ID   SPRC_HUMAN              Reviewed;         303 AA.
AC   P09486; D3DQH9; Q6IBK4;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   24-JAN-2024, entry version 233.
DE   RecName: Full=SPARC;
DE   AltName: Full=Basement-membrane protein 40;
DE            Short=BM-40;
DE   AltName: Full=Osteonectin;
DE            Short=ON;
DE   AltName: Full=Secreted protein acidic and rich in cysteine;
DE   Flags: Precursor;
GN   Name=SPARC; Synonyms=ON;
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], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Placenta;
RX   PubMed=3410046; DOI=10.1016/0014-5793(88)80054-1;
RA   Lankat-Buttgereit B., Mann K., Deutzmann R., Timpl R., Krieg T.;
RT   "Cloning and complete amino acid sequences of human and murine basement
RT   membrane protein BM-40 (SPARC, osteonectin).";
RL   FEBS Lett. 236:352-356(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2838412; DOI=10.1016/0888-7543(88)90107-3;
RA   Swaroop A., Hogan B.L.M., Francke U.;
RT   "Molecular analysis of the cDNA for human SPARC/osteonectin/BM-40:
RT   sequence, expression, and localization of the gene to chromosome 5q31-
RT   q33.";
RL   Genomics 2:37-47(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2790009; DOI=10.1021/bi00441a049;
RA   Villarreal X.C., Mann K.G., Long G.L.;
RT   "Structure of human osteonectin based upon analysis of cDNA and genomic
RT   sequences.";
RL   Biochemistry 28:6483-6491(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2338025; DOI=10.3109/03008209009152419;
RA   Young M.F., Day A.A., Dominquez P., McQuillan C.I., Fisher L.W.,
RA   Termine J.D.;
RT   "Structure and expression of osteonectin mRNA in human tissue.";
RL   Connect. Tissue Res. 24:17-28(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Muscle, PNS, and Skin;
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-154.
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [9]
RP   PROTEIN SEQUENCE OF 18-53, AND CHARACTERIZATION.
RX   PubMed=3597437; DOI=10.1016/s0021-9258(18)47991-4;
RA   Fisher L.W., Hawkins G.R., Tuross N., Termine J.D.;
RT   "Purification and partial characterization of small proteoglycans I and II,
RT   bone sialoproteins I and II, and osteonectin from the mineral compartment
RT   of developing human bone.";
RL   J. Biol. Chem. 262:9702-9708(1987).
RN   [10]
RP   PROTEIN SEQUENCE OF 18-41, CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX   PubMed=2306517;
RA   Kelm R.J. Jr., Mann K.G.;
RT   "Human platelet osteonectin: release, surface expression, and partial
RT   characterization.";
RL   Blood 75:1105-1113(1990).
RN   [11]
RP   SUBCELLULAR LOCATION.
RX   PubMed=3400777;
RA   Wewer U.M., Albrechtsen R., Fisher L.W., Young M.F., Termine J.D.;
RT   "Osteonectin/SPARC/BM-40 in human decidua and carcinoma, tissues
RT   characterized by de novo formation of basement membrane.";
RL   Am. J. Pathol. 132:345-355(1988).
RN   [12]
RP   SUBCELLULAR LOCATION.
RX   PubMed=7495300;
RA   Kuhn C., Mason R.J.;
RT   "Immunolocalization of SPARC, tenascin, and thrombospondin in pulmonary
RT   fibrosis.";
RL   Am. J. Pathol. 147:1759-1769(1995).
RN   [13]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9457905; DOI=10.1046/j.1523-1747.1998.00094.x;
RA   Hunzelmann N., Hafner M., Anders S., Krieg T., Nischt R.;
RT   "BM-40 (osteonectin, SPARC) is expressed both in the epidermal and in the
RT   dermal compartment of adult human skin.";
RL   J. Invest. Dermatol. 110:122-126(1998).
RN   [14]
RP   INVOLVEMENT IN OI17, VARIANTS OI17 HIS-166 AND LYS-263, AND
RP   CHARACTERIZATION OF VARIANTS OI17 HIS-166 AND LYS-263.
