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UniProtKB/Swiss-Prot entry P00749


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name UROK_HUMAN
Primary accession number P00749
Secondary accession numbers Q15844 Q16618 Q969W6
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on March 20, 1987 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 129)
Name and origin of the protein
Protein name Urokinase-type plasminogen activator [Precursor]
Synonyms U-plasminogen activator
uPA
EC 3.4.21.73
Contains Urokinase-type plasminogen activator long chain A
Urokinase-type plasminogen activator short chain A
Urokinase-type plasminogen activator chain B
Gene name
Name: PLAU
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/13.8.2759; PubMed=2987867 [NCBI, ExPASy, EBI, Israel, Japan]
Riccio A., Grimaldi G., Verde P., Sebastio G., Boast S., Blasi F.;
"The human urokinase-plasminogen activator gene and its promoter.";
Nucleic Acids Res. 13:2759-2771(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Holmes W.E., Pennica D., Blaber M., Rey M.W., Guenzler W.A., Steffens G.J., Heyneker H.L.;
"Cloning and expression of the gene for pro-urokinase in Escherichia coli.";
Biotechnology (N.Y.) 3:923-929(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0378-1119(85)90084-8; PubMed=2415429 [NCBI, ExPASy, EBI, Israel, Japan]
Nagai M., Hiramatsu R., Kaneda T., Hayasuke N., Arimura H., Nishida M., Suyama T.;
"Molecular cloning of cDNA coding for human preprourokinase.";
Gene 36:183-188(1985).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3888571 [NCBI, ExPASy, EBI, Israel, Japan]
Jacobs P., Cravador A., Loriau R., Brockly F., Colau B., Chuchana P., van Elsen A., Herzog A., Bollen A.;
"Molecular cloning, sequencing, and expression in Escherichia coli of human preprourokinase cDNA.";
DNA 4:139-146(1985).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-15; LEU-141 AND GLN-231.
SeattleSNPs program for genomic applications;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 21-43, GLYCOSYLATION AT THR-38, AND MASS SPECTROMETRY.
PubMed=2023947 [NCBI, ExPASy, EBI, Israel, Japan]
Buko A.M., Kentzer E.J., Petros A., Menon G., Zuiderweg E.R., Sarin V.K.;
"Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.";
Proc. Natl. Acad. Sci. U.S.A. 88:3992-3996(1991).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 66-431.
PubMed=6589620 [NCBI, ExPASy, EBI, Israel, Japan]
Verde P., Stoppelli M.P., Galeffi P., di Nocera P., Blasi F.;
"Identification and primary sequence of an unspliced human urokinase poly(A)+ RNA.";
Proc. Natl. Acad. Sci. U.S.A. 81:4727-4731(1984).
[9]
PROTEIN SEQUENCE OF 21-177.
PubMed=6754569 [NCBI, ExPASy, EBI, Israel, Japan]
Gunzler W.A., Steffens G.J., Otting F., Kim S.-M.A., Frankus E., Flohe L.;
"The primary structure of high molecular mass urokinase from human urine. The complete amino acid sequence of the A chain.";
Hoppe-Seyler's Z. Physiol. Chem. 363:1155-1165(1982).
[10]
PROTEIN SEQUENCE OF 156-176 AND 179-224.
PubMed=6749491 [NCBI, ExPASy, EBI, Israel, Japan]
Schaller J., Nick H., Rickli E.E., Gillessen D., Lergier W., Studer R.O.;
"Human low-molecular-weight urinary urokinase. Partial characterization and preliminary sequence data of the two polypeptide chains.";
Eur. J. Biochem. 125:251-257(1982).
[11]
PROTEIN SEQUENCE OF 158-410.
PubMed=6754572 [NCBI, ExPASy, EBI, Israel, Japan]
Steffens G.J., Gunzler W.A., Otting F., Frankus E., Flohe L.;
"The complete amino acid sequence of low molecular mass urokinase from human urine.";
Hoppe-Seyler's Z. Physiol. Chem. 363:1043-1058(1982).
[12]
PHOSPHORYLATION AT SER-158 AND SER-323, AND MUTAGENESIS OF SER-158 AND SER-323.
