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Database: UniProt
Entry: P00750
LinkDB: P00750
Original site: P00750 
ID   TPA_HUMAN               Reviewed;         562 AA.
AC   P00750; A8K022; B2R8E8; Q15103; Q503B0; Q6PJA5; Q7Z7N2; Q86YK8;
AC   Q9BU99; Q9BZW1;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   16-JAN-2019, entry version 245.
DE   RecName: Full=Tissue-type plasminogen activator;
DE            Short=t-PA;
DE            Short=t-plasminogen activator;
DE            Short=tPA;
DE            EC=3.4.21.68;
DE   AltName: INN=Alteplase;
DE   AltName: INN=Reteplase;
DE   Contains:
DE     RecName: Full=Tissue-type plasminogen activator chain A;
DE   Contains:
DE     RecName: Full=Tissue-type plasminogen activator chain B;
DE   Flags: Precursor;
GN   Name=PLAT;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Melanoma;
RX   PubMed=6337343; DOI=10.1038/301214a0;
RA   Pennica D., Holmes W.E., Kohr W.J., Harkins R.N., Vehar G.A.,
RA   Ward C.A., Bennett W.F., Yelverton E., Seeburg P.H., Heyneker H.L.,
RA   Goeddel D.V., Collen D.;
RT   "Cloning and expression of human tissue-type plasminogen activator
RT   cDNA in E. coli.";
RL   Nature 301:214-221(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6089198; DOI=10.1073/pnas.81.17.5355;
RA   Ny T., Elgh F., Lund B.;
RT   "The structure of the human tissue-type plasminogen activator gene:
RT   correlation of intron and exon structures to functional and structural
RT   domains.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:5355-5359(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3009482;
RA   Friezner Degen S.J., Rajput B., Reich E.;
RT   "The human tissue plasminogen activator gene.";
RL   J. Biol. Chem. 261:6972-6985(1986).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3090401;
RA   Harris T.J., Patel T., Marston F.A., Little S., Emtage J.S.,
RA   Opdenakker G., Volckaert G., Rombauts W., Billiau A., Somer P.;
RT   "Cloning of cDNA coding for human tissue-type plasminogen activator
RT   and its expression in Escherichia coli.";
RL   Mol. Biol. Med. 3:279-292(1986).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2824147; DOI=10.1089/dna.1987.6.461;
RA   Reddy V.B., Garramone A.J., Sasak H., Wei C.-M., Watkins P., Galli J.,
RA   Hsiung N.;
RT   "Expression of human uterine tissue-type plasminogen activator in
RT   mouse cells using BPV vectors.";
RL   DNA 6:461-472(1987).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal lung;
RX   PubMed=3133640; DOI=10.1093/nar/16.12.5695;
RA   Sasaki H., Saito Y., Hayashi M., Otsuka K., Niwa M.;
RT   "Nucleotide sequence of the tissue-type plasminogen activator cDNA
RT   from human fetal lung cells.";
RL   Nucleic Acids Res. 16:5695-5695(1988).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Umbilical vein;
RX   PubMed=2107528; DOI=10.1093/nar/18.4.1086;
RA   Siebert P.D., Fong K.;
RT   "Variant tissue-type plasminogen activator (PLAT) cDNA obtained from
RT   human endothelial cells.";
RL   Nucleic Acids Res. 18:1086-1086(1990).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA   Dou D.;
RT   "A brain-type plasminogen activator.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Liu Y., Xu L., Zeng Y., He X.;
RT   "cDNA of tissue plasminogen activator.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-34; SER-136;
RP   THR-146 AND TRP-164.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Brain, Placenta, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RX   PubMed=3161893;
RA   Fisher R., Waller E.K., Grossi G., Thompson D., Tizard R.,
RA   Schleuning W.-D.;
RT   "Isolation and characterization of the human tissue-type plasminogen
RT   activator structural gene including its 5' flanking region.";
RL   J. Biol. Chem. 260:11223-11230(1985).
RN   [16]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 31-562.
RX   PubMed=1368681; DOI=10.1271/bbb1961.55.1225;
RA   Itagaki Y., Yasuda H., Morinaga T., Mitsuda S., Higashio K.;
RT   "Purification and characterization of tissue plasminogen activator
RT   secreted by human embryonic lung diploid fibroblasts, IMR-90 cells.";
RL   Agric. Biol. Chem. 55:1225-1232(1991).
RN   [17]
RP   PROTEIN SEQUENCE OF 33-52 AND 311-330.
RC   TISSUE=Melanoma;
RX   PubMed=6682760; DOI=10.1111/j.1432-1033.1983.tb07418.x;
RA   Wallen P., Pohl G., Bergsdorf N., Raanby M., Ny T., Joernvall H.;
RT   "Purification and characterization of a melanoma cell plasminogen
RT   activator.";
RL   Eur. J. Biochem. 132:681-686(1983).