RX   PubMed=26027498; DOI=10.1016/j.ajhg.2015.04.021;
RG   Care4Rare Canada Consortium;
RA   Mendoza-Londono R., Fahiminiya S., Majewski J., Tetreault M., Nadaf J.,
RA   Kannu P., Sochett E., Howard A., Stimec J., Dupuis L., Roschger P.,
RA   Klaushofer K., Palomo T., Ouellet J., Al-Jallad H., Mort J.S., Moffatt P.,
RA   Boudko S., Baechinger H.P., Rauch F.;
RT   "Recessive osteogenesis imperfecta caused by missense mutations in SPARC.";
RL   Am. J. Hum. Genet. 96:979-985(2015).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 153-303.
RX   PubMed=8548457; DOI=10.1038/nsb0196-67;
RA   Hohenester E., Maurer P., Hahoenadl C., Timpl R., Jansonius J.N., Engel J.;
RT   "Structure of a novel extracellular Ca(2+)-binding module in BM-40.";
RL   Nat. Struct. Biol. 3:67-73(1996).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 71-303 IN COMPLEX WITH CALCIUM
RP   IONS, GLYCOSYLATION AT ASN-116, AND DISULFIDE BONDS.
RX   PubMed=9233787; DOI=10.1093/emboj/16.13.3778;
RA   Hohenester E., Maurer P., Timpl R.;
RT   "Crystal structure of a pair of follistatin-like and EF-hand calcium-
RT   binding domains in BM-40.";
RL   EMBO J. 16:3778-3786(1997).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 71-303 IN COMPLEX WITH CALCIUM
RP   IONS, GLYCOSYLATION AT ASN-116, INTERACTION WITH COLLAGEN, AND MUTAGENESIS
RP   OF ARG-166; ASN-173; LEU-259; MET-262 AND GLU-263.
RX   PubMed=9501084; DOI=10.1093/emboj/17.6.1625;
RA   Sasaki T., Hohenester E., Gohring W., Timpl R.;
RT   "Crystal structure and mapping by site-directed mutagenesis of the
RT   collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin.";
RL   EMBO J. 17:1625-1634(1998).
CC   -!- FUNCTION: Appears to regulate cell growth through interactions with the
CC       extracellular matrix and cytokines. Binds calcium and copper, several
CC       types of collagen, albumin, thrombospondin, PDGF and cell membranes.
CC       There are two calcium binding sites; an acidic domain that binds 5 to 8
CC       Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion
CC       with a high affinity.
CC   -!- INTERACTION:
CC       P09486; P02461-1: COL3A1; NbExp=4; IntAct=EBI-2800983, EBI-15740444;
CC       P09486; Q99972: MYOC; NbExp=3; IntAct=EBI-2800983, EBI-11692272;
CC       P09486; Q2TV77: faf; Xeno; NbExp=4; IntAct=EBI-2800983, EBI-6405263;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000269|PubMed:2306517,
CC       ECO:0000269|PubMed:3400777, ECO:0000269|PubMed:7495300,
CC       ECO:0000269|PubMed:9457905}. Note=In or around the basement membrane.
CC   -!- DEVELOPMENTAL STAGE: Expressed at high levels in tissues undergoing
CC       morphogenesis, remodeling and wound repair.
CC   -!- DISEASE: Osteogenesis imperfecta 17 (OI17) [MIM:616507]: An autosomal
CC       recessive form of osteogenesis imperfecta, a connective tissue disorder
CC       characterized by low bone mass, bone fragility and susceptibility to
CC       fractures after minimal trauma. Disease severity ranges from very mild
CC       forms without fractures to intrauterine fractures and perinatal
CC       lethality. Extraskeletal manifestations, which affect a variable number
CC       of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC       sclerae. {ECO:0000269|PubMed:26027498}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA60993.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Osteonectin entry;
CC       URL="https://en.wikipedia.org/wiki/Osteonectin";
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DR   EMBL; Y00755; CAA68724.1; -; mRNA.
DR   EMBL; J03040; AAA60570.1; -; mRNA.
DR   EMBL; M25746; AAA60993.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M25738; AAA60993.1; JOINED; Genomic_DNA.
DR   EMBL; M25739; AAA60993.1; JOINED; Genomic_DNA.
DR   EMBL; M25740; AAA60993.1; JOINED; Genomic_DNA.
