ID SFTPD_HUMAN Reviewed; 375 AA. AC P35247; Q5T0M3; Q6FH08; Q86YK9; Q8TCD8; Q9UCJ2; Q9UCJ3; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 27-SEP-2017, entry version 189. DE RecName: Full=Pulmonary surfactant-associated protein D; DE Short=PSP-D; DE Short=SP-D; DE AltName: Full=Collectin-7; DE AltName: Full=Lung surfactant protein D; DE Flags: Precursor; GN Name=SFTPD; Synonyms=COLEC7, PSPD, SFTP4; 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], PROTEIN SEQUENCE OF 214-243, AND VARIANTS RP THR-31 AND ALA-180. RC TISSUE=Amniotic fluid, and Lung; RX PubMed=1339284; DOI=10.1042/bj2840795; RA Lu J., Willis A.C., Reid K.B.M.; RT "Purification, characterization and cDNA cloning of human lung RT surfactant protein D."; RL Biochem. J. 284:795-802(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Placenta; RX PubMed=8428971; RA Crouch E., Rust K., Veile R., Donis-Keller H., Grosso L.; RT "Genomic organization of human surfactant protein D (SP-D). SP-D is RT encoded on chromosome 10q22.2-23.1."; RL J. Biol. Chem. 268:2976-2983(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-31 AND RP ALA-180. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., RA Korn B., Zuo D., Hu Y., LaBaer J.; 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 [GENOMIC DNA], AND VARIANTS THR-31; VAL-123; RP ALA-180; THR-290 AND LYS-309. RG SeattleSNPs variation discovery resource; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 46-72 AND 223-260. RX PubMed=8424457; RA Crouch E., Persson A., Chang D.; RT "Accumulation of surfactant protein D in human pulmonary alveolar RT proteinosis."; RL Am. J. Pathol. 142:241-248(1993). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-375, AND PARTIAL PROTEIN RP SEQUENCE. RC TISSUE=Lung; RX PubMed=1898081; DOI=10.1016/0003-9861(91)90597-C; RA Rust K., Grosso L., Zhang V., Chang D., Persson A., Longmore W., RA Cai G.-Z., Crouch E.; RT "Human surfactant protein D: SP-D contains a C-type lectin RT carbohydrate recognition domain."; RL Arch. Biochem. Biophys. 290:116-126(1991). RN [9] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=23478426; DOI=10.1038/ijo.2013.23; RA Ortega F.J., Pueyo N., Moreno-Navarrete J.M., Sabater M., RA Rodriguez-Hermosa J.I., Ricart W., Tinahones F.J., RA Fernandez-Real J.M.; RT "The lung innate immune gene surfactant protein-D is expressed in RT adipose tissue and linked to obesity status."; RL Int. J. Obes. Relat. Metab. Disord. 37:1532-1538(2013). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=10368295; DOI=10.1016/S0969-2126(99)80036-7; RA Hakansson K., Lim N.K., Hoppe H.-J., Reid K.B.M.; RT "Crystal structure of the trimeric alpha-helical coiled-coil and the RT three lectin domains of human lung surfactant protein D."; RL Structure 7:255-264(1999). RN [11] RP VARIANTS THR-31; VAL-123; ALA-180 AND THR-290. RX PubMed=19100526; DOI=10.1016/j.ajhg.2008.11.010; RA Wang Y., Kuan P.J., Xing C., Cronkhite J.T., Torres F., RA Rosenblatt R.L., DiMaio J.M., Kinch L.N., Grishin N.V., Garcia C.K.; RT "Genetic defects in surfactant protein A2 are associated with RT pulmonary fibrosis and lung cancer."; RL Am. J. Hum. Genet. 84:52-59(2009). CC -!- FUNCTION: Contributes to the lung's defense against inhaled CC microorganisms, organic antigens and toxins. Interacts with CC compounds such as bacterial lipopolysaccharides, oligosaccharides CC and fatty acids and modulates leukocyte action in immune response. CC May participate in the extracellular reorganization or turnover of CC pulmonary surfactant. Binds strongly maltose residues and to a CC lesser extent other alpha-glucosyl moieties. CC {ECO:0000269|PubMed:23478426}. CC -!