GENTAUR Molecular Products.

 SFTPD_HUMAN             Reviewed;         375 AA.
 P35247; Q5T0M3; Q6FH08; Q86YK9; Q8TCD8; Q9UCJ2; Q9UCJ3;
 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
 11-JAN-2011, sequence version 3.
 12-SEP-2018, entry version 196.
 RecName: Full=Pulmonary surfactant-associated protein D;
          Short=PSP-D;
          Short=SP-D;
 AltName: Full=Collectin-7;
 AltName: Full=Lung surfactant protein D;
 Flags: Precursor;
 Name=SFTPD; Synonyms=COLEC7, PSPD, SFTP4;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 214-243, AND VARIANTS
 THR-31 AND ALA-180.
 TISSUE=Amniotic fluid, and Lung;
 PubMed=1339284; DOI=10.1042/bj2840795;
 Lu J., Willis A.C., Reid K.B.M.;
 "Purification, characterization and cDNA cloning of human lung
 surfactant protein D.";
 Biochem. J. 284:795-802(1992).
 [2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 TISSUE=Placenta;
 PubMed=8428971;
 Crouch E., Rust K., Veile R., Donis-Keller H., Grosso L.;
 "Genomic organization of human surfactant protein D (SP-D). SP-D is
 encoded on chromosome 10q22.2-23.1.";
 J. Biol. Chem. 268:2976-2983(1993).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-31 AND
 ALA-180.
 Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
 Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
 Korn B., Zuo D., Hu Y., LaBaer J.;
 "Cloning of human full open reading frames in Gateway(TM) system entry
 vector (pDONR201).";
 Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
 [4]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-31; VAL-123;
 ALA-180; THR-290 AND LYS-309.
 SeattleSNPs variation discovery resource;
 Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=15164054; DOI=10.1038/nature02462;
 Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
 Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
 Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
 Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
 Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
 Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
 Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
 Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
 Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
 Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
 Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
 Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
 Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
 Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
 Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
 Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
 Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
 Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
 Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
 Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
 Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
 Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
 Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
 Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
 Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
 Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
 "The DNA sequence and comparative analysis of human chromosome 10.";
 Nature 429:375-381(2004).
 [6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 TISSUE=Lung;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [7]
 PROTEIN SEQUENCE OF 46-72 AND 223-260.
 PubMed=8424457;
 Crouch E., Persson A., Chang D.;
 "Accumulation of surfactant protein D in human pulmonary alveolar
 proteinosis.";
 Am. J. Pathol. 142:241-248(1993).
 [8]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-375, AND PARTIAL PROTEIN
 SEQUENCE.
 TISSUE=Lung;
 PubMed=1898081; DOI=10.1016/0003-9861(91)90597-C;
 Rust K., Grosso L., Zhang V., Chang D., Persson A., Longmore W.,
 Cai G.-Z., Crouch E.;
 "Human surfactant protein D: SP-D contains a C-type lectin
 carbohydrate recognition domain.";
 Arch. Biochem. Biophys. 290:116-126(1991).
 [9]
 FUNCTION, AND TISSUE SPECIFICITY.
 PubMed=23478426; DOI=10.1038/ijo.2013.23;
 Ortega F.J., Pueyo N., Moreno-Navarrete J.M., Sabater M.,
 Rodriguez-Hermosa J.I., Ricart W., Tinahones F.J.,
 Fernandez-Real J.M.;
 "The lung innate immune gene surfactant protein-D is expressed in
 adipose tissue and linked to obesity status.";
 Int. J. Obes. Relat. Metab. Disord. 37:1532-1538(2013).
 [10]
 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
 PubMed=10368295; DOI=10.1016/S0969-2126(99)80036-7;
 Hakansson K., Lim N.K., Hoppe H.-J., Reid K.B.M.;
 "Crystal structure of the trimeric alpha-helical coiled-coil and the
 three lectin domains of human lung surfactant protein D.";
 Structure 7:255-264(1999).
 [11]
 VARIANTS THR-31; VAL-123; ALA-180 AND THR-290.
 PubMed=19100526; DOI=10.1016/j.ajhg.2008.11.010;
 Wang Y., Kuan P.J., Xing C., Cronkhite J.T., Torres F.,
 Rosenblatt R.L., DiMaio J.M., Kinch L.N., Grishin N.V., Garcia C.K.;
 "Genetic defects in surfactant protein A2 are associated with
 pulmonary fibrosis and lung cancer.";
 Am. J. Hum. Genet. 84:52-59(2009).