DOI=10.1083/jcb.137.3.779; PubMed=9151681 [NCBI, ExPASy, EBI, Israel, Japan]
Franco P., Iaccarino C., Chiaradonna F., Brandazza A., Iavarone C., Mastronicola M.R., Nolli M.L., Stoppelli M.P.;
"Phosphorylation of human pro-urokinase on Ser138/303 impairs its receptor-dependent ability to promote myelomonocytic adherence and motility.";
J. Cell Biol. 137:779-791(1997).
[13]
INTERACTION WITH MRC2.
DOI=10.1074/jbc.275.3.1993; PubMed=10636902 [NCBI, ExPASy, EBI, Israel, Japan]
Behrendt N., Jensen O.N., Engelholm L.H., Moertz E., Mann M., Danoe K.;
"A urokinase receptor-associated protein with specific collagen binding properties.";
J. Biol. Chem. 275:1993-2002(2000).
[14]
INTERACTION WITH LRP1B.
DOI=10.1074/jbc.M102727200; PubMed=11384978 [NCBI, ExPASy, EBI, Israel, Japan]
Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.;
"The putative tumor suppressor LRP1B, a novel member of the low density lipoprotein (LDL) receptor family, exhibits both overlapping and distinct properties with the LDL receptor-related protein.";
J. Biol. Chem. 276:28889-28896(2001).
[15]
TISSUE SPECIFICITY.
DOI=10.1128/MCB.25.14.6279-6288.2005; PubMed=15988036 [NCBI, ExPASy, EBI, Israel, Japan]
Ustach C.V., Kim H.-R.C.;
"Platelet-derived growth factor D is activated by urokinase plasminogen activator in prostate carcinoma cells.";
Mol. Cell. Biol. 25:6279-6288(2005).
[16]
STRUCTURE BY NMR.
DOI=10.1038/337579a0; PubMed=2536903 [NCBI, ExPASy, EBI, Israel, Japan]
Oswald R.E., Bogusky M.J., Bamberger M., Smith R.A.G., Dobson C.M.;
"Dynamics of the multidomain fibrinolytic protein urokinase from two-dimensional NMR.";
Nature 337:579-582(1989).
[17]
STRUCTURE BY NMR OF 67-155.
DOI=10.1021/bi00155a008; PubMed=1327118 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Smith R.A.G., Dobson C.M.;
"Sequential 1H NMR assignments and secondary structure of the kringle domain from urokinase.";
Biochemistry 31:9562-9571(1992).
[18]
STRUCTURE BY NMR OF 67-155.
DOI=10.1006/jmbi.1994.1106; PubMed=8107091 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Bokman A.M., Llinas M., Smith R.A.G., Dobson C.M.;
"Solution structure of the kringle domain from urokinase-type plasminogen activator.";
J. Mol. Biol. 235:1548-1559(1994).
[19]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1016/S0969-2126(01)00203-9; PubMed=8591045 [NCBI, ExPASy, EBI, Israel, Japan]
Spraggon G., Phillips C., Nowak U.K., Ponting C.P., Saunders D., Dobson C.M., Stuart D.I., Jones E.Y.;
"The crystal structure of the catalytic domain of human urokinase-type plasminogen activator.";
Structure 3:681-691(1995).
[20]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 159-411.
DOI=10.1073/pnas.97.10.5113; PubMed=10805774 [NCBI, ExPASy, EBI, Israel, Japan]
Sperl S., Jacob U., Arroyo de Prada N., Sturzebecher J., Wilhelm O.G., Bode W., Magdolen V., Huber R., Moroder L.;
"(4-aminomethyl)phenylguanidine derivatives as nonpeptidic highly selective inhibitors of human urokinase.";
Proc. Natl. Acad. Sci. U.S.A. 97:5113-5118(2000).
[21]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 31-152 IN COMPLEX WITH PLAUR.
DOI=10.1126/science.1121143; PubMed=16456079 [NCBI, ExPASy, EBI, Israel, Japan]
Huai Q., Mazar A.P., Kuo A., Parry G.C., Shaw D.E., Callahan J., Li Y., Yuan C., Bian C., Chen L., Furie B., Furie B.C., Cines D.B., Huang M.;
"Structure of human urokinase plasminogen activator in complex with its receptor.";
Science 311:656-659(2006).
