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P35247

- SFTPD_HUMAN

UniProt

P35247 - SFTPD_HUMAN

Protein

Pulmonary surfactant-associated protein D

Gene

SFTPD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. carbohydrate binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. defense response to bacterium Source: UniProtKB
    2. innate immune response Source: UniProtKB
    3. lung alveolus development Source: UniProtKB
    4. macrophage chemotaxis Source: UniProtKB
    5. negative regulation of interleukin-2 biosynthetic process Source: UniProtKB
    6. negative regulation of T cell proliferation Source: UniProtKB
    7. positive regulation of phagocytosis Source: UniProtKB
    8. reactive oxygen species metabolic process Source: UniProtKB
    9. receptor-mediated endocytosis Source: UniProtKB
    10. regulation of cytokine production Source: UniProtKB
    11. respiratory gaseous exchange Source: UniProtKB-KW
    12. surfactant homeostasis Source: UniProtKB

    Keywords - Biological processi

    Gaseous exchange, Immunity, Innate immunity

    Keywords - Ligandi

    Calcium, Lectin

    Enzyme and pathway databases

    ReactomeiREACT_23916. Signal regulatory protein (SIRP) family interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pulmonary surfactant-associated protein D
    Short name:
    PSP-D
    Short name:
    SP-D
    Alternative name(s):
    Collectin-7
    Lung surfactant protein D
    Gene namesi
    Name:SFTPD
    Synonyms:COLEC7, PSPD, SFTP4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:10803. SFTPD.

    Subcellular locationi

    GO - Cellular componenti

    1. collagen trimer Source: UniProtKB-KW
    2. endocytic vesicle Source: UniProtKB
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: UniProtKB-SubCell
    5. lysosome Source: UniProtKB
    6. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted, Surface film

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35715.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020By similarityAdd
    BLAST
    Chaini21 – 375355Pulmonary surfactant-associated protein DPRO_0000017465Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei35 – 351S-nitrosocysteineBy similarity
    Modified residuei40 – 401S-nitrosocysteineBy similarity
    Modified residuei78 – 7814-hydroxyprolineBy similarity
    Modified residuei87 – 8715-hydroxylysineBy similarity
    Glycosylationi90 – 901N-linked (GlcNAc...)Sequence Analysis
    Modified residuei96 – 9614-hydroxyprolineBy similarity
    Modified residuei99 – 9915-hydroxylysineBy similarity
    Modified residuei171 – 17114-hydroxyprolineBy similarity
    Modified residuei177 – 17714-hydroxyprolineBy similarity
    Disulfide bondi281 ↔ 373
    Disulfide bondi351 ↔ 365

    Post-translational modificationi

    The N-terminus is blocked.
    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.By similarity
    S-nitrosylation at Cys-35 and Cys-40 alters the quaternary structure which results in a pro-inflammatory chemoattractive signaling activity with macrophages.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation, S-nitrosylation

    Proteomic databases

    PaxDbiP35247.
    PRIDEiP35247.

    Expressioni

    Tissue specificityi

    Expressed in lung, brain, pancreas and adipose tissue (mainly mature adipocytes).1 Publication

    Gene expression databases

    ArrayExpressiP35247.
    BgeeiP35247.
    CleanExiHS_SFTPD.
    GenevestigatoriP35247.

    Organism-specific databases

    HPAiCAB004578.
    HPA044582.

    Interactioni

    Subunit structurei

    Oligomeric complex of 4 set of homotrimers.

    Protein-protein interaction databases

    BioGridi112339. 3 interactions.
    STRINGi9606.ENSP00000361366.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi226 – 25328
    Turni254 – 2563
    Beta strandi257 – 2604
    Beta strandi263 – 27311
    Helixi274 – 28310
    Beta strandi286 – 2883
    Helixi294 – 30714
    Beta strandi311 – 3166
    Beta strandi318 – 3203
    Beta strandi323 – 3253
    Helixi345 – 3473
    Beta strandi351 – 3544
    Beta strandi360 – 3634
    Beta strandi367 – 3759

