Reviewed, UniProtKB/Swiss-Prot P06867 (PLMN_PIG)

Names and origin

Protein names

Recommended name:
    Plasminogen
    EC=3.4.21.7
Cleaved into the following 4 chains:
    1- Recommended name:
            Plasmin heavy chain A
    2- Recommended name:
            Activation peptide
    3- Recommended name:
            Plasmin heavy chain A, short form
    4- Recommended name:
            Plasmin light chain B

Gene names

Name:

PLG

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	809 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	Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation; in ovulation it weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. It cleaves fibrin, fibronectin, thrombospondin, laminin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4.
Catalytic activity	Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products.
Enzyme regulation	Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin. Cannot be activated with streptokinase.
Subunit structure	Interacts with CSPG4 By similarity.
Subcellular location	Secreted.
Domain	Kringle domains mediate interaction with CSPG4 By similarity.
Post-translational modification	N-linked glycan contains N-acetyllactosamine, sialic acid and is core fucosylated. O-linked glycans consist of Gal-GalNAc disaccharide which is modified with up to 2 sialic acid residues (microheterogeneity). In the presence of the inhibitor, the activation involves only cleavage after Arg-579, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide By similarity.
Miscellaneous	Plasmin is inactivated by alpha-2-antiplasmin immediately after dissociation from the clot.
Sequence similarities	Belongs to the peptidase S1 family. Plasminogen subfamily. Contains 5 kringle domains. Contains 1 PAN domain. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Blood coagulation Fibrinolysis Tissue remodeling
Cellular component	Secreted
Domain	Kringle Repeat Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW fibrinolysis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro tissue remodeling Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Ref.2
	Chain	20 – 809	790	Plasminogen		PRO_0000285882
	Chain	20 – 579	560	Plasmin heavy chain A		PRO_0000028075
	Peptide	20 – 97	78	Activation peptide By similarity		PRO_0000028076
	Chain	98 – 579	482	Plasmin heavy chain A, short form		PRO_0000028077
	Chain	580 – 809	230	Plasmin light chain B		PRO_0000028078
Regions
	Domain	20 – 98	79	PAN
	Domain	103 – 181	79	Kringle 1
	Domain	185 – 262	78	Kringle 2
	Domain	275 – 352	78	Kringle 3
	Domain	377 – 454	78	Kringle 4
	Domain	480 – 559	80	Kringle 5
	Domain	580 – 807	228	Peptidase S1
Sites
	Active site	621	1	Charge relay system
	Active site	664	1	Charge relay system
	Active site	759	1	Charge relay system
Amino acid modifications
	Glycosylation	308	1	N-linked (GlcNAc...) Ref.4		CAR_000019
	Glycosylation	359	1	O-linked (GalNAc...) Ref.4		CAR_000020
	Disulfide bond	49 ↔ 73		By similarity
	Disulfide bond	53 ↔ 61		By similarity
	Disulfide bond	103 ↔ 181		By similarity
	Disulfide bond	124 ↔ 164		By similarity
	Disulfide bond	152 ↔ 176		By similarity
	Disulfide bond	185 ↔ 262		By similarity
	Disulfide bond	188 ↔ 316		By similarity
	Disulfide bond	206 ↔ 245		By similarity
	Disulfide bond	234 ↔ 257		By similarity
	Disulfide bond	275 ↔ 352		By similarity
	Disulfide bond	296 ↔ 335		By similarity
	Disulfide bond	324 ↔ 347		By similarity
	Disulfide bond	377 ↔ 454		By similarity
	Disulfide bond	398 ↔ 437		By similarity
	Disulfide bond	426 ↔ 449		By similarity
	Disulfide bond	480 ↔ 559		By similarity
	Disulfide bond	501 ↔ 542		By similarity
	Disulfide bond	530 ↔ 554		By similarity
	Disulfide bond	566 ↔ 684		Interchain (between A and B chains) By similarity
	Disulfide bond	576 ↔ 584		Interchain (between A and B chains) By similarity
	Disulfide bond	606 ↔ 622		By similarity
	Disulfide bond	698 ↔ 765		By similarity
	Disulfide bond	728 ↔ 744		By similarity
	Disulfide bond	755 ↔ 783		By similarity
Experimental info
	Sequence conflict	361	1	Y → H AA sequence Ref.2
	Sequence conflict	599	1	H → Y AA sequence Ref.3
	Sequence conflict	602	1	G → R AA sequence Ref.3
	Sequence conflict	675	1	I → V AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P06867-1 [UniParc]. Last modified May 1, 2007. Version 3. Checksum: 198261D2082A075D	FASTA	809	90,615
	10 20 30 40 50 60 MDHKEVVLLL LLFLKSGLGD SLDDYVNTQG AFLFSLSRKQ VAARSVEECA AKCEAETNFI 70 80 90 100 110 120 CRAFQYHSKD QQCVVMAENS KTSPIARMRD VVLFEKRIYL SECKTGNGKN YRGTTSKTKS 130 140 150 160 170 180 GVICQKWSVS SPHIPKYSPE KFPLAGLEEN YCRNPDNDEK GPWCYTTDPE TRFDYCDIPE 190 200 210 220 230 240 CEDECMHCSG EHYEGKISKT MSGIECQSWG SQSPHAHGYL PSKFPNKNLK MNYCRNPDGE 250 260 270 280 290 300 PRPWCFTTDP NKRWEFCDIP RCTTPPPTSG PTYQCLKGRG ENYRGTVSVT ASGHTCQRWS 310 320 330 340 350 360 AQSPHKHNRT PENFPCKNLE ENYCRNPDGE TAPWCYTTDS EVRWDYCKIP SCGSSTTSTE 370 380 390 400 410 420 YLDAPVPPEQ TPVAQDCYRG NGESYRGTSS TTITGRKCQS WVSMTPHRHE KTPGNFPNAG 430 440 450 460 470 480 LTMNYCRNPD ADKSPWCYTT DPRVRWEYCN LKKCSETEQQ VTNFPAIAQV PSVEDLSEDC 490 500 510 520 530 540 MFGNGKRYRG KRATTVAGVP CQEWAAQEPH RHSIFTPETN PRAGLEKNYC RNPDGDDNGP 550 560 570 580 590 600 WCYTTNPQKL FDYCDVPQCV TSSFDCGKPK VEPKKCPARV VGGCVSIPHS WPWQISLRHR 610 620 630 640 650 660 YGGHFCGGTL ISPEWVLTAK HCLEKSSSPS SYKVILGAHE EYHLGEGVQE IDVSKLFKEP 670 680 690 700 710 720 SEADIALLKL SSPAIITDKV IPACLPTPNY VVADRTACYI TGWGETKGTY GAGLLKEARL 730 740 750 760 770 780 PVIENKVCNR YEYLGGKVSP NELCAGHLAG GIDSCQGDSG GPLVCFEKDK YILQGVTSWG 790 800 LGCALPNKPG VYVRVSRFVT WIEEIMRRN