 -!- FUNCTION: Contributes to the lung's defense against inhaled
     microorganisms, organic antigens and toxins. Interacts with
     compounds such as bacterial lipopolysaccharides, oligosaccharides
     and fatty acids and modulates leukocyte action in immune response.
     May participate in the extracellular reorganization or turnover of
     pulmonary surfactant. Binds strongly maltose residues and to a
     lesser extent other alpha-glucosyl moieties.
     {ECO:0000269|PubMed:23478426}.
 -!- SUBUNIT: Oligomeric complex of 4 set of homotrimers.
 -!- INTERACTION:
     O00322:UPK1A; NbExp=3; IntAct=EBI-11316157, EBI-14031976;
 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
     matrix. Secreted, extracellular space, surface film.
 -!- TISSUE SPECIFICITY: Expressed in lung, brain, pancreas and adipose
     tissue (mainly mature adipocytes). {ECO:0000269|PubMed:23478426}.
 -!- PTM: The N-terminus is blocked.
 -!- PTM: Hydroxylation on proline residues within the sequence motif,
     GXPG, is most likely to be 4-hydroxy as this fits the requirement
     for 4-hydroxylation in vertebrates. {ECO:0000250}.
 -!- PTM: S-nitrosylation at Cys-35 and Cys-40 alters the quaternary
     structure which results in a pro-inflammatory chemoattractive
     signaling activity with macrophages. {ECO:0000250}.
 -!- MISCELLANEOUS: Pulmonary surfactant consists of 90% lipid and 10%
     protein. There are 4 surfactant-associated proteins: 2
     collagenous, carbohydrate-binding glycoproteins (SP-A and SP-D)
     and 2 small hydrophobic proteins (SP-B and SP-C).
 -!- SIMILARITY: Belongs to the SFTPD family. {ECO:0000305}.
 -!- WEB RESOURCE: Name=SeattleSNPs;
     URL="http://pga.gs.washington.edu/data/sftpd/";
 -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
     Note=Pulmonary surfactant protein SP-D;
     URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_228";
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 EMBL; X65018; CAA46152.1; -; mRNA.
 EMBL; L05485; AAB59450.1; -; Genomic_DNA.
 EMBL; L05483; AAB59450.1; JOINED; Genomic_DNA.
 EMBL; L05484; AAB59450.1; JOINED; Genomic_DNA.
 EMBL; CR541948; CAG46746.1; -; mRNA.
 EMBL; AY216721; AAO22991.1; -; Genomic_DNA.
 EMBL; AL512662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; BC022318; AAH22318.1; -; mRNA.
 CCDS; CCDS7362.1; -.
 PIR; A45225; A45225.
 RefSeq; NP_003010.4; NM_003019.4.
 RefSeq; XP_011538389.1; XM_011540087.1.
 UniGene; Hs.253495; -.
 PDB; 1B08; X-ray; 2.30 A; A/B/C=218-375.
 PDB; 1M7L; NMR; -; A/B/C=220-257.
 PDB; 1PW9; X-ray; 1.60 A; A/B/C=199-375.
 PDB; 1PWB; X-ray; 1.40 A; A/B/C=199-375.
 PDB; 2GGU; X-ray; 1.90 A; A/B/C=223-375.
 PDB; 2GGX; X-ray; 1.90 A; A/B/C=223-375.
 PDB; 2ORJ; X-ray; 1.80 A; A/B/C=223-375.
 PDB; 2ORK; X-ray; 1.89 A; A/B/C=223-375.
 PDB; 2OS9; X-ray; 1.70 A; A/B/C=223-375.
 PDB; 2RIA; X-ray; 1.80 A; A/B/C=223-375.
 PDB; 2RIB; X-ray; 1.80 A; A/B/C=223-375.
 PDB; 2RIC; X-ray; 1.80 A; A/B/C=223-375.
 PDB; 2RID; X-ray; 1.80 A; A/B/C=223-375.
 PDB; 2RIE; X-ray; 1.60 A; A/B/C=223-375.
 PDB; 3DBZ; X-ray; 1.80 A; A/B/C=223-375.
 PDB; 3G81; X-ray; 1.80 A; A/B/C=223-375.
 PDB; 3G83; X-ray; 1.90 A; A/B/C=223-375.
