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Database: UniProt
Entry: P07711
LinkDB: P07711
Original site: P07711 
ID   CATL1_HUMAN             Reviewed;         333 AA.
AC   P07711; Q6IAV1; Q96QJ0;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 2.
DT   26-NOV-2014, entry version 172.
DE   RecName: Full=Cathepsin L1;
DE            EC=3.4.22.15;
DE   AltName: Full=Cathepsin L;
DE   AltName: Full=Major excreted protein;
DE            Short=MEP;
DE   Contains:
DE     RecName: Full=Cathepsin L1 heavy chain;
DE   Contains:
DE     RecName: Full=Cathepsin L1 light chain;
DE   Flags: Precursor;
GN   Name=CTSL; Synonyms=CTSL1;
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].
RX   PubMed=3421948;
RA   Gal S., Gottesman M.M.;
RT   "Isolation and sequence of a cDNA for human pro-(cathepsin L).";
RL   Biochem. J. 253:303-306(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2835398; DOI=10.1172/JCI113497;
RA   Joseph L.J., Chang L.C., Stamenkovich D., Sukhatme V.P.;
RT   "Complete nucleotide and deduced amino acid sequences of human and
RT   murine preprocathepsin L. An abundant transcript induced by
RT   transformation of fibroblasts.";
RL   J. Clin. Invest. 81:1621-1629(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon endothelium;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   [7]
RP   PROTEIN SEQUENCE OF 114-288 AND 292-333.
RX   PubMed=3342889; DOI=10.1016/0014-5793(88)80028-0;
RA   Ritonja A., Popovic T., Kotnik M., Machleidt W., Turk V.;
RT   "Amino acid sequences of the human kidney cathepsins H and L.";
RL   FEBS Lett. 228:341-345(1988).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 113-154.
RX   PubMed=3550705; DOI=10.1093/nar/15.7.3186;
RA   Joseph L.J., Lapid S., Sukhatme V.P.;
RT   "The major ras induced protein in NIH3T3 cells is cathepsin L.";
RL   Nucleic Acids Res. 15:3186-3186(1987).
RN   [9]
RP   PROTEIN SEQUENCE OF 114-154 AND 292-333.
RX   PubMed=3545185;
RA   Mason R.W., Walker J.E., Northrop F.D.;
RT   "The N-terminal amino acid sequences of the heavy and light chains of
RT   human cathepsin L. Relationship to a cDNA clone for a major cysteine
RT   proteinase from a mouse macrophage cell line.";
RL   Biochem. J. 240:373-377(1986).
RN   [10]
RP   GLYCOSYLATION AT ASN-221.
RX   PubMed=12754519; DOI=10.1038/nbt827;
RA   Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT   "Identification and quantification of N-linked glycoproteins using
RT   hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL   Nat. Biotechnol. 21:660-666(2003).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-333.
RX   PubMed=8896443;
RA   Coulombe R., Grochulski P., Sivaraman J., Menard R., Mort J.S.,
RA   Cygler M.;
RT   "Structure of human procathepsin L reveals the molecular basis of
RT   inhibition by the prosegment.";
RL   EMBO J. 15:5492-5503(1996).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 114-333.
RX   PubMed=9141479; DOI=10.1016/S0014-5793(97)00216-0;
RA   Fujishima A., Imai Y., Nomura T., Fujisawa Y., Yamamoto Y.,
RA   Sugarawa T.;
RT   "The crystal structure of human cathepsin L complexed with E-64.";
RL   FEBS Lett. 407:47-50(1997).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 18-333.
RA   Cygler M., Coulombe R.;
RL   Submitted (AUG-1999) to the PDB data bank.
CC   -!- FUNCTION: Important for the overall degradation of proteins in
CC       lysosomes.
CC   -!- CATALYTIC ACTIVITY: Specificity close to that of papain. As
CC       compared to cathepsin B, cathepsin L exhibits higher activity
CC       toward protein substrates, but has little activity on Z-Arg-Arg-
CC       NHMec, and no peptidyl-dipeptidase activity.
CC   -!- SUBUNIT: Dimer of a heavy and a light chain linked by disulfide
CC       bonds.
CC   -!- INTERACTION:
CC       G5EFH4:srp-6 (xeno); NbExp=2; IntAct=EBI-1220160, EBI-1549936;
CC   -!- SUBCELLULAR LOCATION: Lysosome.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
CC       ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/CTSL1ID40208ch9q21.html";
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DR   EMBL; X12451; CAA30981.1; -; mRNA.