References

[1]	Chen Y., Tan W., Cheng J. Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Amino acid sequence of the heavy chain of porcine plasmin. Comparison of the carbohydrate attachment sites with the human and bovine species." Schaller J., Marti T., Roesselet S.J., Kaempfer U., Rickli E.E. Fibrinolysis 1:91-102(1987) Cited for: PROTEIN SEQUENCE OF 20-579.
[3]	"Determination of the complete amino-acid sequence of porcine miniplasminogen." Marti T., Schaller J., Rickli E.E. Eur. J. Biochem. 149:279-285(1985) [PubMed: 3846533] [Abstract] Cited for: PROTEIN SEQUENCE OF 469-809.
[4]	"The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen. Species specificity in relation to sialylation and fucosylation patterns." Marti T., Schaller J., Rickli E.E., Schmid K., Kamerling J.P., Gerwig G.J., van Halbeek H., Vliegenthart J.F.G. Eur. J. Biochem. 173:57-63(1988) [PubMed: 3356193] [Abstract] Cited for: GLYCOSYLATION AT ASN-308 AND THR-359, STRUCTURE OF CARBOHYDRATES.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ530369 mRNA. Translation: ABF82358.1.
PIR	PLPG. S03733.
RefSeq	NP_001038055.1.
UniGene	Ssc.55956
3D structure databases
HSSP	HSSP built from PDB template 1BUI based on UniProtKB P00747.
SMR	P06867. Positions 563-809.
ModBase	Search...
Protein family/group databases
MEROPS	S01.233.
PTM databases
GlycoSuiteDB	P06867.
Genome annotation databases
GeneID	733660.
KEGG	ssc:733660.
Phylogenomic databases
HOVERGEN	P06867.
Enzyme and pathway databases
BRENDA	3.4.21.7. 249.
Family and domain databases
InterPro	IPR000001. Kringle. IPR018056. Kringle_CS. IPR018059. Kringle_sub. IPR003014. PAN-1_domain. IPR003609. Pan_app. IPR011358. Pept_S1A_Plasmin. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. IPR003966. Peptidase_S1A_prothrombin. [Graphical view]
Gene3D	G3DSA:2.40.20.10. Kringle. 5 hits.
Pfam	PF00051. Kringle. 5 hits. PF00024. PAN_1. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view]
PIRSF	PIRSF001150. Plasmin. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN. PR00018. KRINGLE. PR01505. PROTHROMBIN.
ProDom	PD000395. Kringle. 5 hits. [Graphical view] [Entries sharing at least one domain]
SMART	SM00130. KR. 5 hits. SM00473. PAN_AP. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS00021. KRINGLE_1. 5 hits. PS50070. KRINGLE_2. 5 hits. PS50948. PAN. 1 hit. PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. False negative. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLMN_PIG

Accession

Primary (citable) accession number: P06867
Secondary accession number(s): Q19AZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	May 1, 2007
Last modified:	June 16, 2009
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)