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B08X-ray2.30A/B/C218-375[»]
    1M7LNMR-A/B/C220-257[»]
    1PW9X-ray1.60A/B/C199-375[»]
    1PWBX-ray1.40A/B/C199-375[»]
    2GGUX-ray1.90A/B/C223-375[»]
    2GGXX-ray1.90A/B/C223-375[»]
    2ORJX-ray1.80A/B/C223-375[»]
    2ORKX-ray1.89A/B/C223-375[»]
    2OS9X-ray1.70A/B/C223-375[»]
    2RIAX-ray1.80A/B/C223-375[»]
    2RIBX-ray1.80A/B/C223-375[»]
    2RICX-ray1.80A/B/C223-375[»]
    2RIDX-ray1.80A/B/C223-375[»]
    2RIEX-ray1.60A/B/C223-375[»]
    3DBZX-ray1.80A/B/C223-375[»]
    3G81X-ray1.80A/B/C223-375[»]
    3G83X-ray1.90A/B/C223-375[»]
    3G84X-ray2.30A/B/C223-375[»]
    3IKNX-ray1.60A/B/C199-375[»]
    3IKPX-ray1.75A/B/C199-375[»]
    3IKQX-ray2.25A/B/C199-375[»]
    3IKRX-ray1.65A/B/C199-375[»]
    4E52X-ray1.70A/B/C201-375[»]
    4M17X-ray2.10A/B/C/D/E/F/G/H/I/J/K/L229-375[»]
    4M18X-ray3.20A/B/C/D/E/F/G/H/I/J/K/L229-375[»]
    ProteinModelPortaliP35247.
    SMRiP35247. Positions 224-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35247.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 222177Collagen-likeAdd
    BLAST
    Domaini260 – 375116C-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili223 – 25230Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SFTPD family.Curated
    Contains 1 C-type lectin domain.PROSITE-ProRule annotation
    Contains 1 collagen-like domain.Curated

    Keywords - Domaini

    Coiled coil, Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG267163.
    HOVERGENiHBG108270.
    InParanoidiP35247.
    KOiK10068.
    OMAiEMKTYSQ.
    OrthoDBiEOG7HXCVB.
    PhylomeDBiP35247.
    TreeFamiTF330481.

    Family and domain databases

    Gene3Di1.20.5.360. 1 hit.
    3.10.100.10. 1 hit.
    InterProiIPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    IPR008160. Collagen.
    IPR015097. Surfac_D-trimer.
    [Graphical view]
    PfamiPF01391. Collagen. 2 hits.
    PF00059. Lectin_C. 1 hit.
    PF09006. Surfac_D-trimer. 1 hit.
    [Graphical view]
    SMARTiSM00034. CLECT. 1 hit.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 1 hit.
    PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P35247-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLFLLSALV LLTQPLGYLE AEMKTYSHRT MPSACTLVMC SSVESGLPGR    50
    DGRDGREGPR GEKGDPGLPG AAGQAGMPGQ AGPVGPKGDN GSVGEPGPKG 100
    DTGPSGPPGP PGVPGPAGRE GPLGKQGNIG PQGKPGPKGE AGPKGEVGAP 150
    GMQGSAGARG LAGPKGERGV PGERGVPGNT GAAGSAGAMG PQGSPGARGP 200
    PGLKGDKGIP GDKGAKGESG LPDVASLRQQ VEALQGQVQH LQAAFSQYKK 250
    VELFPNGQSV GEKIFKTAGF VKPFTEAQLL CTQAGGQLAS PRSAAENAAL 300
    QQLVVAKNEA AFLSMTDSKT EGKFTYPTGE SLVYSNWAPG EPNDDGGSED 350
    CVEIFTNGKW NDRACGEKRL VVCEF 375
    Length:375
    Mass (Da):37,728
    Last modified:January 11, 2011 - v3
    Checksum:i298917699FC40F6A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221E → G in AAH22318. (PubMed:15489334)Curated
    Sequence conflicti59 – 591P → F AA sequence (PubMed:8424457)Curated
    Sequence conflicti122 – 1221P → A in AAB59450. (PubMed:8428971)Curated
    Sequence conflicti240 – 2401H → P AA sequence (PubMed:8424457)Curated
    Sequence conflicti341 – 3411E → K in AAH22318. (PubMed:15489334)Curated
    Sequence conflicti369 – 3691R → S in CAG46746. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311M → T.4 Publications
    Corresponds to variant rs721917 [ dbSNP | Ensembl ].
    VAR_020937
    Natural varianti123 – 1231L → V.2 Publications
    Corresponds to variant rs17878336 [ dbSNP | Ensembl ].
    VAR_020938
    Natural varianti180 – 1801T → A.4 Publications
    Corresponds to variant rs2243639 [ dbSNP | Ensembl ].
    VAR_020939
    Natural varianti290 – 2901S → T.2 Publications
    Corresponds to variant rs3088308 [ dbSNP | Ensembl ].
    VAR_020940
    Natural varianti309 – 3091E → K.1 Publication
    Corresponds to variant rs4469829 [ dbSNP | Ensembl ].
    VAR_020941

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65018 mRNA. Translation: CAA46152.1.
    L05485, L05483, L05484 Genomic DNA. Translation: AAB59450.1.
    CR541948 mRNA. Translation: CAG46746.1.
    AY216721 Genomic DNA. Translation: AAO22991.1.
    AL512662 Genomic DNA. Translation: CAI14436.1.
    BC022318 mRNA. Translation: AAH22318.1.
    CCDSiCCDS7362.1.
    PIRiA45225.
    RefSeqiNP_003010.4. NM_003019.4.
    UniGeneiHs.253495.

    Genome annotation databases

    EnsembliENST00000372292; ENSP00000361366; ENSG00000133661.
    GeneIDi6441.
    KEGGihsa:6441.
    UCSCiuc001kbh.3. human.

    Polymorphism databases

    DMDMi317373510.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs
    Functional Glycomics Gateway - Glycan Binding

    Pulmonary surfactant protein SP-D

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65018 mRNA. Translation: CAA46152.1 .
    L05485 , L05483 , L05484 Genomic DNA. Translation: AAB59450.1 .
    CR541948 mRNA. Translation: CAG46746.1 .
    AY216721 Genomic DNA. Translation: AAO22991.1 .
    AL512662 Genomic DNA. Translation: CAI14436.1 .
    BC022318 mRNA. Translation: AAH22318.1 .
    CCDSi CCDS7362.1.
    PIRi A45225.
    RefSeqi NP_003010.4. NM_003019.4.
    UniGenei Hs.253495.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B08 X-ray 2.30 A/B/C 218-375 [» ]
    1M7L NMR - A/B/C 220-257 [» ]
    1PW9 X-ray 1.60 A/B/C 199-375 [» ]
    1PWB X-ray 1.40 A/B/C 199-375 [» ]
    2GGU X-ray 1.90 A/B/C 223-375 [» ]
    2GGX X-ray 1.90 A/B/C 223-375 [» ]
    2ORJ X-ray 1.80 A/B/C 223-375 [» ]
    2ORK X-ray 1.89 A/B/C 223-375 [» ]
    2OS9 X-ray 1.70 A/B/C 223-375 [» ]
    2RIA X-ray 1.80 A/B/C 223-375 [» ]
    2RIB X-ray 1.80 A/B/C 223-375 [» ]
    2RIC X-ray 1.80 A/B/C 223-375 [» ]
    2RID X-ray 1.80 A/B/C 223-375 [» ]
    2RIE X-ray 1.60 A/B/C 223-375 [» ]
    3DBZ X-ray 1.80 A/B/C 223-375 [» ]
    3G81 X-ray 1.80 A/B/C 223-375 [» ]
    3G83 X-ray 1.90 A/B/C 223-375 [» ]
    3G84 X-ray 2.30 A/B/C 223-375 [» ]
    3IKN X-ray 1.60 A/B/C 199-375 [» ]
    3IKP X-ray 1.75 A/B/C 199-375 [» ]
    3IKQ X-ray 2.25 A/B/C 199-375 [» ]
    3IKR X-ray 1.65 A/B/C 199-375 [» ]
    4E52 X-ray 1.70 A/B/C 201-375 [» ]
    4M17 X-ray 2.10 A/B/C/D/E/F/G/H/I/J/K/L 229-375 [» ]
    4M18 X-ray 3.20 A/B/C/D/E/F/G/H/I/J/K/L 229-375 [» ]
    ProteinModelPortali P35247.
    SMRi P35247. Positions 224-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112339. 3 interactions.
    STRINGi 9606.ENSP00000361366.

    Chemistry

    ChEMBLi CHEMBL2176857.

    Polymorphism databases

    DMDMi 317373510.

    Proteomic databases

    PaxDbi P35247.
    PRIDEi P35247.