[22]
VARIANT LEU-141.
PubMed=8652631 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshimoto M., Ushiyama Y., Sakai M., Tamaki S., Hara H., Takahashi K., Sawasaki Y., Hanada K.;
"Characterization of single chain urokinase-type plasminogen activator with a novel amino-acid substitution in the kringle structure.";
Biochim. Biophys. Acta 1293:83-89(1996).
[23]
VARIANT LEU-141.
PubMed=9065988 [NCBI, ExPASy, EBI, Israel, Japan]
Conne B., Berczy M., Belin D.;
"Detection of polymorphisms in the human urokinase-type plasminogen activator gene.";
Thromb. Haemost. 77:434-435(1997).
[24]
ERRATUM.
Conne B., Berczy M., Belin D.;
Thromb. Haemost. 78:973-973(1997).
[25]
VARIANT LEU-141.
PubMed=9194591 [NCBI, ExPASy, EBI, Israel, Japan]
Turkmen B., Schmitt M., Schmalfeldt B., Trommler P., Hell W., Creutzburg S., Graeff H., Magdolen V.;
"Mutational analysis of the genes encoding urokinase-type plasminogen activator (uPA) and its inhibitor PAI-1 in advanced ovarian cancer.";
Electrophoresis 18:686-689(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X02419; CAA26268.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M15476; AAA61253.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D00244; BAA00175.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D11143; BAA01919.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X02760; CAA26535.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF377330; AAK53822.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013575; AAH13575.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K03226; AAC97138.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02286; AAA61252.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
A21571; CAA01559.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
A18397; CAA01390.1; -; Unassigned_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00931; UKHU.
RefSeq NP_002649.1; -.
UniGene Hs.77274
3D structure databases
PDB
1C5W; X-ray; 1.94 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1C5X; X-ray; 1.75 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1C5Y; X-ray; 1.65 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1C5Z; X-ray; 1.85 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1EJN; X-ray; 1.80 A; A=179-431.[ExPASy / RCSB / EBI]
1F5K; X-ray; 1.80 A; U=179-431.[ExPASy / RCSB / EBI]
1F5L; X-ray; 2.10 A; A=179-431.[ExPASy / RCSB / EBI]
1F92; X-ray; 2.60 A; A=179-431.[ExPASy / RCSB / EBI]
1FV9; X-ray; 3.00 A; A=179-423.[ExPASy / RCSB / EBI]
1GI7; X-ray; 1.79 A; A=156-178, B=179-423.[ExPASy / RCSB / EBI]
1GI8; X-ray; 1.75 A; A=156-178, B=179-423.[ExPASy / RCSB / EBI]
1GI9; X-ray; 1.80 A; A=156-178, B=179-423.[ExPASy / RCSB / EBI]
1GJ7; X-ray; 1.50 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1GJ8; X-ray; 1.64 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1GJ9; X-ray; 1.80 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1GJA; X-ray; 1.56 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1GJB; X-ray; 1.90 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1GJC; X-ray; 1.73 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1GJD; X-ray; 1.75 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1KDU; NMR; -; A=69-153.[ExPASy / RCSB / EBI]