DR   EMBL; M25741; AAA60993.1; JOINED; Genomic_DNA.
DR   EMBL; M25742; AAA60993.1; JOINED; Genomic_DNA.
DR   EMBL; M25743; AAA60993.1; JOINED; Genomic_DNA.
DR   EMBL; M25744; AAA60993.1; JOINED; Genomic_DNA.
DR   EMBL; M25745; AAA60993.1; JOINED; Genomic_DNA.
DR   EMBL; CR456799; CAG33080.1; -; mRNA.
DR   EMBL; CH471062; EAW61668.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61669.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61670.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61672.1; -; Genomic_DNA.
DR   EMBL; BC004974; AAH04974.1; -; mRNA.
DR   EMBL; BC008011; AAH08011.1; -; mRNA.
DR   EMBL; BC072457; AAH72457.1; -; mRNA.
DR   EMBL; AL709729; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS4318.1; -.
DR   PIR; A32821; GEHUN.
DR   RefSeq; NP_001296372.1; NM_001309443.1.
DR   RefSeq; NP_001296373.1; NM_001309444.1.
DR   RefSeq; NP_003109.1; NM_003118.3.
DR   PDB; 1BMO; X-ray; 3.10 A; A/B=71-303.
DR   PDB; 1NUB; X-ray; 2.80 A; A/B=71-303.
DR   PDB; 1SRA; X-ray; 2.00 A; A=153-303.
DR   PDB; 2V53; X-ray; 3.20 A; A=70-303.
DR   PDBsum; 1BMO; -.
DR   PDBsum; 1NUB; -.
DR   PDBsum; 1SRA; -.
DR   PDBsum; 2V53; -.
DR   AlphaFoldDB; P09486; -.
DR   SMR; P09486; -.
DR   BioGRID; 112560; 49.
DR   DIP; DIP-46426N; -.
DR   IntAct; P09486; 23.
DR   MINT; P09486; -.
DR   STRING; 9606.ENSP00000231061; -.
DR   DrugBank; DB11093; Calcium citrate.
DR   DrugBank; DB11348; Calcium Phosphate.
DR   DrugBank; DB14481; Calcium phosphate dihydrate.
DR   TCDB; 8.A.74.1.6; the tm9 or phg1 targeting receptor (phg1) family.
DR   GlyConnect; 706; 37 N-Linked glycans (1 site).
DR   GlyCosmos; P09486; 2 sites, 45 glycans.
DR   GlyGen; P09486; 2 sites, 45 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P09486; -.
DR   MetOSite; P09486; -.
DR   PhosphoSitePlus; P09486; -.
DR   BioMuta; SPARC; -.
DR   DMDM; 129283; -.
DR   OGP; P09486; -.
DR   CPTAC; non-CPTAC-2699; -.
DR   EPD; P09486; -.
DR   jPOST; P09486; -.
DR   MassIVE; P09486; -.
DR   MaxQB; P09486; -.
DR   PaxDb; 9606-ENSP00000231061; -.
DR   PeptideAtlas; P09486; -.
DR   ProteomicsDB; 52226; -.
DR   Pumba; P09486; -.
DR   Antibodypedia; 878; 899 antibodies from 43 providers.
DR   DNASU; 6678; -.
DR   Ensembl; ENST00000231061.9; ENSP00000231061.4; ENSG00000113140.11.
DR   GeneID; 6678; -.
DR   KEGG; hsa:6678; -.
DR   MANE-Select; ENST00000231061.9; ENSP00000231061.4; NM_003118.4; NP_003109.1.
DR   UCSC; uc003lui.5; human.
DR   AGR; HGNC:11219; -.
DR   CTD; 6678; -.
DR   DisGeNET; 6678; -.
DR   GeneCards; SPARC; -.
DR   HGNC; HGNC:11219; SPARC.
DR   HPA; ENSG00000113140; Tissue enhanced (placenta).
DR   MalaCards; SPARC; -.
DR   MIM; 182120; gene.
DR   MIM; 616507; phenotype.
DR   neXtProt; NX_P09486; -.
DR   OpenTargets; ENSG00000113140; -.
DR   Orphanet; 216820; Osteogenesis imperfecta type 4.
