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 07-OCT-2020, entry version 212. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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 surfactant RT 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 encoded RT 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 ALA-180. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA 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; ALA-180; RP 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., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., 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 project: RT 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 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., Cai G.-Z., RA Crouch E.; RT "Human surfactant protein D: SP-D contains a C-type lectin carbohydrate RT 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., Fernandez-Real J.M.; RT "The lung innate immune gene surfactant protein-D is expressed in adipose RT 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 three RT 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., Rosenblatt R.L., RA DiMaio J.M., Kinch L.N., Grishin N.V., Garcia C.K.; RT "Genetic defects in surfactant protein A2 are associated with pulmonary RT 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 compounds CC such as bacterial lipopolysaccharides, oligosaccharides and fatty acids CC and modulates leukocyte action in immune response. May participate in CC the extracellular reorganization or turnover of pulmonary surfactant. CC Binds strongly maltose residues and to a lesser extent other alpha- CC glucosyl moieties. {ECO:0000269|PubMed:23478426}. CC -!- SUBUNIT: Oligomeric complex of 4 set of homotrimers. CC -!- INTERACTION: CC P35247; 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, GXPG, CC is most likely to be 4-hydroxy as this fits the requirement for 4- CC 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 signaling CC activity with macrophages. {ECO:0000250}. CC -!- MISCELLANEOUS: Pulmonary surfactant consists of 90% lipid and 10% CC protein. There are 4 surfactant-associated proteins: 2 collagenous, CC carbohydrate-binding glycoproteins (SP-A and SP-D) and 2 small CC 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 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 PDB; 5OXR; X-ray; 1.75 A; A/B/C=201-375. DR PDB; 5OXS; X-ray; 1.65 A; A/B/C=201-375. 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 PDBsum; 5OXR; -. DR PDBsum; 5OXS; -. DR SMR; P35247; -. DR BioGRID; 112339; 6. DR IntAct; P35247; 4. DR STRING; 9606.ENSP00000361366; -. DR ChEMBL; CHEMBL2176857; -. DR DrugBank; DB02379; Beta-D-Glucose. DR UniLectin; P35247; -. DR GlyGen; P35247; 1 site. DR iPTMnet; P35247; -. DR PhosphoSitePlus; P35247; -. DR BioMuta; SFTPD; -. DR DMDM; 317373510; -. DR EPD; P35247; -. DR MassIVE; P35247; -. DR PaxDb; P35247; -. DR PeptideAtlas; P35247; -. DR PRIDE; P35247; -. DR ProteomicsDB; 55012; -. DR Antibodypedia; 3886; 485 antibodies. 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 HGNC; HGNC:10803; SFTPD. DR HPA; ENSG00000133661; Tissue enriched (lung). DR MIM; 178635; gene. DR neXtProt; NX_P35247; -. DR OpenTargets; ENSG00000133661; -. DR PharmGKB; PA35715; -. DR eggNOG; KOG4297; Eukaryota. DR GeneTree; ENSGT00940000155748; -. DR HOGENOM; CLU_049894_3_0_1; -. DR InParanoid; P35247; -. DR KO; K10068; -. DR OMA; ANTCTLV; -. DR OrthoDB; 1341167at2759; -. DR PhylomeDB; P35247; -. DR TreeFam; TF330481; -. DR PathwayCommons; P35247; -. 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-5683826; Surfactant metabolism. DR Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand. 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 SIGNOR; P35247; -. DR BioGRID-ORCS; 6441; 2 hits in 868 CRISPR screens. DR EvolutionaryTrace; P35247; -. DR GeneWiki; Surfactant_protein_D; -. DR GenomeRNAi; 6441; -. DR Pharos; P35247; Tbio. DR PRO; PR:P35247; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P35247; protein. DR Bgee; ENSG00000133661; Expressed in visceral pleura and 135 other tissues. 