SPRC_HUMAN
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 03-AUG-2022, entry version 225.
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; 46.
DR DIP; DIP-46426N; -.
DR IntAct; P09486; 22.
DR MINT; P09486; -.
DR STRING; 9606.ENSP00000231061; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR GlyConnect; 706; 37 N-Linked glycans (1 site).
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; P09486; -.
DR PeptideAtlas; P09486; -.
DR PRIDE; P09486; -.
DR ProteomicsDB; 52226; -.
DR Antibodypedia; 878; 783 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 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; 1528521at2759; -.
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; 6 hits in 1086 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 216 other tissues.
DR ExpressionAtlas; P09486; baseline and differential.
DR Genevisible; P09486; HS.
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 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; IPR037641; SPARC.
DR InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR PANTHER; PTHR13866:SF6; PTHR13866:SF6; 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; SSF100895; SSF100895; 1.
DR SUPFAM; SSF47473; SSF47473; 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.
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
