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Tissue-type plasminogen activator (t-PA) (t-plasminogen activator) (tPA) (EC 3.4.21.68) [Cleaved into: Tissue-type plasminogen activator chain A; Tissue-type plasminogen activator chain B]

 TPA_PIG                 Reviewed;         562 AA.
Q8SQ23;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
25-OCT-2017, entry version 97.
RecName: Full=Tissue-type plasminogen activator;
Short=t-PA;
Short=t-plasminogen activator;
Short=tPA;
EC=3.4.21.68;
Contains:
RecName: Full=Tissue-type plasminogen activator chain A;
Contains:
RecName: Full=Tissue-type plasminogen activator chain B;
Flags: Precursor;
Name=PLAT;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Enamel organ;
Ding Y., Xue J., Bartlett J.D.;
"T-plasminogen activator in tooth tissues.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Converts the abundant, but inactive, zymogen plasminogen
to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By
controlling plasmin-mediated proteolysis, it plays an important
role in tissue remodeling and degradation, in cell migration and
many other physiopathological events (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Specific cleavage of Arg-|-Val bond in
plasminogen to form plasmin.
-!- ENZYME REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
-!- SUBUNIT: Heterodimer of chain A and chain B held by a disulfide
bond. Binds to fibrin with high affinity. This interaction leads
to an increase in the catalytic efficiency of the enzyme due to an
increase in affinity for plasminogen. Similarly, binding to
heparin increases the activation of plasminogen. Binds to annexin
A2, cytokeratin-8, fibronectin and laminin. Binds to mannose
receptor and the low-density lipoprotein receptor-related protein
(LRP1); these proteins are involved in TPA clearance. Binds LRP1B;
binding is followed by internalization and degradation. Forms
heterodimer with SERPINA5 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
-!- DOMAIN: Both FN1 and one of the kringle domains are required for
binding to fibrin. {ECO:0000250}.
-!- DOMAIN: Both FN1 and EGF-like domains are important for binding to
LRP1. {ECO:0000250}.
-!- DOMAIN: The FN1 domain mediates binding to annexin A2.
{ECO:0000250}.
-!- DOMAIN: The second kringle domain is implicated in binding to
cytokeratin-8 and to the endothelial cell surface binding site.
{ECO:0000250}.
-!- PTM: The single chain, almost fully active enzyme, can be further
processed into a two-chain fully active form by a cleavage after
Arg-310 catalyzed by plasmin, tissue kallikrein or factor Xa.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; AF364605; AAM00297.1; -; mRNA.
RefSeq; NP_999219.1; NM_214054.1.
UniGene; Ssc.196; -.
ProteinModelPortal; Q8SQ23; -.
SMR; Q8SQ23; -.
STRING; 9823.ENSSSCP00000007494; -.
MEROPS; S01.232; -.
PaxDb; Q8SQ23; -.
GeneID; 397121; -.
KEGG; ssc:397121; -.
CTD; 5327; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000237314; -.
HOVERGEN; HBG008633; -.
InParanoid; Q8SQ23; -.
KO; K01343; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0031639; P:plasminogen activation; IEA:InterPro.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000083; Fibronectin_type1.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR026280; Tissue_plasm_act.
InterPro; IPR034811; tPA.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR44617; PTHR44617; 1.
Pfam; PF00008; EGF; 1.
Pfam; PF00039; fn1; 1.
Pfam; PF00051; Kringle; 2.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001145; Tissue_plasm_act; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00181; EGF; 1.
SMART; SM00058; FN1; 1.
SMART; SM00130; KR; 2.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 2.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01253; FN1_1; 1.
PROSITE; PS51091; FN1_2; 1.
PROSITE; PS00021; KRINGLE_1; 2.
PROSITE; PS50070; KRINGLE_2; 2.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
2: Evidence at transcript level;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
EGF-like domain; Glycoprotein; Hydrolase; Kringle;
Plasminogen activation; Protease; Reference proteome; Repeat;
Secreted; Serine protease; Signal; Zymogen.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 32 {ECO:0000250}.
/FTId=PRO_0000285907.
PROPEP 33 35 Removed by plasmin. {ECO:0000250}.
/FTId=PRO_0000285908.
CHAIN 36 562 Tissue-type plasminogen activator.
/FTId=PRO_0000285909.
CHAIN 36 310 Tissue-type plasminogen activator chain
A. {ECO:0000250}.
/FTId=PRO_0000285910.
CHAIN 311 562 Tissue-type plasminogen activator chain
B. {ECO:0000250}.
/FTId=PRO_0000285911.
DOMAIN 39 81 Fibronectin type-I. {ECO:0000255|PROSITE-
ProRule:PRU00478}.
DOMAIN 82 120 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 126 208 Kringle 1. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 214 296 Kringle 2. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 311 561 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 42 52 Important for binding to annexin A2.
{ECO:0000250}.
ACT_SITE 357 357 Charge relay system. {ECO:0000250}.
ACT_SITE 406 406 Charge relay system. {ECO:0000250}.
ACT_SITE 513 513 Charge relay system. {ECO:0000250}.
SITE 102 102 Important for binding to LRP1.
{ECO:0000250}.
SITE 464 464 Important for single-chain activity.
{ECO:0000250}.
SITE 512 512 Important for single-chain activity.
{ECO:0000250}.
CARBOHYD 96 96 O-linked (Fuc) threonine. {ECO:0000250}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 483 483 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 71 {ECO:0000250}.
DISULFID 69 78 {ECO:0000250}.
DISULFID 86 97 {ECO:0000250}.
DISULFID 91 108 {ECO:0000250}.
DISULFID 110 119 {ECO:0000250}.
DISULFID 127 208 {ECO:0000250}.
DISULFID 148 190 {ECO:0000250}.
DISULFID 179 203 {ECO:0000250}.
DISULFID 215 296 {ECO:0000250}.
DISULFID 236 278 {ECO:0000250}.
DISULFID 267 291 {ECO:0000250}.
DISULFID 299 430 Interchain (between A and B chains).
{ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000255|PROSITE-ProRule:PRU00121,
ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000255|PROSITE-ProRule:PRU00478}.
DISULFID 342 358 {ECO:0000250}.
DISULFID 350 419 {ECO:0000250}.
DISULFID 444 519 {ECO:0000250}.
DISULFID 476 492 {ECO:0000250}.
DISULFID 509 537 {ECO:0000250}.
SEQUENCE 562 AA; 63668 MW; F9E6B4C77CB101E8 CRC64;
MYALKRELWC VLLLCGAICT SPSQETHRRL RRGVRSYRVT CRDEKTQMIY QQHQSWLRPL
LRGNRVEHCW CNDGQTQCHS VPVKSCSEPR CFNGGTCLQA IYFSDFVCQC PVGFIGRQCE
IDARATCYED QGITYRGTWS TTESGAECVN WNTSGLASMP YNGRRPDAVK LGLGNHNYCR
NPDKDSKPWC YIFKAEKYSP DFCSTPACTK EKEECYTGKG LDYRGTRSLT MSGAFCLPWN
SLVLMGKIYT AWNSNAQTLG LGKHNYCRNP DGDTQPWCHV LKDHKLTWEY CDLPQCVTCG
LRQYKEPQFR IKGGLYADIT SHPWQAAIFV KNRRSPGERF LCGGILISSC WVLSAAHCFQ
ERFPPHHVRV VLGRTYRLVP GEEEQAFEVE KYIVHKEFDD DTYDNDIALL QLKSDSLTCA
QESDAVRTVC LPEANLQLPD WTECELSGYG KHEASSPFYS ERLKEAHVRL YPSSRCTSKH
LFNKTITNNM LCAGDTRSGG DNANLHDACQ GDSGGPLVCM KGNHMTLVGV ISWGLGCGQK
DVPGVYTKVT NYLNWIRDNT RP


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