RN   [18]
RP   PROTEIN SEQUENCE OF 36-562.
RC   TISSUE=Melanoma;
RX   PubMed=6433976; DOI=10.1021/bi00311a020;
RA   Pohl G., Kaellstroem M., Bergsdorf N., Wallen P., Joernvall H.;
RT   "Tissue plasminogen activator: peptide analyses confirm an indirectly
RT   derived amino acid sequence, identify the active site serine residue,
RT   establish glycosylation sites, and localize variant differences.";
RL   Biochemistry 23:3701-3707(1984).
RN   [19]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 251-358.
RX   PubMed=6572897; DOI=10.1073/pnas.80.2.349;
RA   Edlund T., Ny T., Raanby M., Heden L.-O., Palm G., Holmgren E.,
RA   Josephson S.;
RT   "Isolation of cDNA sequences coding for a part of human tissue
RT   plasminogen activator.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:349-352(1983).
RN   [20]
RP   PARTIAL PROTEIN SEQUENCE, AND SIGNAL SEQUENCE CLEAVAGE SITE.
RA   Jalah R., Pavlakis G.N., Felber B.J.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [21]
RP   GLYCOSYLATION AT ASN-152; ASN-219 AND ASN-483, AND STRUCTURE OF
RP   CARBOHYDRATES.
RX   PubMed=2513186; DOI=10.1111/j.1432-1033.1989.tb15206.x;
RA   Pfeiffer G., Schmidt M., Strube K.-H., Geyer R.;
RT   "Carbohydrate structure of recombinant human uterine tissue
RT   plasminogen activator expressed in mouse epithelial cells.";
RL   Eur. J. Biochem. 186:273-286(1989).
RN   [22]
RP   GLYCOSYLATION AT THR-96.
RX   PubMed=1900431; DOI=10.1021/bi00223a004;
RA   Harris R.J., Leonard C.K., Guzzetta A.W., Spellman M.W.;
RT   "Tissue plasminogen activator has an O-linked fucose attached to
RT   threonine-61 in the epidermal growth factor domain.";
RL   Biochemistry 30:2311-2314(1991).
RN   [23]
RP   DISULFIDE BONDS IN KRINGLE 2 DOMAIN.
RX   PubMed=1645336;
RA   Vlahos C.J., Wilhelm O.G., Hassell T., Jaskunas S.R., Bang N.U.;
RT   "Disulfide pairing of the recombinant kringle-2 domain of tissue
RT   plasminogen activator produced in Escherichia coli.";
RL   J. Biol. Chem. 266:10070-10072(1991).
RN   [24]
RP   ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
RX   PubMed=10340997; DOI=10.1093/molehr/5.6.513;
RA   He S., Lin Y.L., Liu Y.X.;
RT   "Functionally inactive protein C inhibitor in seminal plasma may be
RT   associated with infertility.";
RL   Mol. Hum. Reprod. 5:513-519(1999).
RN   [25]
RP   INTERACTION WITH LRP1B.
RX   PubMed=11384978; DOI=10.1074/jbc.M102727200;
RA   Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.;
RT   "The putative tumor suppressor LRP1B, a novel member of the low
RT   density lipoprotein (LDL) receptor family, exhibits both overlapping
RT   and distinct properties with the LDL receptor-related protein.";
RL   J. Biol. Chem. 276:28889-28896(2001).
RN   [26]
RP   SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX   PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA   Hillman R.T., Green R.E., Brenner S.E.;
RT   "An unappreciated role for RNA surveillance.";
RL   Genome Biol. 5:R8.1-R8.16(2004).
RN   [27]
RP   STRUCTURE BY NMR OF KRINGLE 2.
RX   PubMed=2558718; DOI=10.1021/bi00450a016;
RA   Byeon I.-J.L., Kelley R.F., Llinas M.;
RT   "1H NMR structural characterization of a recombinant kringle 2 domain
RT   from human tissue-type plasminogen activator.";
RL   Biochemistry 28:9350-9360(1989).
RN   [28]
RP   STRUCTURE BY NMR OF KRINGLE 2.
RX   PubMed=1901789; DOI=10.1111/j.1432-1033.1991.tb15894.x;
RA   Byeon I.-J.L., Kelley R.F., Llinas M.;
RT   "Kringle-2 domain of the tissue-type plasminogen activator. 1H-NMR
RT   assignments and secondary structure.";
RL   Eur. J. Biochem. 197:155-165(1991).
RN   [29]
RP   STRUCTURE BY NMR OF KRINGLE 2.
RX   PubMed=1762144; DOI=10.1016/0022-2836(91)90592-T;
RA   Byeon I.-J.L., Llinas M.;
RT   "Solution structure of the tissue-type plasminogen activator kringle 2
RT   domain complexed to 6-aminohexanoic acid an antifibrinolytic drug.";
RL   J. Mol. Biol. 222:1035-1051(1991).
RN   [30]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF KRINGLE 2.
RX   PubMed=1310033; DOI=10.1021/bi00116a037;
RA   de Vos A., Ultsch M.H., Kelley R.F., Padmanabhan K., Tulinskly A.,
RA   Westbrook M.L., Kossiakof A.A.;
RT   "Crystal structure of the kringle 2 domain of tissue plasminogen
RT   activator at 2.4-A resolution.";
RL   Biochemistry 31:270-279(1992).
RN   [31]
RP   STRUCTURE BY NMR OF 38-85.
RX   PubMed=1602484; DOI=10.1016/0022-2836(92)90403-7;
RA   Downing A.K., Driscoll P.C., Harvey T.S., Dudgeon T.J., Smith B.O.,
RA   Baron M., Campbell I.D.;
RT   "Solution structure of the fibrin binding finger domain of tissue-type
RT   plasminogen activator determined by 1H nuclear magnetic resonance.";
RL   J. Mol. Biol. 225:821-833(1992).
RN   [32]
RP   STRUCTURE BY NMR OF 36-126.
RX   PubMed=7582899; DOI=10.1016/S0969-2126(01)00217-9;
RA   Smith B.O., Downing A.K., Driscoll P.C., Dudgeon T.J., Campbell I.D.;
RT   "The solution structure and backbone dynamics of the fibronectin type
RT   I and epidermal growth factor-like pair of modules of tissue-type
RT   plasminogen activator.";
RL   Structure 3:823-833(1995).
RN   [33]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF CATALYTIC DOMAIN.
RX   PubMed=8613982; DOI=10.1006/jmbi.1996.0238;
RA   Lamba D., Bauer M., Huber R., Fischer S., Rudolph R., Kohnert U.,
RA   Bode W.;
RT   "The 2.3 A crystal structure of the catalytic domain of recombinant
RT   two-chain human tissue-type plasminogen activator.";
RL   J. Mol. Biol. 258:117-135(1996).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF CATALYTIC DOMAIN.
RX   PubMed=9305622; DOI=10.1093/emboj/16.16.4797;
RA   Renatus M., Engh R.A., Stubbs M.T., Huber R., Fischer S., Kohnert U.,
RA   Bode W.;
RT   "Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray
RT   crystal structure of single-chain human tPA.";
RL   EMBO J. 16:4797-4805(1997).
CC   -!- FUNCTION: Converts the abundant, but inactive, zymogen plasminogen
CC       to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By
CC       controlling plasmin-mediated proteolysis, it plays an important
CC       role in tissue remodeling and degradation, in cell migration and
CC       many other physiopathological events. Plays a direct role in
CC       facilitating neuronal migration.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to
CC         form plasmin.; EC=3.4.21.68;
CC   -!- ACTIVITY REGULATION: Inhibited by SERPINA5.
CC       {ECO:0000269|PubMed:10340997}.
CC   -!- SUBUNIT: Heterodimer of chain A and chain B held by a disulfide
CC       bond. Forms a heterodimer with SERPINA5. Binds to fibrin with high
CC       affinity. This interaction leads to an increase in the catalytic
CC       efficiency of the enzyme between 100-fold and 1000-fold, due to an
CC       increase in affinity for plasminogen. Similarly, binding to
CC       heparin increases the activation of plasminogen. Binds to annexin
CC       A2, cytokeratin-8, fibronectin and laminin. Binds to mannose
CC       receptor and the low-density lipoprotein receptor-related protein
CC       (LRP1); these proteins are involved in TPA clearance. Yet
CC       unidentified interactions on endothelial cells and vascular smooth
CC       muscle cells (VSMC) lead to a 100-fold stimulation of plasminogen
CC       activation. In addition, binding to VSMC reduces TPA inhibition by
CC       PAI-1 by 30-fold. Binds LRP1B; binding is followed by
CC       internalization and degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Long;
CC         IsoId=P00750-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P00750-2; Sequence=VSP_005411, VSP_005412;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay.;
CC       Name=3;
CC         IsoId=P00750-3; Sequence=VSP_015957;
CC         Note=No experimental confirmation available.;
CC       Name=4; Synonyms=Neonatal;
CC         IsoId=P00750-4; Sequence=VSP_028029, VSP_028030;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Synthesized in numerous tissues (including
CC       tumors) and secreted into most extracellular body fluids, such as
CC       plasma, uterine fluid, saliva, gingival crevicular fluid, tears,
CC       seminal fluid, and milk.
CC   -!- DOMAIN: Both FN1 and one of the kringle domains are required for
CC       binding to fibrin.
CC   -!- DOMAIN: Both FN1 and EGF-like domains are important for binding to
CC       LRP1.
