CPLM-001773

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-001773

UniProt Accession

F13A_HUMAN; P00488; Q59HA7; Q8N6X2; Q96P24; Q9BX29

Genbank Protein ID

M14539; M14354; M22001; M21987; M21988; M21989; M21990; M21991; M21992; M21993; M21995; M21996; M21997; M21998; M21999; M22000; AB208852; AF418272; AL157775; AL133326; AL391420; AL391420; AL133326; AL157775; AL133326; AL157775; AL391420; BC027963

Genbank Nucleotide ID

AAA52489.1; AAA52488.1; AAA52415.1; AAA52415.1; AAA52415.1; AAA52415.1; AAA52415.1; AAA52415.1; AAA52415.1; AAA52415.1; AAA52415.1; AAA52415.1; AAA52415.1; AAA52415.1; AAA52415.1; AAA52415.1; BAD92089.1; AAL12161.1; CAC36886.3; CAC36886.3; CAC36886.3; CAI39797.2; CAI39797.2; CAI39797.2; CAO03607.1; CAO03607.1; CAO03607.1; AAH27963.1

Protein Name

Coagulation factor XIII A chain

Protein Synonyms/Alias

Coagulation factor XIIIa; Protein-glutamine gamma-glutamyltransferase A chain; Transglutaminase A chain

Gene Name

F13A1

Gene Synonyms/Alias

F13A

Created Date

July 27, 2013

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Lysine Modification

Position	Peptide	Type	References
55	VTSVHLFKERWDTNK	acetylation	[1, 2]
69	KVDHHTDKYENNKLI	acetylation	[2]
74	TDKYENNKLIVRRGQ	acetylation	[1, 2]
114	GRYPQENKGTYIPVP	acetylation	[2]
130	VSELQSGKWGAKIVM	acetylation	[2]
134	QSGKWGAKIVMREDR	acetylation	[1, 2]
157	SPKCIVGKFRMYVAV	acetylation	[1, 2]
200	AVYLDNEKEREEYVL	acetylation	[2]
222	YGEVNDIKTRSWSYG	acetylation	[1, 2]
258	SGRGNPIKVSRVGSA	acetylation	[1, 2]
463	VDATHIGKLIVTKQI	acetylation	[1]
468	IGKLIVTKQIGGDGM	acetylation	[1]
483	MDITDTYKFQEGQEE	acetylation	[1, 2]
504	TALMYGAKKPLNTEG	acetylation	[2]
505	ALMYGAKKPLNTEGV	acetylation	[2]
514	LNTEGVMKSRSNVDM	acetylation	[2]
532	VENAVLGKDFKLSIT	acetylation	[2]
535	AVLGKDFKLSITFRN	acetylation	[1, 2]
584	TLEPLSFKKEAVLIQ	acetylation	[1, 2]
585	LEPLSFKKEAVLIQA	acetylation	[1, 2]
622	ETRDVLAKQKSTVLT	acetylation	[1, 2]
624	RDVLAKQKSTVLTIP	acetylation	[1, 2]
636	TIPEIIIKVRGTQVV	acetylation	[1, 2]
678	PGVTRPMKKMFREIR	acetylation	[1]
679	GVTRPMKKMFREIRP	acetylation	[1]
705	PWVSGHRKLIASMSS	acetylation	[1, 2]

Reference

[1] Mapping of factor XIII solvent accessibility as a function of activation state using chemical modification methods.
Turner BT Jr, Sabo TM, Wilding D, Maurer MC.
Biochemistry. 2004 Aug 3;43(30):9755-65. [PMID: 15274630]
[2] Perturbations in factor XIII resulting from activation and inhibition examined by solution based methods and detected by MALDI-TOF MS.
Sabo TM, Brasher PB, Maurer MC.
Biochemistry. 2007 Sep 4;46(35):10089-101. [PMID: 17691819]

Functional Description

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.

Sequence Annotation

ACT_SITE 315 315
ACT_SITE 374 374
ACT_SITE 397 397
METAL 437 437 Calcium.
METAL 439 439 Calcium.
METAL 486 486 Calcium.
METAL 491 491 Calcium.
MOD_RES 2 2 N-acetylserine.
CARBOHYD 614 614 N-linked (GlcNAc...).

Keyword

3D-structure; Acetylation; Acyltransferase; Blood coagulation; Calcium; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Glycoprotein; Hemostasis; Metal-binding; Polymorphism; Reference proteome; Secreted; Transferase; Zymogen.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

732 AA

Protein Sequence

MSETSRTAFG GRRAVPPNNS NAAEDDLPTV ELQGVVPRGV NLQEFLNVTS VHLFKERWDT 60
NKVDHHTDKY ENNKLIVRRG QSFYVQIDFS RPYDPRRDLF RVEYVIGRYP QENKGTYIPV 120
PIVSELQSGK WGAKIVMRED RSVRLSIQSS PKCIVGKFRM YVAVWTPYGV LRTSRNPETD 180
TYILFNPWCE DDAVYLDNEK EREEYVLNDI GVIFYGEVND IKTRSWSYGQ FEDGILDTCL 240
YVMDRAQMDL SGRGNPIKVS RVGSAMVNAK DDEGVLVGSW DNIYAYGVPP SAWTGSVDIL 300
LEYRSSENPV RYGQCWVFAG VFNTFLRCLG IPARIVTNYF SAHDNDANLQ MDIFLEEDGN 360
VNSKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQAVDSTP QENSDGMYRC GPASVQAIKH 420
GHVCFQFDAP FVFAEVNSDL IYITAKKDGT HVVENVDATH IGKLIVTKQI GGDGMMDITD 480
TYKFQEGQEE ERLALETALM YGAKKPLNTE GVMKSRSNVD MDFEVENAVL GKDFKLSITF 540
RNNSHNRYTI TAYLSANITF YTGVPKAEFK KETFDVTLEP LSFKKEAVLI QAGEYMGQLL 600
EQASLHFFVT ARINETRDVL AKQKSTVLTI PEIIIKVRGT QVVGSDMTVT VQFTNPLKET 660
LRNVWVHLDG PGVTRPMKKM FREIRPNSTV QWEEVCRPWV SGHRKLIASM SSDSLRHVYG 720
ELDVQIQRRP SM 732

Gene Ontology

GO:0005576; C:extracellular region; TAS:Reactome.
GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; TAS:Reactome.
GO:0018149; P:peptide cross-linking; IEA:Compara.
GO:0030168; P:platelet activation; TAS:Reactome.
GO:0002576; P:platelet degranulation; TAS:Reactome.

Interpro

IPR023608; Gln_gamma-glutamylTfrase_euk.
IPR013783; Ig-like_fold.
IPR014756; Ig_E-set.
IPR002931; Transglutaminase-like.
IPR008958; Transglutaminase_C.
IPR013808; Transglutaminase_CS.
IPR001102; Transglutaminase_N.

Pfam

PF00927; Transglut_C
PF01841; Transglut_core
PF00868; Transglut_N

SMART

SM00460; TGc

PROSITE

PS00547; TRANSGLUTAMINASES

PRINTS