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; IBA:GO_Central. DR GO; GO:0005764; C:lysosome; TAS:UniProtKB. DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central. DR GO; GO:0005791; C:rough endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0030246; F:carbohydrate binding; TAS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. 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:0032703; P:negative regulation of interleukin-2 production; TAS:UniProtKB. DR GO; GO:0042130; P:negative regulation of T cell proliferation; TAS:UniProtKB. DR GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central. 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 by respiratory system; 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 DisProt; DP01868; -. DR Gene3D; 3.10.100.10; -; 1. DR InterPro; IPR001304; C-type_lectin-like. DR InterPro; IPR016186; C-type_lectin-like/link_sf. 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; Direct protein sequencing; KW Disulfide bond; Extracellular matrix; Gaseous exchange; Glycoprotein; KW Hydroxylation; Immunity; Innate immunity; Lectin; Polymorphism; KW Reference proteome; Repeat; S-nitrosylation; Secreted; Signal; KW Surface film. FT SIGNAL 1..20 FT /evidence="ECO:0000250" FT CHAIN 21..375 FT /note="Pulmonary surfactant-associated protein D" FT /id="PRO_0000017465" FT DOMAIN 46..222 FT /note="Collagen-like" FT DOMAIN 260..375 FT /note="C-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT COILED 223..252 FT /evidence="ECO:0000255" FT MOD_RES 35 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:P35248" FT MOD_RES 40 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:P35248" FT MOD_RES 78 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT MOD_RES 87 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250" FT MOD_RES 96 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT MOD_RES 99 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250" FT MOD_RES 171 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT MOD_RES 177 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT CARBOHYD 90 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 281..373 FT DISULFID 351..365 FT VARIANT 31 FT /note="M -> T (in dbSNP:rs721917)" FT /evidence="ECO:0000269|PubMed:1339284, FT ECO:0000269|PubMed:19100526, ECO:0000269|Ref.3, FT ECO:0000269|Ref.4" FT /id="VAR_020937" FT VARIANT 123 FT /note="L -> V (in dbSNP:rs17878336)" FT /evidence="ECO:0000269|PubMed:19100526, ECO:0000269|Ref.4" FT /id="VAR_020938" FT VARIANT 180 FT /note="T -> A (in dbSNP:rs2243639)" FT /evidence="ECO:0000269|PubMed:1339284, FT ECO:0000269|PubMed:19100526, ECO:0000269|Ref.3, FT ECO:0000269|Ref.4" FT /id="VAR_020939" FT VARIANT 290 FT /note="S -> T (in dbSNP:rs3088308)" FT /evidence="ECO:0000269|PubMed:19100526, ECO:0000269|Ref.4" FT /id="VAR_020940" FT VARIANT 309 FT /note="E -> K (in dbSNP:rs4469829)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_020941" FT CONFLICT 22 FT /note="E -> G (in Ref. 6; AAH22318)" FT /evidence="ECO:0000305" FT CONFLICT 59 FT /note="P -> F (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 122 FT /note="P -> A (in Ref. 2; AAB59450)" FT /evidence="ECO:0000305" FT CONFLICT 240 FT /note="H -> P (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 341 FT /note="E -> K (in Ref. 6; AAH22318)" FT /evidence="ECO:0000305" FT CONFLICT 369 FT /note="R -> S (in Ref. 3; CAG46746)" FT /evidence="ECO:0000305" FT HELIX 226..253 FT /evidence="ECO:0000244|PDB:1PWB" FT TURN 254..256 FT /evidence="ECO:0000244|PDB:1PWB" FT STRAND 257..260 FT /evidence="ECO:0000244|PDB:1PWB" FT STRAND 263..273 FT /evidence="ECO:0000244|PDB:1PWB" FT HELIX 274..283 FT /evidence="ECO:0000244|PDB:1PWB" FT STRAND 286..288 FT /evidence="ECO:0000244|PDB:1PWB" FT HELIX 294..307 FT /evidence="ECO:0000244|PDB:1PWB" FT STRAND 311..316 FT /evidence="ECO:0000244|PDB:2RIA" FT STRAND 318..320 FT /evidence="ECO:0000244|PDB:1PWB" FT STRAND 323..325 FT /evidence="ECO:0000244|PDB:2GGX" FT HELIX 345..347 FT /evidence="ECO:0000244|PDB:1PWB" FT STRAND 351..354 FT /evidence="ECO:0000244|PDB:1PWB" FT STRAND 360..363 FT /evidence="ECO:0000244|PDB:1PWB" FT STRAND 367..375 FT /evidence="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 //