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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   29-OCT-2014, entry version 171.
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   ChiTaRS; CTSL1; human.
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
FT   HELIX        26     35
FT   HELIX        44     67
FT   STRAND       72     75
FT   TURN         79     82
FT   HELIX        85     92
FT   STRAND      103    105
FT   HELIX       120    123
FT   STRAND      134    136
FT   HELIX       138    155
FT   HELIX       163    169
FT   TURN        171    174
FT   HELIX       177    179
FT   HELIX       183    193
FT   STRAND      196    198
FT   TURN        199    201
FT   HELIX       215    217
FT   STRAND      218    220
FT   STRAND      223    227
FT   HELIX       232    241
FT   STRAND      245    249
FT   HELIX       254    257
FT   STRAND      261    264
FT   STRAND      271    273
FT   STRAND      276    285
FT   STRAND      289    291
FT   STRAND      294    299
FT   STRAND      304    306
FT   STRAND      311    315
FT   STRAND      317    320
FT   HELIX       321    323
FT   TURN        324    326
FT   STRAND      329    332
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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