1LMW; X-ray; 2.50 A; A/C=156-178, B/D=179-431.[ExPASy / RCSB / EBI]
1O3P; X-ray; 1.81 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1O5A; X-ray; 1.68 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1O5B; X-ray; 1.85 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1O5C; X-ray; 1.63 A; A=156-178, B=179-431.[ExPASy / RCSB / EBI]
1OWD; X-ray; 2.32 A; A=179-423.[ExPASy / RCSB / EBI]
1OWE; X-ray; 1.60 A; A=179-423.[ExPASy / RCSB / EBI]
1OWH; X-ray; 1.61 A; A=179-423.[ExPASy / RCSB / EBI]
1OWI; X-ray; 2.93 A; A=179-423.[ExPASy / RCSB / EBI]
1OWJ; X-ray; 3.10 A; A=179-423.[ExPASy / RCSB / EBI]
1OWK; X-ray; 2.80 A; A=179-423.[ExPASy / RCSB / EBI]
1SC8; X-ray; 2.40 A; U=164-425.[ExPASy / RCSB / EBI]
1SQA; X-ray; 2.00 A; A=179-423.[ExPASy / RCSB / EBI]
1SQO; X-ray; 1.84 A; A=179-423.[ExPASy / RCSB / EBI]
1SQT; X-ray; 1.90 A; A=179-423.[ExPASy / RCSB / EBI]
1U6Q; X-ray; 2.02 A; A=179-423.[ExPASy / RCSB / EBI]
1URK; NMR; -; A=26-155.[ExPASy / RCSB / EBI]
1VJ9; X-ray; 2.40 A; U=164-425.[ExPASy / RCSB / EBI]
1VJA; X-ray; 2.00 A; U=164-425.[ExPASy / RCSB / EBI]
2FD6; X-ray; 1.90 A; A=31-152.[ExPASy / RCSB / EBI]
2I9A; X-ray; 1.90 A; A/B/C/D=19-163.[ExPASy / RCSB / EBI]
2I9B; X-ray; 2.80 A; A/B/C/D=19-163.[ExPASy / RCSB / EBI]
2JDE; X-ray; 2.20 A; A/B/C/D/E/F=156-431.[ExPASy / RCSB / EBI]
2NWN; X-ray; 2.15 A; A=179-431.[ExPASy / RCSB / EBI]
2O8T; X-ray; 1.45 A; A=179-431.[ExPASy / RCSB / EBI]
2O8U; X-ray; 1.70 A; A=179-431.[ExPASy / RCSB / EBI]
2O8W; X-ray; 1.86 A; A=179-431.[ExPASy / RCSB / EBI]
2VIN; X-ray; 1.90 A; A=179-431.[ExPASy / RCSB / EBI]
2VIO; X-ray; 1.80 A; A=179-431.[ExPASy / RCSB / EBI]
2VIP; X-ray; 1.72 A; A=179-431.[ExPASy / RCSB / EBI]
2VIQ; X-ray; 2.00 A; A=179-431.[ExPASy / RCSB / EBI]
2VIV; X-ray; 1.72 A; A=179-431.[ExPASy / RCSB / EBI]
2VIW; X-ray; 2.05 A; A=179-431.[ExPASy / RCSB / EBI]
2VNT; X-ray; 2.20 A; A/B/C/D/E/F=156-431.[ExPASy / RCSB / EBI]
3BT1; X-ray; 2.80 A; A=19-153.[ExPASy / RCSB / EBI]
3BT2; X-ray; 2.50 A; A=19-153.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1C5W; -.
1C5X; -.
1C5Y; -.
1C5Z; -.
1EJN; -.
1F5K; -.
1F5L; -.
1F92; -.
1FV9; -.
1GI7; -.
1GI8; -.
1GI9; -.
1GJ7; -.
1GJ8; -.
1GJ9; -.
1GJA; -.
1GJB; -.
1GJC; -.
1GJD; -.
1KDU; -.
1LMW; -.
1O3P; -.
1O5A; -.
1O5B; -.
1O5C; -.
1OWD; -.
1OWE; -.
1OWH; -.
1OWI; -.
1OWJ; -.
1OWK; -.
1SC8; -.
1SQA; -.
1SQO; -.
1SQT; -.
1U6Q; -.
1URK; -.
1VJ9; -.
1VJA; -.
2FD6; -.
2I9A; -.
2I9B; -.
2JDE; -.
2NWN; -.
2O8T; -.
2O8U; -.
2O8W; -.
2VIN; -.
2VIO; -.
2VIP; -.
2VIQ; -.
2VIV; -.
2VIW; -.
2VNT; -.
3BT1; -.
3BT2; -.
ModBase P00749.
Protein family/group databases
MEROPS S01.231; -.
PTM databases
GlycoSuiteDB P00749; -.
PhosphoSite P00749; -.
Enzyme and pathway databases
Reactome REACT_604; Hemostasis.
Organism-specific databases
HGNC HGNC:9052; PLAU.
GenAtlas PLAU.
HPA HPA008719; -.
MIM 191840; gene. [NCBI / EBI]
PharmGKB PA33382; -.
GeneCards P00749.
Gene expression databases
ArrayExpress P00749; -.
CleanEx HS_PLAU; -.
GermOnline ENSG00000122861; Homo sapiens.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from experiment from Reactome).