DR   EMBL; M20496; AAA66974.1; -; mRNA.
DR   EMBL; CR457053; CAG33334.1; -; mRNA.
DR   EMBL; BX537395; CAD97637.1; -; mRNA.
DR   EMBL; AL160279; CAI16308.1; -; Genomic_DNA.
DR   EMBL; BC012612; AAH12612.1; -; mRNA.
DR   EMBL; X05256; CAA28877.1; -; mRNA.
DR   CCDS; CCDS6675.1; -.
DR   PIR; S01002; KHHUL.
DR   RefSeq; NP_001244900.1; NM_001257971.1.
DR   RefSeq; NP_001244901.1; NM_001257972.1.
DR   RefSeq; NP_001903.1; NM_001912.4.
DR   RefSeq; NP_666023.1; NM_145918.2.
DR   RefSeq; XP_005251773.1; XM_005251716.1.
DR   UniGene; Hs.731507; -.
DR   PDB; 1CJL; X-ray; 2.20 A; A=22-333.
DR   PDB; 1CS8; X-ray; 1.80 A; A=19-333.
DR   PDB; 1ICF; X-ray; 2.00 A; A/C=114-288, B/D=292-333.
DR   PDB; 1MHW; X-ray; 1.90 A; A/B=114-288, C/D=292-333.
DR   PDB; 2NQD; X-ray; 1.75 A; B=113-333.
DR   PDB; 2VHS; X-ray; 1.50 A; A/B/C/D=114-285, A/B/C/D=294-333.
DR   PDB; 2XU1; X-ray; 1.45 A; A/B/C/D=114-333.
DR   PDB; 2XU3; X-ray; 0.90 A; A=114-333.
DR   PDB; 2XU4; X-ray; 1.12 A; A=114-333.
DR   PDB; 2XU5; X-ray; 1.60 A; A=114-333.
DR   PDB; 2YJ2; X-ray; 1.15 A; A=114-333.
DR   PDB; 2YJ8; X-ray; 1.30 A; A=114-333.
DR   PDB; 2YJ9; X-ray; 1.35 A; A=114-333.
DR   PDB; 2YJB; X-ray; 1.40 A; A=114-333.
DR   PDB; 2YJC; X-ray; 1.14 A; A=114-333.
DR   PDB; 3BC3; X-ray; 2.20 A; A/B=114-333.
DR   PDB; 3H89; X-ray; 2.50 A; A/B/C/D/E/F=114-333.
DR   PDB; 3H8B; X-ray; 1.80 A; A/B/C/D/E/F=114-333.
DR   PDB; 3H8C; X-ray; 2.50 A; A/B=114-333.
DR   PDB; 3HHA; X-ray; 1.27 A; A/B/C/D=114-333.
DR   PDB; 3HWN; X-ray; 2.33 A; A/B/C/D=76-333.
DR   PDB; 3IV2; X-ray; 2.20 A; A/B=114-333.
DR   PDB; 3K24; X-ray; 2.50 A; A/B=114-333.
DR   PDB; 3KSE; X-ray; 1.71 A; A/B/C=114-333.
DR   PDB; 3OF8; X-ray; 2.20 A; A=113-333.
DR   PDB; 3OF9; X-ray; 1.76 A; A=113-333.
DR   PDB; 4AXL; X-ray; 1.92 A; A=114-333.
DR   PDB; 4AXM; X-ray; 2.80 A; A/B/F/I/L/O=114-333.
DR   PDBsum; 1CJL; -.
DR   PDBsum; 1CS8; -.
DR   PDBsum; 1ICF; -.
DR   PDBsum; 1MHW; -.
DR   PDBsum; 2NQD; -.
DR   PDBsum; 2VHS; -.
DR   PDBsum; 2XU1; -.
DR   PDBsum; 2XU3; -.
DR   PDBsum; 2XU4; -.
DR   PDBsum; 2XU5; -.
DR   PDBsum; 2YJ2; -.
DR   PDBsum; 2YJ8; -.
DR   PDBsum; 2YJ9; -.
DR   PDBsum; 2YJB; -.
DR   PDBsum; 2YJC; -.
DR   PDBsum; 3BC3; -.
DR   PDBsum; 3H89; -.
DR   PDBsum; 3H8B; -.
DR   PDBsum; 3H8C; -.
DR   PDBsum; 3HHA; -.