 PDB; 3G84; X-ray; 2.30 A; A/B/C=223-375.
 PDB; 3IKN; X-ray; 1.60 A; A/B/C=199-375.
 PDB; 3IKP; X-ray; 1.75 A; A/B/C=199-375.
 PDB; 3IKQ; X-ray; 2.25 A; A/B/C=199-375.
 PDB; 3IKR; X-ray; 1.65 A; A/B/C=199-375.
 PDB; 4E52; X-ray; 1.70 A; A/B/C=201-375.
 PDB; 4M17; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=229-375.
 PDB; 4M18; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L=229-375.
 PDB; 5OXR; X-ray; 1.75 A; A/B/C=201-375.
 PDB; 5OXS; X-ray; 1.65 A; A/B/C=201-375.
 PDBsum; 1B08; -.
 PDBsum; 1M7L; -.
 PDBsum; 1PW9; -.
 PDBsum; 1PWB; -.
 PDBsum; 2GGU; -.
 PDBsum; 2GGX; -.
 PDBsum; 2ORJ; -.
 PDBsum; 2ORK; -.
 PDBsum; 2OS9; -.
 PDBsum; 2RIA; -.
 PDBsum; 2RIB; -.
 PDBsum; 2RIC; -.
 PDBsum; 2RID; -.
 PDBsum; 2RIE; -.
 PDBsum; 3DBZ; -.
 PDBsum; 3G81; -.
 PDBsum; 3G83; -.
 PDBsum; 3G84; -.
 PDBsum; 3IKN; -.
 PDBsum; 3IKP; -.
 PDBsum; 3IKQ; -.
 PDBsum; 3IKR; -.
 PDBsum; 4E52; -.
 PDBsum; 4M17; -.
 PDBsum; 4M18; -.
 PDBsum; 5OXR; -.
 PDBsum; 5OXS; -.
 ProteinModelPortal; P35247; -.
 SMR; P35247; -.
 BioGrid; 112339; 4.
 IntAct; P35247; 3.
 STRING; 9606.ENSP00000361366; -.
 ChEMBL; CHEMBL2176857; -.
 DrugBank; DB02379; Beta-D-Glucose.
 UniLectin; P35247; -.
 iPTMnet; P35247; -.
 PhosphoSitePlus; P35247; -.
 BioMuta; SFTPD; -.
 DMDM; 317373510; -.
 EPD; P35247; -.
 PaxDb; P35247; -.
 PeptideAtlas; P35247; -.
 PRIDE; P35247; -.
 ProteomicsDB; 55012; -.
 DNASU; 6441; -.
 Ensembl; ENST00000372292; ENSP00000361366; ENSG00000133661.
 GeneID; 6441; -.
 KEGG; hsa:6441; -.
 UCSC; uc001kbh.4; human.
 CTD; 6441; -.
 DisGeNET; 6441; -.
 EuPathDB; HostDB:ENSG00000133661.15; -.
 GeneCards; SFTPD; -.
 H-InvDB; HIX0008974; -.
 HGNC; HGNC:10803; SFTPD.
 HPA; CAB004578; -.
 HPA; HPA044582; -.
 HPA; HPA056768; -.
 MIM; 178635; gene.
 neXtProt; NX_P35247; -.
 OpenTargets; ENSG00000133661; -.
 PharmGKB; PA35715; -.
 eggNOG; ENOG410IS48; Eukaryota.
 eggNOG; ENOG4110NRD; LUCA.
 GeneTree; ENSGT00700000104102; -.
 HOVERGEN; HBG108270; -.
 InParanoid; P35247; -.
 KO; K10068; -.
 OMA; AENCVEI; -.
 OrthoDB; EOG091G0MYV; -.
 PhylomeDB; P35247; -.
 TreeFam; TF330481; -.
 Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
 Reactome; R-HSA-168179; Toll Like Receptor TLR1:TLR2 Cascade.
 Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
 Reactome; R-HSA-391160; Signal regulatory protein family interactions.
 Reactome; R-HSA-5683826; Surfactant metabolism.
 Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
 Reactome; R-HSA-5687868; Defective SFTPA2 causes idiopathic pulmonary fibrosis (IPF).
 Reactome; R-HSA-5688849; Defective CSF2RB causes pulmonary surfactant metabolism dysfunction 5 (SMDP5).