CC   -!- DOMAIN: The FN1 domain mediates binding to annexin A2.
CC   -!- DOMAIN: The second kringle domain is implicated in binding to
CC       cytokeratin-8 and to the endothelial cell surface binding site.
CC   -!- PTM: The single chain, almost fully active enzyme, can be further
CC       processed into a two-chain fully active form by a cleavage after
CC       Arg-310 catalyzed by plasmin, tissue kallikrein or factor Xa.
CC   -!- PTM: Differential cell-specific N-linked glycosylation gives rise
CC       to two glycoforms, type I (glycosylated at Asn-219) and type II
CC       (not glycosylated at Asn-219). The single chain type I glycoform
CC       is less readily converted into the two-chain form by plasmin, and
CC       the two-chain type I glycoform has a lower activity than the two-
CC       chain type II glycoform in the presence of fibrin.
CC       {ECO:0000269|PubMed:1900431}.
CC   -!- PTM: N-glycosylation of Asn-152; the bound oligomannosidic glycan
CC       is involved in the interaction with the mannose receptor.
CC       {ECO:0000269|PubMed:1900431}.
CC   -!- PTM: Characterization of O-linked glycan was studied in Bowes
CC       melanoma cell line. {ECO:0000269|PubMed:1900431}.
CC   -!- DISEASE: Note=Increased activity of TPA results in increased
CC       fibrinolysis of fibrin blood clots that is associated with
CC       excessive bleeding. Defective release of TPA results in
CC       hypofibrinolysis that can lead to thrombosis or embolism.
CC       {ECO:0000269|PubMed:1762144}.
CC   -!- PHARMACEUTICAL: Available under the names Activase (Genentech) and
CC       Retavase (Centocor and Roche) [Retavase is a fragment of TPA that
CC       contains kringle 2 and the protease domain; it was also known as
CC       BM 06.022]. Used in Acute Myocardial Infarction (AMI), in Acute
CC       Ischemic Stroke (AIS) and Pulmonary Embolism (PE) to initiate
CC       fibrinolysis.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Tissue plasminogen activator
CC       entry;
CC       URL="https://en.wikipedia.org/wiki/Tissue_plasminogen_Activator";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/plat/";
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=PLAT";
CC   -!- WEB RESOURCE: Name=Activase; Note=Clinical information on
CC       Activase;
CC       URL="https://www.activase.com/";
CC   -!- WEB RESOURCE: Name=Chiesi; Note=Clinical information on Retavase;
CC       URL="https://chiesiusa.com/products/retavase-2/";
DR   EMBL; L00153; AAB59510.1; -; Genomic_DNA.
DR   EMBL; L00141; AAB59510.1; JOINED; Genomic_DNA.
DR   EMBL; L00142; AAB59510.1; JOINED; Genomic_DNA.
DR   EMBL; L00143; AAB59510.1; JOINED; Genomic_DNA.
DR   EMBL; L00144; AAB59510.1; JOINED; Genomic_DNA.
DR   EMBL; L00145; AAB59510.1; JOINED; Genomic_DNA.
DR   EMBL; L00146; AAB59510.1; JOINED; Genomic_DNA.
DR   EMBL; L00147; AAB59510.1; JOINED; Genomic_DNA.
DR   EMBL; L00148; AAB59510.1; JOINED; Genomic_DNA.
DR   EMBL; L00149; AAB59510.1; JOINED; Genomic_DNA.
DR   EMBL; L00150; AAB59510.1; JOINED; Genomic_DNA.
DR   EMBL; L00151; AAB59510.1; JOINED; Genomic_DNA.
DR   EMBL; K03021; AAA98809.1; -; Genomic_DNA.
DR   EMBL; M15518; AAA60111.1; -; mRNA.
DR   EMBL; M18182; AAA36800.1; -; mRNA.
DR   EMBL; X07393; CAA30302.1; -; mRNA.
DR   EMBL; X13097; CAA31489.1; -; mRNA.
DR   EMBL; AF260825; AAK11956.1; -; mRNA.
DR   EMBL; AY221101; AAO34406.1; -; mRNA.
DR   EMBL; AK289387; BAF82076.1; -; mRNA.
DR   EMBL; AK290575; BAF83264.1; -; mRNA.
DR   EMBL; AK313342; BAG36145.1; -; mRNA.
DR   EMBL; BT007060; AAP35709.1; -; mRNA.
DR   EMBL; AY291060; AAP34246.1; -; Genomic_DNA.
DR   EMBL; CH471080; EAW63235.1; -; Genomic_DNA.
DR   EMBL; CH471080; EAW63233.1; -; Genomic_DNA.
DR   EMBL; BC002795; AAH02795.3; -; mRNA.
DR   EMBL; BC007231; AAH07231.1; -; mRNA.
DR   EMBL; BC013968; AAH13968.3; -; mRNA.
DR   EMBL; BC018636; AAH18636.3; -; mRNA.
DR   EMBL; BC095403; AAH95403.1; -; mRNA.
DR   EMBL; M11890; AAA61213.1; -; Genomic_DNA.
DR   EMBL; M11889; AAA61213.1; JOINED; Genomic_DNA.
DR   EMBL; D01096; BAA00881.1; -; mRNA.
DR   EMBL; V00570; CAA23833.1; -; mRNA.
DR   CCDS; CCDS6126.1; -. [P00750-1]
DR   CCDS; CCDS6127.1; -. [P00750-3]
DR   PIR; A94004; UKHUT.
DR   PIR; I38098; I38098.
DR   RefSeq; NP_000921.1; NM_000930.4. [P00750-1]
DR   RefSeq; NP_001306118.1; NM_001319189.1.
DR   RefSeq; NP_127509.1; NM_033011.3. [P00750-3]
DR   UniGene; Hs.491582; -.
DR   PDB; 1A5H; X-ray; 2.90 A; A/B=311-562, C/D=298-304.
DR   PDB; 1BDA; X-ray; 3.35 A; A/B=298-562.
DR   PDB; 1PK2; NMR; -; A=209-298.
DR   PDB; 1PML; X-ray; 2.38 A; A/B/C=213-298.
DR   PDB; 1RTF; X-ray; 2.30 A; B=311-562.
DR   PDB; 1TPG; NMR; -; A=36-126.
DR   PDB; 1TPK; X-ray; 2.40 A; A/B/C=211-298.
DR   PDB; 1TPM; NMR; -; A=36-85.
DR   PDB; 1TPN; NMR; -; A=36-85.
DR   PDB; 5BRR; X-ray; 3.16 A; E=311-562.
DR   PDBsum; 1A5H; -.
DR   PDBsum; 1BDA; -.
DR   PDBsum; 1PK2; -.
DR   PDBsum; 1PML; -.
DR   PDBsum; 1RTF; -.
DR   PDBsum; 1TPG; -.
DR   PDBsum; 1TPK; -.
DR   PDBsum; 1TPM; -.
DR   PDBsum; 1TPN; -.
DR   PDBsum; 5BRR; -.
DR   ProteinModelPortal; P00750; -.
DR   SMR; P00750; -.
DR   BioGrid; 111343; 40.
DR   ComplexPortal; CPX-494; tPA-PAI-1 complex.
DR   ELM; P00750; -.
DR   IntAct; P00750; 2.
DR   MINT; P00750; -.
DR   STRING; 9606.ENSP00000220809; -.
DR   BindingDB; P00750; -.
DR   ChEMBL; CHEMBL1873; -.
DR   DrugBank; DB07684; 5-(DIMETHYLAMINO)-2-NAPHTHALENESULFONIC ACID.
DR   DrugBank; DB00513; Aminocaproic Acid.
DR   DrugBank; DB06404; C1 Esterase Inhibitor (Human).
DR   DrugBank; DB09228; C1 Esterase Inhibitor (Recombinant).
DR   DrugBank; DB01050; Ibuprofen.
DR   DrugBank; DB01088; Iloprost.
DR   DrugBank; DB00013; Urokinase.
DR   GuidetoPHARMACOLOGY; 2392; -.
DR   MEROPS; S01.232; -.
DR   GlyConnect; 503; -.
DR   GlyConnect; 504; -.
DR   GlyConnect; 603; -.
DR   iPTMnet; P00750; -.
DR   PhosphoSitePlus; P00750; -.
DR   UniCarbKB; P00750; -.
DR   BioMuta; PLAT; -.
DR   DMDM; 137119; -.
DR   EPD; P00750; -.
DR   jPOST; P00750; -.
DR   MaxQB; P00750; -.
DR   PaxDb; P00750; -.
DR   PeptideAtlas; P00750; -.
DR   PRIDE; P00750; -.
DR   ProteomicsDB; 51281; -.
DR   ProteomicsDB; 51282; -. [P00750-2]
DR   ProteomicsDB; 51283; -. [P00750-3]
DR   ProteomicsDB; 51284; -. [P00750-4]
DR   DNASU; 5327; -.
DR   Ensembl; ENST00000220809; ENSP00000220809; ENSG00000104368. [P00750-1]
DR   Ensembl; ENST00000352041; ENSP00000270188; ENSG00000104368. [P00750-3]
DR   Ensembl; ENST00000429089; ENSP00000392045; ENSG00000104368. [P00750-1]
DR   GeneID; 5327; -.
DR   KEGG; hsa:5327; -.
DR   UCSC; uc003xos.3; human. [P00750-1]
DR   CTD; 5327; -.
DR   DisGeNET; 5327; -.
DR   EuPathDB; HostDB:ENSG00000104368.17; -.
