Reviewed, UniProtKB/Swiss-Prot P00488 (F13A_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	732 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Biological process	Blood coagulation
Cellular component	Cytoplasm Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
PTM	Acetylation Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	blood coagulation Traceable author statement. Source: ProtInc
Cellular component	extracellular region Ref.2 Inferred from Experiment. Source: Reactome platelet alpha granule lumen Inferred from Experiment. Source: Reactome
Molecular function	acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein-glutamine gamma-glutamyltransferase activity Ref.8 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8 Ref.9

Propeptide

2 – 38

37

Activation peptide

PRO_0000033646

Chain

39 – 732

694

Coagulation factor XIII A chain

PRO_0000033647

Sites

Active site

315

1

Active site

374

1

Active site

397

1

Metal binding

437

1

Calcium

Metal binding

439

1

Calcium

Metal binding

486

1

Calcium

Metal binding

491

1

Calcium

Site

38 – 39

2

Cleavage; by thrombin; to produce active factor XIII-A

Amino acid modifications

Modified residue

2

1

N-acetylserine

Glycosylation

614

1

N-linked (GlcNAc...) Ref.10

Natural variations

Natural variant

35

1

V → L Higher specific activity. dbSNP rs5985. Ref.5 Ref.17 Ref.18

VAR_013927

Natural variant

40

1

V → I

VAR_020910

Natural variant

205

1

Y → F: dbSNP rs3024477. Ref.5

VAR_020911

Natural variant

351

1

M → K: dbSNP rs2230848.

VAR_057350

Natural variant

551

1

T → I: dbSNP rs5984. Ref.18

VAR_013928

Natural variant

565

1

P → L in allele F13A*1A, allele F13A*2A and allele F13*(2)A. dbSNP rs5982. Ref.5 Ref.18 Ref.3

VAR_007471

Natural variant

589

1

L → Q: dbSNP rs5983. Ref.18

VAR_013929

Natural variant

650

1

T → I: dbSNP rs17852475. Ref.7

VAR_060545

Natural variant

651

1

V → I in allele F13A*2A and allele F13A*2B. dbSNP rs5987. Ref.5 Ref.18 Ref.1

VAR_007472

Natural variant

652

1

Q → E in allele F13A*1A and allele F13A*1B. dbSNP rs5988. Ref.5 Ref.18 Ref.7 Ref.4 Ref.6

VAR_007473

Natural variant

682

1

R → H in F13A deficiency. Ref.16

VAR_007474

Experimental info

Sequence conflict

36

1

Missing AA sequence Ref.9

Sequence conflict

89

1

F → L in AAA52488. Ref.1

Secondary structure

1

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732

Helix Strand Turn

Details...

Beta strand

48 – 52

5

Helix

60 – 64

5

Beta strand

74 – 78

5

Beta strand

83 – 91

9

Turn

95 – 97

3

Beta strand

100 – 105

6

Beta strand

107 – 109

3

Helix

112 – 114

3

Beta strand

116 – 120

5

Beta strand

122 – 125

4

Beta strand

132 – 139

8

Beta strand

142 – 148

7

Beta strand

156 – 166

11

Beta strand

169 – 172

4

Helix

177 – 179

3

Beta strand

181 – 184

4

Helix

199 – 205

7

Beta strand

210 – 217

8

Beta strand

220 – 227

8

Helix

235 – 245

11

Helix

250 – 252

3

Helix

256 – 267

12

Beta strand

274 – 278

5

Turn

290 – 292

3

Helix

297 – 306

10

Beta strand

310 – 313

4

Helix

315 – 329

15

Beta strand

333 – 341

9

Beta strand

348 – 355

8

Turn

363 – 365

3

Beta strand

371 – 381

11

Beta strand

392 – 403

12

Beta strand

406 – 414

9

Helix

415 – 420

6

Beta strand

425 – 428

4

Helix

429 – 437

9

Beta strand

439 – 445

7

Beta strand

451 – 457

7

Beta strand

464 – 468

5

Beta strand

470 – 473

4

Beta strand

475 – 477

3

Helix

479 – 482

4

Helix

489 – 500

12

Beta strand

519 – 525

7

Beta strand

534 – 542

9

Beta strand

544 – 546

3

Beta strand

548 – 559

12

Beta strand

565 – 578

14

Beta strand

580 – 590

11

Helix

592 – 594

3

Turn

595 – 598

4

Beta strand

604 – 613

10

Turn

614 – 616

3

Beta strand

619 – 627

9

Beta strand

634 – 639

6

Beta strand

647 – 654

8

Beta strand

657 – 659

3

Beta strand

661 – 669

9

Turn

671 – 673

3

Beta strand

677 – 684

8

Beta strand

689 – 696

8

Beta strand

706 – 711

6

Beta strand

718 – 722

5

Beta strand

725 – 727

3

Sequences

	Sequence		Length	Mass (Da)
	P00488-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 51A83A9B8B1370D4	FASTA	732	83,267
	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

References

	« Hide 'large scale' referencesShow '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. , 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 , 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.

IPI

IPI00297550.

PIR

EKHUX. A35583.

RefSeq

NP_000120.2.

UniGene

Hs.335513

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EVU	X-ray	2.01	A/B	2-732	[»]
1EX0	X-ray	2.00	A/B	2-732	[»]
1F13	X-ray	2.10	A/B	2-732	[»]
1FIE	X-ray	2.50	A/B	2-732	[»]
1GGT	X-ray	2.65	A/B	2-732	[»]
1GGU	X-ray	2.10	A/B	2-732	[»]
1GGY	X-ray	2.50	A/B	2-732	[»]
1QRK	X-ray	2.50	A/B	2-732	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-377N.

STRING

P00488.

PTM databases

PhosphoSite

P00488.

2-D gel databases

OGP

P00488.

Proteomic databases

PRIDE

P00488.

Genome annotation databases

Ensembl

ENST00000264870; ENSP00000264870; ENSG00000124491; Homo sapiens. [Genome view]

GeneID

2162.

KEGG

hsa:2162.

Organism-specific databases

CTD

2162.

GeneCards

GC06M006089.

HGNC

HGNC:3531. F13A1.

HPA

CAB002155.
HPA001804.

MIM

134570. gene+phenotype.

Orphanet

331. Congenital factor XIII deficiency.

PharmGKB

PA162.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18947.

HOGENOM

HBG444754.

HOVERGEN

P00488.

InParanoid

P00488.

Enzyme and pathway databases

BRENDA

2.3.2.13. 247.

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P00488.

Bgee

P00488.

CleanEx

HS_F13A1.

Genevestigator

P00488.

GermOnline

ENSG00000124491. Homo sapiens.

Family and domain databases

InterPro

IPR008957. 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]

Gene3D

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

Pfam

PF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]

SMART

SM00460. TGc. 1 hit.
[Graphical view]

PROSITE

PS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00130. L-Glutamine.

NextBio

8735.

PMAP-CutDB

P00488.

SOURCE

Search...

Entry information

Entry name

F13A_HUMAN

Accession

Primary (citable) accession number: P00488
Secondary accession number(s): Q59HA7 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.