DR   PDBsum; 3HWN; -.
DR   PDBsum; 3IV2; -.
DR   PDBsum; 3K24; -.
DR   PDBsum; 3KSE; -.
DR   PDBsum; 3OF8; -.
DR   PDBsum; 3OF9; -.
DR   PDBsum; 4AXL; -.
DR   PDBsum; 4AXM; -.
DR   ProteinModelPortal; P07711; -.
DR   SMR; P07711; 18-333.
DR   BioGrid; 107894; 17.
DR   IntAct; P07711; 13.
DR   MINT; MINT-3005764; -.
DR   STRING; 9606.ENSP00000345344; -.
DR   BindingDB; P07711; -.
DR   ChEMBL; CHEMBL2111380; -.
DR   GuidetoPHARMACOLOGY; 2351; -.
DR   MEROPS; C01.032; -.
DR   PhosphoSite; P07711; -.
DR   DMDM; 115741; -.
DR   MaxQB; P07711; -.
DR   PaxDb; P07711; -.
DR   PeptideAtlas; P07711; -.
DR   PRIDE; P07711; -.
DR   DNASU; 1514; -.
DR   Ensembl; ENST00000340342; ENSP00000365061; ENSG00000135047.
DR   Ensembl; ENST00000343150; ENSP00000345344; ENSG00000135047.
DR   GeneID; 1514; -.
DR   KEGG; hsa:1514; -.
DR   UCSC; uc004aph.3; human.
DR   CTD; 1514; -.
DR   GeneCards; GC09P090352; -.
DR   H-InvDB; HIX0058839; -.
DR   H-InvDB; HIX0170314; -.
DR   HGNC; HGNC:2537; CTSL.
DR   HPA; CAB000459; -.
DR   MIM; 116880; gene.
DR   neXtProt; NX_P07711; -.
DR   PharmGKB; PA162382890; -.
DR   eggNOG; COG4870; -.
DR   GeneTree; ENSGT00760000118871; -.
DR   HOGENOM; HOG000230774; -.
DR   HOVERGEN; HBG011513; -.
DR   InParanoid; P07711; -.
DR   KO; K01365; -.
DR   OMA; NPEYSVA; -.
DR   OrthoDB; EOG786H3P; -.
DR   PhylomeDB; P07711; -.
DR   TreeFam; TF313739; -.
DR   BRENDA; 3.4.22.15; 2681.
DR   Reactome; REACT_111168; Endosomal/Vacuolar pathway.
DR   Reactome; REACT_118572; Degradation of the extracellular matrix.
DR   Reactome; REACT_118632; Trafficking and processing of endosomal TLR.
DR   Reactome; REACT_121399; MHC class II antigen presentation.
DR   Reactome; REACT_150180; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; REACT_150401; Collagen degradation.
DR   EvolutionaryTrace; P07711; -.
DR   GeneWiki; Cathepsin_L1; -.
DR   GenomeRNAi; 1514; -.
DR   NextBio; 6271; -.
DR   PMAP-CutDB; P07711; -.
DR   PRO; PR:P07711; -.
DR   Bgee; P07711; -.
DR   CleanEx; HS_CTSL1; -.
DR   ExpressionAtlas; P07711; baseline and differential.
DR   Genevestigator; P07711; -.
DR   GO; GO:0036021; C:endolysosome lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR   GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR   GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; TAS:BHF-UCL.
DR   GO; GO:0005518; F:collagen binding; IDA:BHF-UCL.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
DR   GO; GO:0001968; F:fibronectin binding; IPI:BHF-UCL.
DR   GO; GO:0042393; F:histone binding; IDA:BHF-UCL.
DR   GO; GO:0043394; F:proteoglycan binding; IPI:BHF-UCL.
DR   GO; GO:0002250; P:adaptive immune response; IEP:UniProtKB.
DR   GO; GO:0019882; P:antigen processing and presentation; TAS:UniProtKB.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR   GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEP:UniProtKB.
DR   GO; GO:0030574; P:collagen catabolic process; IDA:BHF-UCL.
DR   GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0071888; P:macrophage apoptotic process; NAS:BHF-UCL.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:BHF-UCL.
DR   GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; PTHR12411; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW   Reference proteome; Signal; Thiol protease; Zymogen.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   PROPEP       18    113       Activation peptide.
FT                                /FTId=PRO_0000026244.
FT   CHAIN       114    288       Cathepsin L1 heavy chain.
