proc. Natl. Acad. Sci. U.S.A. 91:7296-7300(1994) [PubMed: 7913750] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[12]"Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII."
Yee V.C., Pedersen L.C., Bishop P.D., Stenkamp R.E., Teller D.C.
Thromb. Res. 78:389-397(1995) [PubMed: 7660355] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[13]"Two non-proline cis peptide bonds may be important for factor XIII function."
Weiss M.S., Metzner H.J., Hilgenfeld R.
FEBS Lett. 423:291-296(1998) [PubMed: 9515726] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[14]"Identification of the calcium binding site and a novel ytterbium site in blood coagulation factor XIII by X-ray crystallography."
Fox B.A., Yee V.C., Pedersen L.C., le Trong I., Bishop P.D., Stenkamp R.E., Teller D.C.
J. Biol. Chem. 274:4917-4923(1999) [PubMed: 9988734] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[15]"Molecular basis for subtypic differences of the 'a' subunit of coagulation factor XIII with description of the genesis of the subtypes."
Suzuki K., Iwata M., Ito S., Matsui K., Uchida A., Mizoi Y.
Hum. Genet. 94:129-135(1994) [PubMed: 7913909] [Abstract]
Cited for: POLYMORPHISM.
[16]"Identification of a point mutation in factor XIII A subunit deficiency."
Board P., Coggan M., Miloszewski K.
Blood 80:937-941(1992) [PubMed: 1353995] [Abstract]
Cited for: VARIANT F13A DEFICIENCY HIS-682.
[17]"The Val34Leu polymorphism in the A subunit of coagulation factor XIII contributes to the large normal range in activity and demonstrates that the activation peptide plays a role in catalytic activity."
Kangsadalampai S., Board P.G.
Blood 92:2766-2770(1998) [PubMed: 9763561] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT LEU-35.
[18]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed: 10391209] [Abstract]
Cited for: VARIANTS LEU-35; ILE-551; LEU-565; GLN-589; ILE-651 AND GLU-652.
[19]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
+Additional computationally mapped references.

Web resources

GeneReviews
SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Factor XIII entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14539 mRNA. Translation: AAA52489.1. Different initiation.
M14354 mRNA. Translation: AAA52488.1.
M22001 expand/collapse EMBL AC list , M21987, M21988, M21989, M21990, M21991, M21992, M21993, M21995, M21996, M21997, M21998, M21999, M22000 Genomic DNA. Translation: AAA52415.1.
AB208852 mRNA. Translation: BAD92089.1. Different initiation.
AF418272 Genomic DNA. Translation: AAL12161.1.
AL157775, AL133326, AL391420 Genomic DNA. Translation: CAC36886.3.
AL391420, AL133326, AL157775 Genomic DNA. Translation: CAI39797.2.
AL133326, AL157775, AL391420 Genomic DNA. Translation: CAO03607.1.
BC027963 mRNA. Translation: AAH27963.1.
IPIIPI00297550.
PIREKHUX. A35583.
RefSeqNP_000120.2.
UniGeneHs.335513

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EVUX-ray2.01A/B2-732[»]
1EX0X-ray2.00A/B2-732[»]
1F13X-ray2.10A/B2-732[»]
1FIEX-ray2.50A/B2-732[»]
1GGTX-ray2.65A/B2-732[»]
1GGUX-ray2.10A/B2-732[»]
1GGYX-ray2.50A/B2-732[»]
1QRKX-ray2.50A/B2-732[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-377N.
STRINGP00488.

PTM databases

PhosphoSiteP00488.

2-D gel databases

OGPP00488.

Proteomic databases

PRIDEP00488.

Genome annotation databases

EnsemblENST00000264870; ENSP00000264870; ENSG00000124491; Homo sapiens. [Genome view]
GeneID2162.
KEGGhsa:2162.

Organism-specific databases

CTD2162.
GeneCardsGC06M006089.
HGNCHGNC:3531. F13A1.
HPACAB002155.
HPA001804.
MIM134570. gene+phenotype.
Orphanet331. Congenital factor XIII deficiency.
PharmGKBPA162.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG18947.
HOGENOMHBG444754.
HOVERGENP00488.
InParanoidP00488.

Enzyme and pathway databases

BRENDA2.3.2.13. 247.
ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP00488.
BgeeP00488.
CleanExHS_F13A1.
GenevestigatorP00488.
GermOnlineENSG00000124491. Homo sapiens.

Family and domain databases

InterProIPR008957. Fibronectin_typ-III-like_fold.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PfamPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
SMARTSM00460. TGc. 1 hit.
[Graphical view]
PROSITEPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00130. L-Glutamine.
NextBio8735.
PMAP-CutDBP00488.
SOURCESearch...

Entry information

Entry nameF13A_HUMAN
AccessionPrimary (citable) accession number: P00488
Secondary accession number(s): Q59HA7 expand/collapse secondary AC list , Q8N6X2, Q96P24, Q9BX29
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 19, 2010
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents