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Pulmonary surfactant-associated protein D (PSP-D) (SP-D) (Collectin-7) (Lung surfactant protein D)
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.
28-FEB-2018, entry version 192.
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.
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; -.
ProteinModelPortal; P35247; -.
SMR; P35247; -.
BioGrid; 112339; 4.
IntAct; P35247; 3.
STRING; 9606.ENSP00000361366; -.
ChEMBL; CHEMBL2176857; -.
DrugBank; DB02379; Beta-D-Glucose.
iPTMnet; P35247; -.
PhosphoSitePlus; P35247; -.
BioMuta; SFTPD; -.
DMDM; 317373510; -.
PaxDb; P35247; -.
PeptideAtlas; P35247; -.
PRIDE; P35247; -.
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-5683678; Defective ABCA3 causes pulmonary surfactant metabolism dysfunction type 3 (SMDP3).
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; -.
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:0042599; C:lamellar body; TAS:Reactome.
GO; GO:0005764; C:lysosome; TAS:UniProtKB.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
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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547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com
Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123
GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel: 0208-080893 Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62 SWIFT RABONL2U
GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur
ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF
GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX 058 710 33 48
poland@gentaur.com | Gentaur
Other countries
Österreich +43720880899
Canada Montreal +15149077481
Ceská republika Praha +420246019719
Danmark +4569918806
Finland Helsset +358942419041
Magyarország Budapest +3619980547
Ireland Dublin+35316526556
Luxembourg+35220880274
Norge Oslo+4721031366
Sverige Stockholm+46852503438
Schweiz Züri+41435006251
US New York+17185132983
GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo
Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur
Pathways :
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair
Related Genes :
[SFTPB SFTP3] Pulmonary surfactant-associated protein B (SP-B) (18 kDa pulmonary-surfactant protein) (6 kDa protein) (Pulmonary surfactant-associated proteolipid SPL(Phe))
[SFTPA1 COLEC4 PSAP SFTP1 SFTPA SFTPA1B] Pulmonary surfactant-associated protein A1 (PSP-A) (PSPA) (SP-A) (SP-A1) (35 kDa pulmonary surfactant-associated protein) (Alveolar proteinosis protein) (Collectin-4)
[SFTPC SFTP2] Pulmonary surfactant-associated protein C (SP-C) (Pulmonary surfactant-associated proteolipid SPL(Val)) (SP5)
[SFTPA2 COLEC5 PSAP SFTP1 SFTPA SFTPA2B] Pulmonary surfactant-associated protein A2 (PSP-A) (PSPA) (SP-A) (SP-A2) (35 kDa pulmonary surfactant-associated protein) (Alveolar proteinosis protein) (Collectin-5)
[Sftpb Sftp3] Pulmonary surfactant-associated protein B (SP-B) (Pulmonary surfactant-associated proteolipid SPL(Phe))
[Sftpc Sftp2] Pulmonary surfactant-associated protein C (SP-C) (Pulmonary surfactant-associated proteolipid SPL(Val))
[SFTPD COLEC7 PSPD SFTP4] Pulmonary surfactant-associated protein D (PSP-D) (SP-D) (Collectin-7) (Lung surfactant protein D)
[Sftpd Sftp4] Pulmonary surfactant-associated protein D (PSP-D) (SP-D) (Lung surfactant protein D)