DR   PharmGKB; PA36055; -.
DR   VEuPathDB; HostDB:ENSG00000113140; -.
DR   eggNOG; KOG4004; Eukaryota.
DR   GeneTree; ENSGT00510000046787; -.
DR   HOGENOM; CLU_047416_0_0_1; -.
DR   InParanoid; P09486; -.
DR   OMA; IWKFCEL; -.
DR   OrthoDB; 4695638at2759; -.
DR   PhylomeDB; P09486; -.
DR   TreeFam; TF319356; -.
DR   PathwayCommons; P09486; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   Reactome; R-HSA-3000497; Scavenging by Class H Receptors.
DR   SignaLink; P09486; -.
DR   SIGNOR; P09486; -.
DR   BioGRID-ORCS; 6678; 8 hits in 1168 CRISPR screens.
DR   ChiTaRS; SPARC; human.
DR   EvolutionaryTrace; P09486; -.
DR   GeneWiki; Osteonectin; -.
DR   GenomeRNAi; 6678; -.
DR   Pharos; P09486; Tbio.
DR   PRO; PR:P09486; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; P09486; Protein.
DR   Bgee; ENSG00000113140; Expressed in tibia and 218 other cell types or tissues.
DR   ExpressionAtlas; P09486; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB.
DR   GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR   GO; GO:0031092; C:platelet alpha granule membrane; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
DR   GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
DR   GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:UniProtKB.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; IDA:UniProtKB.
DR   CDD; cd16231; EFh_SPARC_like; 1.
DR   CDD; cd01328; FSL_SPARC; 1.
DR   Gene3D; 3.30.60.30; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   IDEAL; IID00648; -.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR003645; Fol_N.
DR   InterPro; IPR015369; Follistatin/Osteonectin_EGF.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR001999; Osteonectin_CS.
DR   InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR   InterPro; IPR037641; SPARC_FS.
DR   PANTHER; PTHR13866:SF6; SPARC; 1.
DR   PANTHER; PTHR13866; SPARC OSTEONECTIN; 1.
DR   Pfam; PF09289; FOLN; 1.
DR   Pfam; PF00050; Kazal_1; 1.
DR   Pfam; PF10591; SPARC_Ca_bdg; 1.
DR   SMART; SM00274; FOLN; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS00612; OSTEONECTIN_1; 1.
DR   PROSITE; PS00613; OSTEONECTIN_2; 1.
DR   Genevisible; P09486; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Basement membrane; Calcium; Copper;
KW   Direct protein sequencing; Disease variant; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Metal-binding; Osteogenesis imperfecta;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:2306517,
FT                   ECO:0000269|PubMed:3597437"
FT   CHAIN           18..303
FT                   /note="SPARC"
FT                   /id="PRO_0000020304"
FT   DOMAIN          71..93
FT                   /note="Follistatin-like"
FT   DOMAIN          89..151
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          261..296
FT                   /note="EF-hand"
FT   BINDING         274
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT   BINDING         276
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT   BINDING         278
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT   BINDING         280
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT   BINDING         285
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:9233787,
FT                   ECO:0000269|PubMed:9501084"
FT   DISULFID        72..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798,
FT                   ECO:0000269|PubMed:9233787"
FT   DISULFID        77..93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798,
FT                   ECO:0000269|PubMed:9233787"
FT   DISULFID        95..130
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798,
FT                   ECO:0000269|PubMed:9233787"
FT   DISULFID        101..123
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798,
FT                   ECO:0000269|PubMed:9233787"
FT   DISULFID        112..149
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798,
FT                   ECO:0000269|PubMed:9233787"
FT   DISULFID        155..265
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798,
FT                   ECO:0000269|PubMed:9233787"
FT   DISULFID        273..289
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798,
FT                   ECO:0000269|PubMed:9233787"
FT   VARIANT         19
FT                   /note="P -> S (in dbSNP:rs6874468)"
FT                   /id="VAR_050431"
FT   VARIANT         70
FT                   /note="N -> S (in dbSNP:rs13359508)"
FT                   /id="VAR_059530"
FT   VARIANT         166
FT                   /note="R -> H (in OI17; decreased secretion of the protein;
FT                   altered secretion of procollagen type I;
FT                   dbSNP:rs1057517662)"
FT                   /evidence="ECO:0000269|PubMed:26027498"
FT                   /id="VAR_075142"
FT   VARIANT         263
FT                   /note="E -> K (in OI17; no effect on expression and
FT                   secretion of the protein; altered secretion of procollagen
FT                   type I; dbSNP:rs1057517663)"
FT                   /evidence="ECO:0000269|PubMed:26027498"
FT                   /id="VAR_075143"
FT   MUTAGEN         166
FT                   /note="R->A,L,K: Strongly reduced collagen binding."