FT                                /FTId=PRO_0000026245.
FT   PROPEP      289    291
FT                                /FTId=PRO_0000026246.
FT   CHAIN       292    333       Cathepsin L1 light chain.
FT                                /FTId=PRO_0000026247.
FT   ACT_SITE    138    138
FT   ACT_SITE    276    276
FT   ACT_SITE    300    300
FT   CARBOHYD    221    221       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:12754519,
FT                                ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:19159218}.
FT   DISULFID    135    178
FT   DISULFID    169    211
FT   DISULFID    269    322       Interchain (between heavy and light
FT                                chains).
FT   CONFLICT     56     56       M -> V (in Ref. 6; AAH12612).
FT                                {ECO:0000305}.
FT   CONFLICT    268    268       D -> N (in Ref. 7; AA sequence).
FT                                {ECO:0000305}.
FT   HELIX        23     25       {ECO:0000244|PDB:1CS8}.
FT   HELIX        26     35       {ECO:0000244|PDB:1CS8}.
FT   HELIX        44     67       {ECO:0000244|PDB:1CS8}.
FT   STRAND       72     75       {ECO:0000244|PDB:1CS8}.
FT   TURN         79     82       {ECO:0000244|PDB:1CS8}.
FT   HELIX        85     92       {ECO:0000244|PDB:1CS8}.
FT   STRAND      103    105       {ECO:0000244|PDB:1CJL}.
FT   HELIX       120    123       {ECO:0000244|PDB:2XU3}.
FT   STRAND      134    136       {ECO:0000244|PDB:2XU3}.
FT   HELIX       138    155       {ECO:0000244|PDB:2XU3}.
FT   HELIX       163    169       {ECO:0000244|PDB:2XU3}.
FT   TURN        171    174       {ECO:0000244|PDB:2XU3}.
FT   HELIX       177    179       {ECO:0000244|PDB:2XU4}.
FT   HELIX       183    193       {ECO:0000244|PDB:2XU3}.
FT   STRAND      196    198       {ECO:0000244|PDB:2XU3}.
FT   TURN        199    201       {ECO:0000244|PDB:2XU3}.
FT   HELIX       215    217       {ECO:0000244|PDB:2XU3}.
FT   STRAND      218    220       {ECO:0000244|PDB:2XU3}.
FT   STRAND      223    227       {ECO:0000244|PDB:2XU3}.
FT   HELIX       232    241       {ECO:0000244|PDB:2XU3}.
FT   STRAND      245    249       {ECO:0000244|PDB:2XU3}.
FT   HELIX       254    257       {ECO:0000244|PDB:2XU3}.
FT   STRAND      261    264       {ECO:0000244|PDB:2XU3}.
FT   STRAND      271    273       {ECO:0000244|PDB:4AXL}.
FT   STRAND      276    285       {ECO:0000244|PDB:2XU3}.
FT   STRAND      289    291       {ECO:0000244|PDB:2XU3}.
FT   STRAND      294    299       {ECO:0000244|PDB:2XU3}.
FT   STRAND      304    306       {ECO:0000244|PDB:3KSE}.
FT   STRAND      311    315       {ECO:0000244|PDB:2XU3}.
FT   STRAND      317    320       {ECO:0000244|PDB:2XU3}.
FT   HELIX       321    323       {ECO:0000244|PDB:2XU3}.
FT   TURN        324    326       {ECO:0000244|PDB:2XU3}.
FT   STRAND      329    332       {ECO:0000244|PDB:2XU3}.
SQ   SEQUENCE   333 AA;  37564 MW;  8CD17D00EF859D85 CRC64;
     MNPTLILAAF CLGIASATLT FDHSLEAQWT KWKAMHNRLY GMNEEGWRRA VWEKNMKMIE
     LHNQEYREGK HSFTMAMNAF GDMTSEEFRQ VMNGFQNRKP RKGKVFQEPL FYEAPRSVDW
     REKGYVTPVK NQGQCGSCWA FSATGALEGQ MFRKTGRLIS LSEQNLVDCS GPQGNEGCNG
     GLMDYAFQYV QDNGGLDSEE SYPYEATEES CKYNPKYSVA NDTGFVDIPK QEKALMKAVA
     TVGPISVAID AGHESFLFYK EGIYFEPDCS SEDMDHGVLV VGYGFESTES DNNKYWLVKN
     SWGEEWGMGG YVKMAKDRRN HCGIASAASY PTV
//
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