 Reactome; R-HSA-5688890; Defective CSF2RA causes pulmonary surfactant metabolism dysfunction 4 (SMDP4).
 SIGNOR; P35247; -.
 EvolutionaryTrace; P35247; -.
 GeneWiki; Surfactant_protein_D; -.
 GenomeRNAi; 6441; -.
 PRO; PR:P35247; -.
 Proteomes; UP000005640; Chromosome 10.
 Bgee; ENSG00000133661; Expressed in 116 organ(s), highest expression level in visceral pleura.
 CleanEx; HS_SFTPD; -.
 ExpressionAtlas; P35247; baseline and differential.
 Genevisible; P35247; HS.
 GO; GO:0045334; C:clathrin-coated endocytic vesicle; TAS:Reactome.
 GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
 GO; GO:0030139; C:endocytic vesicle; TAS:UniProtKB.
 GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
 GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
 GO; GO:0005764; C:lysosome; TAS:UniProtKB.
 GO; GO:0030246; F:carbohydrate binding; TAS:UniProtKB.
 GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
 GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
 GO; GO:0042742; P:defense response to bacterium; TAS:UniProtKB.
 GO; GO:0043152; P:induction of bacterial agglutination; IMP:AgBase.
 GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
 GO; GO:0048286; P:lung alveolus development; IMP:UniProtKB.
 GO; GO:0048246; P:macrophage chemotaxis; TAS:UniProtKB.
 GO; GO:0052405; P:negative regulation by host of symbiont molecular function; IDA:AgBase.
 GO; GO:0045085; P:negative regulation of interleukin-2 biosynthetic process; TAS:UniProtKB.
 GO; GO:0042130; P:negative regulation of T cell proliferation; TAS:UniProtKB.
 GO; GO:0050766; P:positive regulation of phagocytosis; TAS:UniProtKB.
 GO; GO:0072593; P:reactive oxygen species metabolic process; TAS:UniProtKB.
 GO; GO:0006898; P:receptor-mediated endocytosis; TAS:UniProtKB.
 GO; GO:1905226; P:regulation of adhesion of symbiont to host epithelial cell; IDA:AgBase.
 GO; GO:0001817; P:regulation of cytokine production; NAS:UniProtKB.
 GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
 GO; GO:0007585; P:respiratory gaseous exchange; IEA:UniProtKB-KW.
 GO; GO:0043129; P:surfactant homeostasis; IMP:UniProtKB.
 GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
 CDD; cd03591; CLECT_collectin_like; 1.
 Gene3D; 3.10.100.10; -; 1.
 InterPro; IPR001304; C-type_lectin-like.
 InterPro; IPR016186; C-type_lectin-like/link_sf.
 InterPro; IPR018378; C-type_lectin_CS.
 InterPro; IPR008160; Collagen.
 InterPro; IPR033990; Collectin_CTLD.
 InterPro; IPR016187; CTDL_fold.
 InterPro; IPR015097; Surfac_D-trimer.
 Pfam; PF01391; Collagen; 2.
 Pfam; PF00059; Lectin_C; 1.
 Pfam; PF09006; Surfac_D-trimer; 1.
 SMART; SM00034; CLECT; 1.
 SUPFAM; SSF56436; SSF56436; 1.
 PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
 PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
 1: Evidence at protein level;
 3D-structure; Calcium; Coiled coil; Collagen; Complete proteome;
 Direct protein sequencing; Disulfide bond; Extracellular matrix;
 Gaseous exchange; Glycoprotein; Hydroxylation; Immunity;
 Innate immunity; Lectin; Polymorphism; Reference proteome; Repeat;
 S-nitrosylation; Secreted; Signal; Surface film.
 SIGNAL        1     20       {ECO:0000250}.
 CHAIN        21    375       Pulmonary surfactant-associated protein
                              D.
                              /FTId=PRO_0000017465.
 DOMAIN       46    222       Collagen-like.
 DOMAIN      260    375       C-type lectin. {ECO:0000255|PROSITE-
                              ProRule:PRU00040}.
 COILED      223    252       {ECO:0000255}.
 MOD_RES      35     35       S-nitrosocysteine.
                              {ECO:0000250|UniProtKB:P35248}.
 MOD_RES      40     40       S-nitrosocysteine.
                              {ECO:0000250|UniProtKB:P35248}.
 MOD_RES      78     78       4-hydroxyproline. {ECO:0000250}.