FT                   /evidence="ECO:0000269|PubMed:9501084"
FT   MUTAGEN         173
FT                   /note="N->A,Q: Strongly reduced collagen binding."
FT                   /evidence="ECO:0000269|PubMed:9501084"
FT   MUTAGEN         259
FT                   /note="L->A: Loss of collagen binding."
FT                   /evidence="ECO:0000269|PubMed:9501084"
FT   MUTAGEN         262
FT                   /note="M->A: Strongly reduced collagen binding."
FT                   /evidence="ECO:0000269|PubMed:9501084"
FT   MUTAGEN         263
FT                   /note="E->A: Loss of collagen binding."
FT                   /evidence="ECO:0000269|PubMed:9501084"
FT   CONFLICT        42..43
FT                   /note="SV -> PT (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        205
FT                   /note="R -> L (in Ref. 3; AAA60993)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        269
FT                   /note="F -> L (in Ref. 3; AAA60993)"
FT                   /evidence="ECO:0000305"
FT   TURN            71..74
FT                   /evidence="ECO:0007829|PDB:1NUB"
FT   STRAND          81..85
FT                   /evidence="ECO:0007829|PDB:1NUB"
FT   STRAND          91..95
FT                   /evidence="ECO:0007829|PDB:1NUB"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:1NUB"
FT   HELIX           107..109
FT                   /evidence="ECO:0007829|PDB:1NUB"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:1NUB"
FT   TURN            114..116
FT                   /evidence="ECO:0007829|PDB:2V53"
FT   STRAND          118..121
FT                   /evidence="ECO:0007829|PDB:1NUB"
FT   HELIX           122..131
FT                   /evidence="ECO:0007829|PDB:1NUB"
FT   TURN            132..134
FT                   /evidence="ECO:0007829|PDB:1NUB"
FT   HELIX           136..140
FT                   /evidence="ECO:0007829|PDB:1NUB"
FT   STRAND          143..148
FT                   /evidence="ECO:0007829|PDB:1NUB"
FT   HELIX           157..181
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   STRAND          183..188
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   HELIX           190..201
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   HELIX           213..222
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   HELIX           224..227
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   HELIX           228..238
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   STRAND          244..247
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   TURN            249..252
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   HELIX           253..256
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   TURN            257..259
FT                   /evidence="ECO:0007829|PDB:2V53"
FT   HELIX           260..262
FT                   /evidence="ECO:0007829|PDB:2V53"
FT   HELIX           263..265
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   HELIX           266..273
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   STRAND          278..282
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   HELIX           283..289
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   HELIX           294..296
FT                   /evidence="ECO:0007829|PDB:1SRA"
FT   HELIX           299..301
FT                   /evidence="ECO:0007829|PDB:1SRA"
SQ   SEQUENCE   303 AA;  34632 MW;  B914599F79705945 CRC64;
     MRAWIFFLLC LAGRALAAPQ QEALPDETEV VEETVAEVTE VSVGANPVQV EVGEFDDGAE
     ETEEEVVAEN PCQNHHCKHG KVCELDENNT PMCVCQDPTS CPAPIGEFEK VCSNDNKTFD
     SSCHFFATKC TLEGTKKGHK LHLDYIGPCK YIPPCLDSEL TEFPLRMRDW LKNVLVTLYE
     RDEDNNLLTE KQKLRVKKIH ENEKRLEAGD HPVELLARDF EKNYNMYIFP VHWQFGQLDQ
     HPIDGYLSHT ELAPLRAPLI PMEHCTTRFF ETCDLDNDKY IALDEWAGCF GIKQKDIDKD
     LVI
//