[Sftpa1 Sftp-1 Sftp1 Sftpa] Pulmonary surfactant-associated protein A (PSAP) (PSP-A) (SP-A)
[Sftpd Sftp4] Pulmonary surfactant-associated protein D (PSP-D) (SP-D) (CP4) (Lung surfactant protein D)
[SFTPB SFTP3] Pulmonary surfactant-associated protein B (SP-B) (6 kDa protein) (Pulmonary surfactant protein 18) (SP 18) (Pulmonary surfactant-associated proteolipid SPL(Phe)) (Fragment)
[SFTPB SFTP3] Pulmonary surfactant-associated protein B (SP-B) (6 kDa protein) (Pulmonary surfactant-associated proteolipid SPL(Phe))
[Sftpb Sftp3] Pulmonary surfactant-associated protein B (SP-B) (Pulmonary surfactant-associated proteolipid SPL(Phe))
[pol] Gag-Pro-Pol polyprotein [Cleaved into: Matrix protein p10; Phosphorylated protein; p12; Capsid protein p27; Nucleocapsid protein-dUTPase (NC-dUTPase) (EC 3.6.1.23); Protease 17 kDa (EC 3.4.23.-); Protease 13 kDa (EC 3.4.23.-); G-patch peptide; Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[pro] Gag-Pro polyprotein [Cleaved into: Matrix protein p10; Phosphorylated protein; p12; Capsid protein p27; Nucleocapsid protein-dUTPase (NC-dUTPase) (EC 3.6.1.23); Protease 17 kDa (EC 3.4.23.-); Protease 13 kDa (EC 3.4.23.-); G-patch peptide]
[gag] Gag polyprotein (Core polyprotein) [Cleaved into: Matrix protein p10; Phosphorylated protein pp24; p12; Capsid protein p27; Nucleocapsid protein p14; p4]
[CCL18 AMAC1 DCCK1 MIP4 PARC SCYA18] C-C motif chemokine 18 (Alternative macrophage activation-associated CC chemokine 1) (AMAC-1) (CC chemokine PARC) (Dendritic cell chemokine 1) (DC-CK1) (Macrophage inflammatory protein 4) (MIP-4) (Pulmonary and activation-regulated chemokine) (Small-inducible cytokine A18) [Cleaved into: CCL18(1-68); CCL18(3-69); CCL18(4-69)]
[SFTPD SFTP4] Pulmonary surfactant-associated protein D (PSP-D) (SP-D) (Lung surfactant protein D)
[SFTPB SFTP3] Pulmonary surfactant-associated protein B (SP-B) (8 kDa protein) (Pulmonary surfactant-associated proteolipid SPL(Phe))
[env] Envelope glycoprotein (Env polyprotein) [Cleaved into: Surface protein (SU) (Glycoprotein 52) (gp52); Transmembrane protein (TM) (Glycoprotein 36) (gp36)]
[SFTPB SFTP3] Pulmonary surfactant-associated protein B (SP-B) (6 kDa protein) (Pulmonary surfactant-associated proteolipid SPL(Phe))
[Sftpa1 Sftp-1 Sftp1 Sftpa] Pulmonary surfactant-associated protein A (PSAP) (PSP-A) (SP-A)
[Sftpc Sftp2] Pulmonary surfactant-associated protein C (SP-C) (Pulmonary surfactant-associated proteolipid SPL(Val)) (SP5)
[SFTPC SFTP2] Pulmonary surfactant-associated protein C (SP-C) (Pulmonary surfactant-associated proteolipid SPL(Val))
[SFTPD] Pulmonary surfactant-associated protein D (PSP-D) (SP-D) (Lung surfactant protein D)
[SFTPC SFTP2] Pulmonary surfactant-associated protein C (SP-C) (Pulmonary surfactant-associated proteolipid SPL(Val))
[FMO2] Dimethylaniline monooxygenase [N-oxide-forming] 2 (EC 1.14.13.8) (Dimethylaniline oxidase 2) (FMO 1B1) (Pulmonary flavin-containing monooxygenase 2) (FMO 2)
[SFTPA1 SFTP1 SFTPA] Pulmonary surfactant-associated protein A (PSAP) (PSP-A) (SP-A)
[SFTPD] Pulmonary surfactant-associated protein D (PSP-D) (SP-D) (Lung surfactant protein D)
[DMBT1 GP340] Deleted in malignant brain tumors 1 protein (Glycoprotein 340) (Gp-340) (Hensin) (Salivary agglutinin) (SAG) (Surfactant pulmonary-associated D-binding protein)
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