DR   GeneCards; PLAT; -.
DR   HGNC; HGNC:9051; PLAT.
DR   HPA; CAB009335; -.
DR   HPA; HPA003412; -.
DR   MalaCards; PLAT; -.
DR   MIM; 173370; gene.
DR   neXtProt; NX_P00750; -.
DR   OpenTargets; ENSG00000104368; -.
DR   Orphanet; 480528; Lethal hydranencephaly-diaphragmatic hernia syndrome.
DR   PharmGKB; PA33381; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000158930; -.
DR   HOVERGEN; HBG008633; -.
DR   InParanoid; P00750; -.
DR   KO; K01343; -.
DR   OMA; PLVCMKD; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; P00750; -.
DR   TreeFam; TF329901; -.
DR   BRENDA; 3.4.21.68; 2681.
DR   Reactome; R-HSA-186797; Signaling by PDGF.
DR   Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
DR   SIGNOR; P00750; -.
DR   ChiTaRS; PLAT; human.
DR   EvolutionaryTrace; P00750; -.
DR   GeneWiki; Tissue_plasminogen_activator; -.
DR   GenomeRNAi; 5327; -.
DR   PMAP-CutDB; P00750; -.
DR   PRO; PR:P00750; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   Bgee; ENSG00000104368; Expressed in 217 organ(s), highest expression level in metanephric glomerulus.
DR   ExpressionAtlas; P00750; baseline and differential.
DR   Genevisible; P00750; HS.
DR   GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR   GO; GO:0051219; F:phosphoprotein binding; IPI:AgBase.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:AgBase.
DR   GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR   GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
DR   GO; GO:0042730; P:fibrinolysis; TAS:Reactome.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IDA:BHF-UCL.
DR   GO; GO:0031639; P:plasminogen activation; IDA:UniProtKB.
DR   GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0014909; P:smooth muscle cell migration; IBA:GO_Central.
DR   GO; GO:0099183; P:trans-synaptic signaling by BDNF, modulating synaptic transmission; IEA:Ensembl.
DR   CDD; cd00061; FN1; 1.
DR   CDD; cd00108; KR; 2.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.20.10; -; 2.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000083; Fibronectin_type1.
DR   InterPro; IPR000001; Kringle.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR018056; Kringle_CS.
DR   InterPro; IPR038178; Kringle_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR026280; Tissue_plasm_act.
DR   InterPro; IPR034811; tPA.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR44617; PTHR44617; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00039; fn1; 1.
DR   Pfam; PF00051; Kringle; 2.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001145; Tissue_plasm_act; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00058; FN1; 1.
DR   SMART; SM00130; KR; 2.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57440; SSF57440; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01253; FN1_1; 1.
DR   PROSITE; PS51091; FN1_2; 1.
DR   PROSITE; PS00021; KRINGLE_1; 2.
DR   PROSITE; PS50070; KRINGLE_2; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Hydrolase; Kringle; Pharmaceutical;
KW   Plasminogen activation; Polymorphism; Protease; Reference proteome;
KW   Repeat; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     22       {ECO:0000269|Ref.20}.
FT   PROPEP       23     32       {ECO:0000269|PubMed:6682760}.
FT                                /FTId=PRO_0000028348.
FT   PROPEP       33     35       Removed by plasmin.
FT                                {ECO:0000269|PubMed:6433976}.
FT                                /FTId=PRO_0000028349.
FT   CHAIN        36    562       Tissue-type plasminogen activator.
FT                                /FTId=PRO_0000028350.
FT   CHAIN        36    310       Tissue-type plasminogen activator chain
FT                                A.
FT                                /FTId=PRO_0000028351.
FT   CHAIN       311    562       Tissue-type plasminogen activator chain
FT                                B.
FT                                /FTId=PRO_0000028352.
FT   DOMAIN       39     81       Fibronectin type-I. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00478}.
FT   DOMAIN       82    120       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      127    208       Kringle 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      215    296       Kringle 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      311    561       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   REGION       42     52       Important for binding to annexin A2.
FT   ACT_SITE    357    357       Charge relay system.
FT                                {ECO:0000305|PubMed:8613982}.
FT   ACT_SITE    406    406       Charge relay system.
FT                                {ECO:0000305|PubMed:8613982}.
FT   ACT_SITE    513    513       Charge relay system.
FT                                {ECO:0000305|PubMed:8613982}.
FT   SITE        102    102       Important for binding to LRP1.
FT   SITE        253    253       Not glycosylated.
FT   SITE        464    464       Important for single-chain activity.
FT   SITE        512    512       Important for single-chain activity.
FT   CARBOHYD     96     96       O-linked (Fuc) threonine.
FT                                {ECO:0000269|PubMed:1900431}.
FT                                /FTId=CAR_000029.