- SUBUNIT: Oligomeric complex of 4 set of homotrimers. CC -!- INTERACTION: CC O00322:UPK1A; NbExp=3; IntAct=EBI-11316157, EBI-14031976; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. Secreted, extracellular space, surface film. CC -!- TISSUE SPECIFICITY: Expressed in lung, brain, pancreas and adipose CC tissue (mainly mature adipocytes). {ECO:0000269|PubMed:23478426}. CC -!- PTM: The N-terminus is blocked. CC -!- PTM: Hydroxylation on proline residues within the sequence motif, CC GXPG, is most likely to be 4-hydroxy as this fits the requirement CC for 4-hydroxylation in vertebrates. {ECO:0000250}. CC -!- PTM: S-nitrosylation at Cys-35 and Cys-40 alters the quaternary CC structure which results in a pro-inflammatory chemoattractive CC signaling activity with macrophages. {ECO:0000250}. CC -!- MISCELLANEOUS: Pulmonary surfactant consists of 90% lipid and 10% CC protein. There are 4 surfactant-associated proteins: 2 CC collagenous, carbohydrate-binding glycoproteins (SP-A and SP-D) CC and 2 small hydrophobic proteins (SP-B and SP-C). CC -!- SIMILARITY: Belongs to the SFTPD family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/sftpd/"; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=Pulmonary surfactant protein SP-D; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_228"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X65018; CAA46152.1; -; mRNA. DR EMBL; L05485; AAB59450.1; -; Genomic_DNA. DR EMBL; L05483; AAB59450.1; JOINED; Genomic_DNA. DR EMBL; L05484; AAB59450.1; JOINED; Genomic_DNA. DR EMBL; CR541948; CAG46746.1; -; mRNA. DR EMBL; AY216721; AAO22991.1; -; Genomic_DNA. DR EMBL; AL512662; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC022318; AAH22318.1; -; mRNA. DR CCDS; CCDS7362.1; -. DR PIR; A45225; A45225. DR RefSeq; NP_003010.4; NM_003019.4. DR RefSeq; XP_011538389.1; XM_011540087.1. DR UniGene; Hs.253495; -. DR PDB; 1B08; X-ray; 2.30 A; A/B/C=218-375. DR PDB; 1M7L; NMR; -; A/B/C=220-257. DR PDB; 1PW9; X-ray; 1.60 A; A/B/C=199-375. DR PDB; 1PWB; X-ray; 1.40 A; A/B/C=199-375. DR PDB; 2GGU; X-ray; 1.90 A; A/B/C=223-375. DR PDB; 2GGX; X-ray; 1.90 A; A/B/C=223-375. DR PDB; 2ORJ; X-ray; 1.80 A; A/B/C=223-375. DR PDB; 2ORK; X-ray; 1.89 A; A/B/C=223-375. DR PDB; 2OS9; X-ray; 1.70 A; A/B/C=223-375. DR PDB; 2RIA; X-ray; 1.80 A; A/B/C=223-375. DR PDB; 2RIB; X-ray; 1.80 A; A/B/C=223-375. DR PDB; 2RIC; X-ray; 1.80 A; A/B/C=223-375. DR PDB; 2RID; X-ray; 1.80 A; A/B/C=223-375. DR PDB; 2RIE; X-ray; 1.60 A; A/B/C=223-375. DR PDB; 3DBZ; X-ray; 1.80 A; A/B/C=223-375. DR PDB; 3G81; X-ray; 1.80 A; A/B/C=223-375. DR PDB; 3G83; X-ray; 1.90 A; A/B/C=223-375. DR PDB; 3G84; X-ray; 2.30 A; A/B/C=223-375. DR PDB; 3IKN; X-ray; 1.60 A; A/B/C=199-375. DR PDB; 3IKP; X-ray; 1.75 A; A/B/C=199-375. DR PDB; 3IKQ; X-ray; 2.25 A; A/B/C=199-375. DR PDB; 3IKR; X-ray; 1.65 A; A/B/C=199-375. DR PDB; 4E52; X-ray; 1.70 A; A/B/C=201-375. DR PDB; 4M17; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=229-375. DR PDB; 4M18; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L=229-375. DR PDBsum; 1B08; -. DR PDBsum; 1M7L; -. DR PDBsum; 1PW9; -. DR PDBsum; 1PWB; -. DR PDBsum; 2GGU; -. DR PDBsum; 2GGX; -. DR PDBsum; 2ORJ; -. DR PDBsum; 2ORK; -. DR PDBsum; 2OS9; -. DR PDBsum; 2RIA; -. DR PDBsum; 2RIB; -. DR PDBsum; 2RIC; -. DR PDBsum; 2RID; -. DR PDBsum; 2RIE; -. DR PDBsum; 3DBZ; -. DR PDBsum; 3G81; -. DR PDBsum; 3G83; -. DR PDBsum; 3G84; -. DR PDBsum; 3IKN; -. DR PDBsum; 3IKP; -. DR PDBsum; 3IKQ; -. DR PDBsum; 3IKR; -. DR PDBsum; 4E52; -. DR PDBsum; 4M17; -. DR PDBsum; 4M18; -. DR ProteinModelPortal; P35247; -. DR