GO:0006935; Biological process: chemotaxis (traceable author statement from ProtInc).
GO:0006508; Biological process: proteolysis (traceable author statement from ProtInc).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR006210; EGF.
IPR000742; EGF_3.
IPR013032; EGF_like_reg_CS.
IPR000001; Kringle.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.
Gene3D G3DSA:2.40.20.10; Kringle; 1.
Pfam PF00051; Kringle; 1.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PRINTS PR00722; CHYMOTRYPSIN.
PR00018; KRINGLE.
ProDom PD000395; Kringle; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00181; EGF; 1.
SM00130; KR; 1.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS00022; EGF_1; 1.
PS01186; EGF_2; FALSE_NEG.
PS50026; EGF_3; 1.
PS00021; KRINGLE_1; 1.
PS50070; KRINGLE_2; 1.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00749.
ProtoNet P00749.
Genome annotation databases
Ensembl ENSG00000122861; Homo sapiens. [Contig view]
GeneID 5328; -.
KEGG hsa:5328; -.
Phylogenomic databases
HOGENOM P00749; -.
HOVERGEN P00749; -.
Other
BindingDB P00749; -.
DrugBank DB00594; Amiloride.
DB00013; Urokinase.
LinkHub P00749; -.
NextBio 20628; -.
SOURCE PLAU; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Blood coagulation; Direct protein sequencing; EGF-like domain; Fibrinolysis; Glycoprotein; Hydrolase; Kringle; Pharmaceutical; Phosphoprotein; Plasminogen activation; Polymorphism; Protease; Secreted; Serine protease; Signal; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20      
CHAIN   21   431  411     Urokinase-type plasminogen activator. PRO_0000028318
CHAIN   21   177  157     Urokinase-type plasminogen activator long chain A. PRO_0000028319
CHAIN   156   177  22     Urokinase-type plasminogen activator short chain A. PRO_0000028320
CHAIN   179   431  253     Urokinase-type plasminogen activator chain B. PRO_0000028321
DOMAIN   27    63  37     EGF-like. 
DOMAIN   70   151  82     Kringle. 
DOMAIN   179   424  246     Peptidase S1. 
REGION   34    57  24     Binds urokinase plasminogen activator surface receptor (By similarity). 
REGION   152   177  26     Connecting peptide. 
ACT_SITE   224   224        Charge relay system. 
ACT_SITE   275   275        Charge relay system. 
ACT_SITE   376   376        Charge relay system. 
SITE   177   178  2     Cleavage; during zymogen activation. 
MOD_RES   158   158        Phosphoserine. 
MOD_RES   323   323        Phosphoserine. 
CARBOHYD   38    38        O-linked (Fuc). 
CARBOHYD   322   322        N-linked (GlcNAc...) [GlycoSuiteDB]. CAR_000026
DISULFID   31    39         
DISULFID   33    51         
DISULFID   53    62         
DISULFID   70   151         
DISULFID   91   133         
DISULFID   122   146         
DISULFID   168   299        Interchain (between A and B chains). 
DISULFID   209   225         
DISULFID   217   288         
DISULFID   313   382         
DISULFID   345   361         
DISULFID   372   400         
VARIANT   15    15  1     V -> L. VAR_038730 
VARIANT   141   141  1     P -> L (rare polymorphism; linked with a decrease in the affinity for fibrin-binding). VAR_006722 
VARIANT   214   214  1     M -> I. VAR_013102 [3D]
VARIANT   231   231  1     K -> Q. VAR_038731 [3D]
MUTAGEN   158   158        S->E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-323. 
MUTAGEN   323   323        S->E: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-158. 
CONFLICT   151   151        C -> W (in Ref. 4; CAA26535). 
CONFLICT   386   386        G -> C (in Ref. 4; CAA26535). 
CONFLICT   430   430        A -> V (in Ref. 4; CAA26535). 
STRAND   38    41  4      
TURN   43    47  5      
STRAND   49    52  4      
STRAND   57    59  3      
STRAND   64    67  4      
HELIX   99   101  3      
STRAND   106   108  3      
HELIX   109   112  4      
TURN   113   115  3      
STRAND   117   119  3      
STRAND   132   135  4