FT   CARBOHYD    152    152       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:2513186}.
FT   CARBOHYD    219    219       N-linked (GlcNAc...) asparagine; partial.
FT                                {ECO:0000269|PubMed:2513186}.
FT                                /FTId=CAR_000030.
FT   CARBOHYD    483    483       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:2513186}.
FT                                /FTId=CAR_000031.
FT   DISULFID     41     71       {ECO:0000269|PubMed:1645336}.
FT   DISULFID     69     78       {ECO:0000269|PubMed:1645336}.
FT   DISULFID     86     97       {ECO:0000269|PubMed:1645336}.
FT   DISULFID     91    108       {ECO:0000269|PubMed:1645336}.
FT   DISULFID    110    119       {ECO:0000269|PubMed:1645336}.
FT   DISULFID    127    208       {ECO:0000250}.
FT   DISULFID    148    190       {ECO:0000250}.
FT   DISULFID    179    203       {ECO:0000250}.
FT   DISULFID    215    296       {ECO:0000269|PubMed:1645336}.
FT   DISULFID    236    278       {ECO:0000269|PubMed:1645336}.
FT   DISULFID    267    291       {ECO:0000269|PubMed:1645336}.
FT   DISULFID    299    430       Interchain (between A and B chains).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076,
FT                                ECO:0000255|PROSITE-ProRule:PRU00121,
FT                                ECO:0000255|PROSITE-ProRule:PRU00274,
FT                                ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000269|PubMed:1645336}.
FT   DISULFID    342    358       {ECO:0000250}.
FT   DISULFID    350    419       {ECO:0000250}.
FT   DISULFID    444    519       {ECO:0000250}.
FT   DISULFID    476    492       {ECO:0000250}.
FT   DISULFID    509    537       {ECO:0000250}.
FT   VAR_SEQ       1     40       MDAMKRGLCCVLLLCGAVFVSPSQEIHARFRRGARSYQVI
FT                                -> MAS (in isoform 4).
FT                                {ECO:0000303|Ref.8}.
FT                                /FTId=VSP_028029.
FT   VAR_SEQ      39     85       VICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCH
FT                                SVPVKS -> G (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_015957.
FT   VAR_SEQ      79    208       Missing (in isoform 4).
FT                                {ECO:0000303|Ref.8}.
FT                                /FTId=VSP_028030.
FT   VAR_SEQ     269    291       NPDGDAKPWCHVLKNRRLTWEYC -> TGRSVSSPATASMR
FT                                PCPLSIRSG (in isoform 2).
FT                                {ECO:0000303|PubMed:2107528}.
FT                                /FTId=VSP_005411.
FT   VAR_SEQ     292    562       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:2107528}.
FT                                /FTId=VSP_005412.
FT   VARIANT      34     34       A -> D (in dbSNP:rs8178733).
FT                                {ECO:0000269|Ref.12}.
FT                                /FTId=VAR_020181.
FT   VARIANT     136    136       R -> S (in dbSNP:rs8178747).
FT                                {ECO:0000269|Ref.12}.
FT                                /FTId=VAR_038732.
FT   VARIANT     146    146       A -> T (in dbSNP:rs8178748).
FT                                {ECO:0000269|Ref.12}.
FT                                /FTId=VAR_038733.
FT   VARIANT     164    164       R -> W (in dbSNP:rs2020921).
FT                                {ECO:0000269|Ref.12}.
FT                                /FTId=VAR_011783.
FT   CONFLICT     93     93       N -> T (in Ref. 2; AAB59510).
FT                                {ECO:0000305}.
FT   CONFLICT    159    160       KP -> NA (in Ref. 7; CAA31489).
FT                                {ECO:0000305}.
FT   CONFLICT    247    247       K -> N (in Ref. 9; AAO34406).
FT                                {ECO:0000305}.
FT   CONFLICT    283    283       N -> S (in Ref. 14; AAH95403).
FT                                {ECO:0000305}.
FT   CONFLICT    333    334       RR -> EE (in Ref. 8; AAK11956).
FT                                {ECO:0000305}.
FT   CONFLICT    389    389       V -> C (in Ref. 8; AAK11956).
FT                                {ECO:0000305}.
FT   STRAND       41     43       {ECO:0000244|PDB:1TPM}.
FT   STRAND       44     46       {ECO:0000244|PDB:1TPG}.
FT   STRAND       48     50       {ECO:0000244|PDB:1TPM}.
FT   STRAND       55     59       {ECO:0000244|PDB:1TPG}.
FT   STRAND       61     64       {ECO:0000244|PDB:1TPG}.
FT   STRAND       66     70       {ECO:0000244|PDB:1TPG}.
FT   STRAND       72     74       {ECO:0000244|PDB:1TPG}.
FT   STRAND       77     81       {ECO:0000244|PDB:1TPM}.