 MOD_RES      87     87       5-hydroxylysine. {ECO:0000250}.
 MOD_RES      96     96       4-hydroxyproline. {ECO:0000250}.
 MOD_RES      99     99       5-hydroxylysine. {ECO:0000250}.
 MOD_RES     171    171       4-hydroxyproline. {ECO:0000250}.
 MOD_RES     177    177       4-hydroxyproline. {ECO:0000250}.
 CARBOHYD     90     90       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 DISULFID    281    373
 DISULFID    351    365
 VARIANT      31     31       M -> T (in dbSNP:rs721917).
                              {ECO:0000269|PubMed:1339284,
                              ECO:0000269|PubMed:19100526,
                              ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
                              /FTId=VAR_020937.
 VARIANT     123    123       L -> V (in dbSNP:rs17878336).
                              {ECO:0000269|PubMed:19100526,
                              ECO:0000269|Ref.4}.
                              /FTId=VAR_020938.
 VARIANT     180    180       T -> A (in dbSNP:rs2243639).
                              {ECO:0000269|PubMed:1339284,
                              ECO:0000269|PubMed:19100526,
                              ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
                              /FTId=VAR_020939.
 VARIANT     290    290       S -> T (in dbSNP:rs3088308).
                              {ECO:0000269|PubMed:19100526,
                              ECO:0000269|Ref.4}.
                              /FTId=VAR_020940.
 VARIANT     309    309       E -> K (in dbSNP:rs4469829).
                              {ECO:0000269|Ref.4}.
                              /FTId=VAR_020941.
 CONFLICT     22     22       E -> G (in Ref. 6; AAH22318).
                              {ECO:0000305}.
 CONFLICT     59     59       P -> F (in Ref. 7; AA sequence).
                              {ECO:0000305}.
 CONFLICT    122    122       P -> A (in Ref. 2; AAB59450).
                              {ECO:0000305}.
 CONFLICT    240    240       H -> P (in Ref. 7; AA sequence).
                              {ECO:0000305}.
 CONFLICT    341    341       E -> K (in Ref. 6; AAH22318).
                              {ECO:0000305}.
 CONFLICT    369    369       R -> S (in Ref. 3; CAG46746).
                              {ECO:0000305}.
 HELIX       226    253       {ECO:0000244|PDB:1PWB}.
 TURN        254    256       {ECO:0000244|PDB:1PWB}.
 STRAND      257    260       {ECO:0000244|PDB:1PWB}.
 STRAND      263    273       {ECO:0000244|PDB:1PWB}.
 HELIX       274    283       {ECO:0000244|PDB:1PWB}.
 STRAND      286    288       {ECO:0000244|PDB:1PWB}.
 HELIX       294    307       {ECO:0000244|PDB:1PWB}.
 STRAND      311    316       {ECO:0000244|PDB:2RIA}.
 STRAND      318    320       {ECO:0000244|PDB:1PWB}.
 STRAND      323    325       {ECO:0000244|PDB:2GGX}.
 HELIX       345    347       {ECO:0000244|PDB:1PWB}.
 STRAND      351    354       {ECO:0000244|PDB:1PWB}.
 STRAND      360    363       {ECO:0000244|PDB:1PWB}.
 STRAND      367    375       {ECO:0000244|PDB:1PWB}.
 SEQUENCE   375 AA;  37728 MW;  298917699FC40F6A CRC64;
 MLLFLLSALV LLTQPLGYLE AEMKTYSHRT MPSACTLVMC SSVESGLPGR DGRDGREGPR
 GEKGDPGLPG AAGQAGMPGQ AGPVGPKGDN GSVGEPGPKG DTGPSGPPGP PGVPGPAGRE
 GPLGKQGNIG PQGKPGPKGE AGPKGEVGAP GMQGSAGARG LAGPKGERGV PGERGVPGNT
 GAAGSAGAMG PQGSPGARGP PGLKGDKGIP GDKGAKGESG LPDVASLRQQ VEALQGQVQH
 LQAAFSQYKK VELFPNGQSV GEKIFKTAGF VKPFTEAQLL CTQAGGQLAS PRSAAENAAL
 QQLVVAKNEA AFLSMTDSKT EGKFTYPTGE SLVYSNWAPG EPNDDGGSED CVEIFTNGKW
 NDRACGEKRL VVCEF

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