Summary: Kringle domain
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Kringle domain Edit Wikipedia article
![]() Fragment of bovine prothrombin in complex with calcium and lysophosphatidylserine. The protein associate with membrane through its alpha-helical GLA domain. The adjacent kringle domain is beta-structural (yellow). | |||||||||
Identifiers | |||||||||
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Symbol | Kringle | ||||||||
Pfam | PF00051 | ||||||||
InterPro | IPR000001 | ||||||||
SMART | KR | ||||||||
PROSITE | PDOC00020 | ||||||||
SCOPe | 1pk4 / SUPFAM | ||||||||
OPM superfamily | 115 | ||||||||
OPM protein | 1h8p | ||||||||
CDD | cd00108 | ||||||||
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Kringle Domains are autonomous protein domains that fold into large loops stabilized by 3 disulfide linkages. These are important in protein–protein interactions with blood coagulation factors. The name Kringle comes from the Scandinavian pastry that these structures resemble.
Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein(a).
Kringles are found throughout the blood clotting and fibrinolytic proteins. Kringle domains are believed to play a role in binding mediators (e.g., membranes, other proteins or phospholipids), and in the regulation of proteolytic activity.[1][2][3] Kringle domains[4][5][6] are characterised by a triple loop, 3-disulfide bridge structure, whose conformation is defined by a number of hydrogen bonds and small pieces of anti-parallel beta-sheet. They are found in a varying number of copies in some plasma proteins including prothrombin and urokinase-type plasminogen activator, which are serine proteases belonging to MEROPS peptidase family S1A.
Human proteins containing this domain
ATF; F12; F2; HABP2; HGF; HGFAC; KREMEN1; KREMEN2; LPA; LPAL2; MST1; PIK3IP1; PLAT; PLAU; PLG; PRSS12; ROR1; ROR2;
References
- ^ Fujikawa K, McMullen BA (1985). "Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor)". J. Biol. Chem. 260 (9): 5328–5341. PMID 3886654.
- ^ Patthy L, Trexler M, Banyai L, Varadi A, Vali Z (1984). "Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteases". FEBS Lett. 171 (1): 131–136. doi:10.1016/0014-5793(84)80473-1. PMID 6373375.
- ^ Atkinson RA, Williams RJ (1990). "Solution structure of the kringle 4 domain from human plasminogen by 1H nuclear magnetic resonance spectroscopy and distance geometry". J. Mol. Biol. 212 (3): 541–552. doi:10.1016/0022-2836(90)90330-O. PMID 2157850.
- ^ Castellino FJ, Beals JM (1987). "The genetic relationships between the kringle domains of human plasminogen, prothrombin, tissue plasminogen activator, urokinase, and coagulation factor XII". J. Mol. Evol. 26 (4): 358–369. doi:10.1007/BF02101155. PMID 3131537.
- ^ Patthy L (1985). "Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules". Cell. 41 (3): 657–663. doi:10.1016/S0092-8674(85)80046-5. PMID 3891096.
- ^ Takahashi K, Ikeo K, Gojobori T (1991). "Evolutionary origin of numerous kringles in human and simian apolipoprotein(a)". FEBS Lett. 287 (1): 146–148. doi:10.1016/0014-5793(91)80036-3. PMID 1879523.
External links
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Kringle domain Provide feedback
Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.
External database links
HOMSTRAD: | kringle |
MEROPS: | S1 |
PRINTS: | PR00018 |
PROSITE: | PDOC00020 |
PROSITE profile: | PS50070 |
SCOP: | 1pk4 |
SMART: | KR |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000001
Kringles are autonomous structural domains, found throughout the blood clotting and fibrinolytic proteins. Kringle domains are believed to play a role in binding mediators (e.g., membranes, other proteins or phospholipids), and in the regulation of proteolytic activity [PUBMED:3886654, PUBMED:6373375, PUBMED:2157850]. Kringle domains [PUBMED:3131537, PUBMED:3891096, PUBMED:1879523] are characterised by a triple loop, 3-disulphide bridge structure, whose conformation is defined by a number of hydrogen bonds and small pieces of anti-parallel beta-sheet. They are found in a varying number of copies in some plasma proteins including prothrombin and urokinase-type plasminogen activator, which are serine proteases belonging to MEROPS peptidase family S1A.
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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Seed (23) |
Full (7468) |
Representative proteomes | UniProt (11875) |
NCBI (20584) |
Meta (48) |
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RP15 (1041) |
RP35 (2084) |
RP55 (4852) |
RP75 (7434) |
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HTML | |||||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (23) |
Full (7468) |
Representative proteomes | UniProt (11875) |
NCBI (20584) |
Meta (48) |
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RP15 (1041) |
RP35 (2084) |
RP55 (4852) |
RP75 (7434) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
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Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
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Curation
Seed source: | Swissprot_feature_table |
Previous IDs: | kringle; |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Sonnhammer ELL |
Number in seed: | 23 |
Number in full: | 7468 |
Average length of the domain: | 78.00 aa |
Average identity of full alignment: | 39 % |
Average coverage of the sequence by the domain: | 20.38 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 79 | ||||||||||||
Family (HMM) version: | 19 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Interactions
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Kringle domain has been found. There are 207 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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