FT   STRAND       83     85       {ECO:0000244|PDB:1TPG}.
FT   STRAND       96    104       {ECO:0000244|PDB:1TPG}.
FT   STRAND      106    109       {ECO:0000244|PDB:1TPG}.
FT   STRAND      115    118       {ECO:0000244|PDB:1TPG}.
FT   STRAND      221    223       {ECO:0000244|PDB:1PK2}.
FT   STRAND      229    233       {ECO:0000244|PDB:1PK2}.
FT   HELIX       242    244       {ECO:0000244|PDB:1PML}.
FT   STRAND      248    250       {ECO:0000244|PDB:1PML}.
FT   STRAND      251    253       {ECO:0000244|PDB:1PK2}.
FT   HELIX       256    259       {ECO:0000244|PDB:1PML}.
FT   STRAND      262    264       {ECO:0000244|PDB:1PML}.
FT   STRAND      277    282       {ECO:0000244|PDB:1PML}.
FT   STRAND      285    291       {ECO:0000244|PDB:1PML}.
FT   STRAND      309    311       {ECO:0000244|PDB:1BDA}.
FT   STRAND      312    316       {ECO:0000244|PDB:1RTF}.
FT   HELIX       319    321       {ECO:0000244|PDB:1RTF}.
FT   STRAND      325    331       {ECO:0000244|PDB:1RTF}.
FT   STRAND      338    346       {ECO:0000244|PDB:1RTF}.
FT   STRAND      348    354       {ECO:0000244|PDB:1RTF}.
FT   HELIX       356    359       {ECO:0000244|PDB:1RTF}.
FT   HELIX       365    367       {ECO:0000244|PDB:1RTF}.
FT   STRAND      368    373       {ECO:0000244|PDB:1RTF}.
FT   STRAND      375    379       {ECO:0000244|PDB:1RTF}.
FT   STRAND      385    394       {ECO:0000244|PDB:1RTF}.
FT   TURN        400    402       {ECO:0000244|PDB:1RTF}.
FT   STRAND      408    412       {ECO:0000244|PDB:1RTF}.
FT   STRAND      415    417       {ECO:0000244|PDB:1RTF}.
FT   STRAND      423    425       {ECO:0000244|PDB:5BRR}.
FT   STRAND      443    449       {ECO:0000244|PDB:1RTF}.
FT   STRAND      451    453       {ECO:0000244|PDB:1BDA}.
FT   STRAND      464    470       {ECO:0000244|PDB:1RTF}.
FT   HELIX       473    475       {ECO:0000244|PDB:1RTF}.
FT   TURN        478    483       {ECO:0000244|PDB:1RTF}.
FT   STRAND      490    494       {ECO:0000244|PDB:1RTF}.
FT   STRAND      499    501       {ECO:0000244|PDB:1A5H}.
FT   STRAND      516    521       {ECO:0000244|PDB:1RTF}.
FT   STRAND      524    533       {ECO:0000244|PDB:1RTF}.
FT   STRAND      535    538       {ECO:0000244|PDB:1RTF}.
FT   STRAND      544    548       {ECO:0000244|PDB:1RTF}.
FT   HELIX       549    552       {ECO:0000244|PDB:1RTF}.
FT   HELIX       553    559       {ECO:0000244|PDB:1RTF}.
SQ   SEQUENCE   562 AA;  62917 MW;  B7EC9B1A5E3FDC4D CRC64;
     MDAMKRGLCC VLLLCGAVFV SPSQEIHARF RRGARSYQVI CRDEKTQMIY QQHQSWLRPV
     LRSNRVEYCW CNSGRAQCHS VPVKSCSEPR CFNGGTCQQA LYFSDFVCQC PEGFAGKCCE
     IDTRATCYED QGISYRGTWS TAESGAECTN WNSSALAQKP YSGRRPDAIR LGLGNHNYCR
     NPDRDSKPWC YVFKAGKYSS EFCSTPACSE GNSDCYFGNG SAYRGTHSLT ESGASCLPWN
     SMILIGKVYT AQNPSAQALG LGKHNYCRNP DGDAKPWCHV LKNRRLTWEY CDVPSCSTCG
     LRQYSQPQFR IKGGLFADIA SHPWQAAIFA KHRRSPGERF LCGGILISSC WILSAAHCFQ
     ERFPPHHLTV ILGRTYRVVP GEEEQKFEVE KYIVHKEFDD DTYDNDIALL QLKSDSSRCA
     QESSVVRTVC LPPADLQLPD WTECELSGYG KHEALSPFYS ERLKEAHVRL YPSSRCTSQH
     LLNRTVTDNM LCAGDTRSGG PQANLHDACQ GDSGGPLVCL NDGRMTLVGI ISWGLGCGQK
     DVPGVYTKVT NYLDWIRDNM RP
//
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