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-MAR-2024, entry version 228.
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; DOI=10.1016/s0021-9258(18)53869-2;
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; Q9BYF1: ACE2; NbExp=2; IntAct=EBI-11316157, EBI-7730807;
CC       P35247; O00322: UPK1A; NbExp=3; IntAct=EBI-11316157, EBI-14031976;
CC       P35247; P0DTC2: S; Xeno; NbExp=3; IntAct=EBI-11316157, EBI-25474821;
CC       PRO_0000017465; P0DTC2: S; Xeno; NbExp=11; IntAct=EBI-27021977, EBI-25474821;
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";
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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   AlphaFoldDB; P35247; -.
DR   SMR; P35247; -.
DR   BioGRID; 112339; 9.
DR   IntAct; P35247; 6.
DR   STRING; 9606.ENSP00000361366; -.
DR   ChEMBL; CHEMBL2176857; -.
DR   DrugBank; DB02379; Beta-D-Glucose.
DR   UniLectin; P35247; -.
DR   GlyCosmos; P35247; 1 site, No reported glycans.
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; 9606-ENSP00000361366; -.
DR   PeptideAtlas; P35247; -.
DR   ProteomicsDB; 55012; -.
DR   Antibodypedia; 3886; 645 antibodies from 38 providers.
DR   DNASU; 6441; -.
DR   Ensembl; ENST00000372292.8; ENSP00000361366.3; ENSG00000133661.17.
DR   GeneID; 6441; -.
DR   KEGG; hsa:6441; -.
DR   MANE-Select; ENST00000372292.8; ENSP00000361366.3; NM_003019.5; NP_003010.4.
DR   UCSC; uc001kbh.4; human.
DR   AGR; HGNC:10803; -.
DR   CTD; 6441; -.
DR   DisGeNET; 6441; -.
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   VEuPathDB; HostDB:ENSG00000133661; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000155748; -.
DR   HOGENOM; CLU_049894_3_0_1; -.
DR   InParanoid; P35247; -.
DR   OMA; EMFTNGK; -.
DR   OrthoDB; 4641030at2759; -.
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 SMDP5.
DR   Reactome; R-HSA-5688890; Defective CSF2RA causes SMDP4.
DR   Reactome; R-HSA-9692916; SARS-CoV-1 activates/modulates innate immune responses.
DR   Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR   SignaLink; P35247; -.
DR   SIGNOR; P35247; -.
DR   BioGRID-ORCS; 6441; 9 hits in 1147 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 lower lobe of lung and 114 other cell types or tissues.
DR   ExpressionAtlas; P35247; baseline and differential.
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:0030246; F:carbohydrate binding; TAS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0042742; P:defense response to bacterium; TAS:UniProtKB.
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: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:0001817; P:regulation of cytokine production; NAS:UniProtKB.
DR   GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:UniProtKB-KW.
DR   GO; GO:0043129; P:surfactant homeostasis; IMP:UniProtKB.
DR   CDD; cd03591; CLECT_collectin_like; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   Gene3D; 1.20.5.360; SFTPD helical domain; 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   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1082; COLLAGEN ALPHA-1(X) CHAIN; 1.
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; C-type lectin-like; 1.
DR   SUPFAM; SSF57944; Triple coiled coil domain of C-type lectins; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   Genevisible; P35247; HS.
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; Reference proteome;
KW   Repeat; S-nitrosylation; Secreted; Signal; 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   REGION          45..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          223..252
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        49..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..117
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007829|PDB:1PWB"
FT   TURN            254..256
FT                   /evidence="ECO:0007829|PDB:1PWB"
FT   STRAND          257..260
FT                   /evidence="ECO:0007829|PDB:1PWB"
FT   STRAND          263..273
FT                   /evidence="ECO:0007829|PDB:1PWB"
FT   HELIX           274..283
FT                   /evidence="ECO:0007829|PDB:1PWB"
FT   STRAND          286..288
FT                   /evidence="ECO:0007829|PDB:1PWB"
FT   HELIX           294..307
FT                   /evidence="ECO:0007829|PDB:1PWB"
FT   STRAND          311..316
FT                   /evidence="ECO:0007829|PDB:2RIA"
FT   STRAND          318..320
FT                   /evidence="ECO:0007829|PDB:1PWB"
FT   STRAND          323..325
FT                   /evidence="ECO:0007829|PDB:2GGX"
FT   HELIX           345..347
FT                   /evidence="ECO:0007829|PDB:1PWB"
FT   STRAND          351..354
FT                   /evidence="ECO:0007829|PDB:1PWB"
FT   STRAND          360..363
FT                   /evidence="ECO:0007829|PDB:1PWB"
FT   STRAND          367..375
FT                   /evidence="ECO:0007829|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
//