SMR; P35247; -. DR BioGrid; 112339; 4. DR IntAct; P35247; 3. DR STRING; 9606.ENSP00000361366; -. DR ChEMBL; CHEMBL2176857; -. DR DrugBank; DB02379; Beta-D-Glucose. DR iPTMnet; P35247; -. DR PhosphoSitePlus; P35247; -. DR BioMuta; SFTPD; -. DR DMDM; 317373510; -. DR PaxDb; P35247; -. DR PeptideAtlas; P35247; -. DR PRIDE; P35247; -. DR DNASU; 6441; -. DR Ensembl; ENST00000372292; ENSP00000361366; ENSG00000133661. DR GeneID; 6441; -. DR KEGG; hsa:6441; -. DR UCSC; uc001kbh.4; human. DR CTD; 6441; -. DR DisGeNET; 6441; -. DR EuPathDB; HostDB:ENSG00000133661.15; -. DR GeneCards; SFTPD; -. DR H-InvDB; HIX0008974; -. DR HGNC; HGNC:10803; SFTPD. DR HPA; CAB004578; -. DR HPA; HPA044582; -. DR HPA; HPA056768; -. DR MIM; 178635; gene. DR neXtProt; NX_P35247; -. DR OpenTargets; ENSG00000133661; -. DR PharmGKB; PA35715; -. DR eggNOG; ENOG410IS48; Eukaryota. DR eggNOG; ENOG4110NRD; LUCA. DR GeneTree; ENSGT00700000104102; -. DR HOVERGEN; HBG108270; -. DR InParanoid; P35247; -. DR KO; K10068; -. DR OMA; AENCVEI; -. DR OrthoDB; EOG091G0MYV; -. DR PhylomeDB; P35247; -. DR TreeFam; TF330481; -. DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade. DR Reactome; R-HSA-168179; Toll Like Receptor TLR1:TLR2 Cascade. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-HSA-391160; Signal regulatory protein family interactions. DR Reactome; R-HSA-5683678; Defective ABCA3 causes pulmonary surfactant metabolism dysfunction type 3 (SMDP3). DR Reactome; R-HSA-5683826; Surfactant metabolism. DR Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand. DR Reactome; R-HSA-5687868; Defective SFTPA2 causes idiopathic pulmonary fibrosis (IPF). DR Reactome; R-HSA-5688849; Defective CSF2RB causes pulmonary surfactant metabolism dysfunction 5 (SMDP5). DR Reactome; R-HSA-5688890; Defective CSF2RA causes pulmonary surfactant metabolism dysfunction 4 (SMDP4). DR EvolutionaryTrace; P35247; -. DR GeneWiki; Surfactant_protein_D; -. DR GenomeRNAi; 6441; -. DR PRO; PR:P35247; -. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; ENSG00000133661; -. DR CleanEx; HS_SFTPD; -. DR ExpressionAtlas; P35247; baseline and differential. DR Genevisible; P35247; HS. DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; TAS:Reactome. DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW. DR GO; GO:0030139; C:endocytic vesicle; TAS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR GO; GO:0042599; C:lamellar body; TAS:Reactome. DR GO; GO:0005764; C:lysosome; TAS:UniProtKB. DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; TAS:UniProtKB. DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:0042742; P:defense response to bacterium; TAS:UniProtKB. DR GO; GO:0043152; P:induction of bacterial agglutination; IMP:AgBase. DR GO; GO:0045087; P:innate immune response; TAS:UniProtKB. DR GO; GO:0048286; P:lung alveolus development; IMP:UniProtKB. DR GO; GO:0048246; P:macrophage chemotaxis; TAS:UniProtKB. DR GO; GO:0052405; P:negative regulation by host of symbiont molecular function; IDA:AgBase. DR GO; GO:0045085; P:negative regulation of interleukin-2 biosynthetic process; TAS:UniProtKB. DR GO; GO:0042130; P:negative regulation of T cell proliferation; TAS:UniProtKB. DR GO; GO:0050766; P:positive regulation of phagocytosis; TAS:UniProtKB. DR GO; GO:0072593; P:reactive oxygen species metabolic process; TAS:UniProtKB. DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:UniProtKB. DR GO; GO:1905226; P:regulation of adhesion of symbiont to host epithelial cell; IDA:AgBase. DR GO; GO:0001817; P:regulation of cytokine production; NAS:UniProtKB. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0007585; P:respiratory gaseous exchange; IEA:UniProtKB-KW. DR GO; GO:0043129; P:surfactant homeostasis; IMP:UniProtKB. DR GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome. DR CDD; cd03591; CLECT_collectin_like; 1. DR Gene3D; 3.10.100.10; -; 1. DR InterPro; IPR001304; C-type_lectin-like. DR InterPro; IPR016186; C-type_lectin-like/link. DR InterPro; IPR018378; C-type_lectin_CS. DR InterPro; IPR008160; Collagen. DR InterPro; IPR033990; Collectin_CTLD. DR InterPro; IPR016187; CTDL_fold. DR InterPro; IPR015097; Surfac_D-trimer. DR Pfam; PF01391; Collagen; 2. DR Pfam; PF00059; Lectin_C; 1. DR Pfam; PF09006; Surfac_D-trimer; 1. DR SMART; SM00034; CLECT; 1. DR SUPFAM; SSF56436; SSF56436; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Coiled coil; Collagen; Complete proteome; KW Direct protein sequencing; Disulfide bond; Extracellular matrix; KW Gaseous exchange; Glycoprotein; Hydroxylation; Immunity; KW Innate immunity; Lectin; Polymorphism; Reference proteome; Repeat; KW S-nitrosylation; Secreted; Signal; Surface film. FT SIGNAL 1 20 {ECO:0000250}. FT CHAIN 21 375 Pulmonary surfactant-associated protein FT D. FT /FTId=PRO_0000017465. FT DOMAIN 46 222 Collagen-like. FT DOMAIN 260 375 C-type lectin. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT COILED 223 252 {ECO:0000255}. FT MOD_RES 35 35 S-nitrosocysteine. FT {ECO:0000250|UniProtKB:P35248}. FT MOD_RES 40 40 S-nitrosocysteine. FT {ECO:0000250|UniProtKB:P35248}. FT MOD_RES 78 78 4-hydroxyproline. {ECO:0000250}. FT MOD_RES 87 87 5-hydroxylysine. {ECO:0000250}. FT MOD_RES 96 96 4-hydroxyproline. {ECO:0000250}. FT MOD_RES 99 99 5-hydroxylysine. {ECO:0000250}. FT MOD_RES 171 171 4-hydroxyproline. {ECO:0000250}. FT MOD_RES 177 177 4-hydroxyproline. {ECO:0000250}. FT CARBOHYD 90 90 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 281 373 FT DISULFID 351 365 FT VARIANT 31 31 M -> T (in dbSNP:rs721917). FT {ECO:0000269|PubMed:1339284, FT ECO:0000269|PubMed:19100526, FT ECO:0000269|Ref.3, ECO:0000269|Ref.4}. FT /FTId=VAR_020937. FT VARIANT 123 123 L -> V (in dbSNP:rs17878336). FT {ECO:0000269|PubMed:19100526, FT ECO:0000269|Ref.4}. FT /FTId=VAR_020938. FT VARIANT 180 180 T -> A (in dbSNP:rs2243639). FT {ECO:0000269|PubMed:1339284, FT ECO:0000269|PubMed:19100526, FT ECO:0000269|Ref.3, ECO:0000269|Ref.4}. FT /FTId=VAR_020939. FT VARIANT 290 290 S -> T (in dbSNP:rs3088308). FT {ECO:0000269|PubMed:19100526, FT ECO:0000269|Ref.4}. FT /FTId=VAR_020940. FT VARIANT 309 309 E -> K (in dbSNP:rs4469829). FT {ECO:0000269|Ref.4}. FT /FTId=VAR_020941. FT CONFLICT 22 22 E -> G (in Ref. 6; AAH22318). FT {ECO:0000305}. FT CONFLICT 59 59 P -> F (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 122 122 P -> A (in Ref. 2; AAB59450). FT {ECO:0000305}. FT CONFLICT 240 240 H -> P (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 341 341 E -> K (in Ref. 6; AAH22318). FT {ECO:0000305}. FT CONFLICT 369 369 R -> S (in Ref. 3; CAG46746). FT {ECO:0000305}. FT HELIX 226 253 {ECO:0000244|PDB:1PWB}. FT TURN 254 256 {ECO:0000244|PDB:1PWB}. FT STRAND 257 260 {ECO:0000244|PDB:1PWB}. FT STRAND 263 273 {ECO:0000244|PDB:1PWB}. FT HELIX 274 283 {ECO:0000244|PDB:1PWB}. FT STRAND 286 288 {ECO:0000244|PDB:1PWB}. FT HELIX 294 307 {ECO:0000244|PDB:1PWB}. FT STRAND 311 316 {ECO:0000244|PDB:2RIA}. FT STRAND 318 320 {ECO:0000244|PDB:1PWB}. FT STRAND 323 325 {ECO:0000244|PDB:2GGX}. FT HELIX 345 347 {ECO:0000244|PDB:1PWB}. FT STRAND 351 354 {ECO:0000244|PDB:1PWB}. FT STRAND 360 363 {ECO:0000244|PDB:1PWB}. FT STRAND 367 375 {ECO:0000244|PDB:1PWB}. SQ 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 //