    Protocols and materials databases

    DNASUi 6441.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372292 ; ENSP00000361366 ; ENSG00000133661 .
    GeneIDi 6441.
    KEGGi hsa:6441.
    UCSCi uc001kbh.3. human.

    Organism-specific databases

    CTDi 6441.
    GeneCardsi GC10M081687.
    H-InvDB HIX0008974.
    HGNCi HGNC:10803. SFTPD.
    HPAi CAB004578.
    HPA044582.
    MIMi 178635. gene.
    neXtProti NX_P35247.
    PharmGKBi PA35715.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG267163.
    HOVERGENi HBG108270.
    InParanoidi P35247.
    KOi K10068.
    OMAi EMKTYSQ.
    OrthoDBi EOG7HXCVB.
    PhylomeDBi P35247.
    TreeFami TF330481.

    Enzyme and pathway databases

    Reactomei REACT_23916. Signal regulatory protein (SIRP) family interactions.

    Miscellaneous databases

    EvolutionaryTracei P35247.
    GeneWikii Surfactant_protein_D.
    GenomeRNAii 6441.
    NextBioi 25031.
    PROi P35247.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35247.
    Bgeei P35247.
    CleanExi HS_SFTPD.
    Genevestigatori P35247.

    Family and domain databases

    Gene3Di 1.20.5.360. 1 hit.
    3.10.100.10. 1 hit.
    InterProi IPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    IPR008160. Collagen.
    IPR015097. Surfac_D-trimer.
    [Graphical view ]
    Pfami PF01391. Collagen. 2 hits.
    PF00059. Lectin_C. 1 hit.
    PF09006. Surfac_D-trimer. 1 hit.
    [Graphical view ]
    SMARTi SM00034. CLECT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    PROSITEi PS00615. C_TYPE_LECTIN_1. 1 hit.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification, characterization and cDNA cloning of human lung surfactant protein D."
      Lu J., Willis A.C., Reid K.B.M.
      Biochem. J. 284:795-802(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 214-243, VARIANTS THR-31 AND ALA-180.
      Tissue: Amniotic fluid and Lung.
    2. "Genomic organization of human surfactant protein D (SP-D). SP-D is encoded on chromosome 10q22.2-23.1."
      Crouch E., Rust K., Veile R., Donis-Keller H., Grosso L.
      J. Biol. Chem. 268:2976-2983(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      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.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS THR-31 AND ALA-180.
    4. SeattleSNPs variation discovery resource
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-31; VAL-123; ALA-180; THR-290 AND LYS-309.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      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.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    7. "Accumulation of surfactant protein D in human pulmonary alveolar proteinosis."
      Crouch E., Persson A., Chang D.
      Am. J. Pathol. 142:241-248(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 46-72 AND 223-260.
    8. "Human surfactant protein D: SP-D contains a C-type lectin carbohydrate recognition domain."
      Rust K., Grosso L., Zhang V., Chang D., Persson A., Longmore W., Cai G.-Z., Crouch E.
      Arch. Biochem. Biophys. 290:116-126(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-375, PARTIAL PROTEIN SEQUENCE.
      Tissue: Lung.
    9. "The lung innate immune gene surfactant protein-D is expressed in adipose tissue and linked to obesity status."
      Ortega F.J., Pueyo N., Moreno-Navarrete J.M., Sabater M., Rodriguez-Hermosa J.I., Ricart W., Tinahones F.J., Fernandez-Real J.M.
      Int. J. Obes. Relat. Metab. Disord. 37:1532-1538(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    10. "Crystal structure of the trimeric alpha-helical coiled-coil and the three lectin domains of human lung surfactant protein D."
      Hakansson K., Lim N.K., Hoppe H.-J., Reid K.B.M.
      Structure 7:255-264(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    11. "Genetic defects in surfactant protein A2 are associated with pulmonary fibrosis and lung cancer."
      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.
      Am. J. Hum. Genet. 84:52-59(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS THR-31; VAL-123; ALA-180 AND THR-290.

    Entry informationi

    Entry nameiSFTPD_HUMAN
    AccessioniPrimary (citable) accession number: P35247
    Secondary accession number(s): Q5T0M3
    , Q6FH08, Q86YK9, Q8TCD8, Q9UCJ2, Q9UCJ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 159 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    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).

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3