ID   ASPN_HUMAN              Reviewed;         380 AA.
AC   Q9BXN1; Q5TBF3; Q96K79; Q96LD0; Q9NXP3;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   24-JAN-2024, entry version 194.
DE   RecName: Full=Asporin;
DE   AltName: Full=Periodontal ligament-associated protein 1;
DE            Short=PLAP-1;
DE   Flags: Precursor;
GN   Name=ASPN; Synonyms=PLAP1, SLRR1C; ORFNames=UNQ215/PRO241;
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], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT
RP   SER-55 AND ASN-282, IDENTIFICATION BY MASS SPECTROMETRY, AND POLYMORPHISM
RP   OF POLY-ASP REGION.
RC   TISSUE=Cartilage;
RX   PubMed=11152692; DOI=10.1074/jbc.m010932200;
RA   Lorenzo P., Aspberg A., Oennerfjord P., Bayliss M.T., Neame P.J.,
RA   Heinegaard D.;
RT   "Identification and characterization of asporin. A novel member of the
RT   leucine-rich repeat protein family closely related to decorin and
RT   biglycan.";
RL   J. Biol. Chem. 276:12201-12211(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11587855; DOI=10.1016/s0378-1119(01)00683-7;
RA   Yamada S., Murakami S., Matoba R., Ozawa Y., Yokokoji T., Nakahira Y.,
RA   Ikezawa K., Takayama S., Matsubara K., Okada H.;
RT   "Expression profile of active genes in human periodontal ligament and
RT   isolation of PLAP-1, a novel SLRP family gene.";
RL   Gene 275:279-286(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon, and Embryo;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=11152695; DOI=10.1074/jbc.m011290200;
RA   Henry S.P., Takanosu M., Boyd T.C., Mayne P.M., Eberspaecher H., Zhou W.,
RA   de Crombrugghe B., Hoeoek M., Mayne R.;
RT   "Expression pattern and gene characterization of asporin. A newly
RT   discovered member of the leucine-rich repeat protein family.";
RL   J. Biol. Chem. 276:12212-12221(2001).
RN   [8]
RP   ASSOCIATION WITH OS3.
RX   PubMed=15640800; DOI=10.1038/ng1496;
RA   Kizawa H., Kou I., Iida A., Sudo A., Miyamoto Y., Fukuda A., Mabuchi A.,
RA   Kotani A., Kawakami A., Yamamoto S., Uchida A., Nakamura K., Notoya K.,
RA   Nakamura Y., Ikegawa S.;
RT   "An aspartic acid repeat polymorphism in asporin inhibits chondrogenesis
RT   and increases susceptibility to osteoarthritis.";
RL   Nat. Genet. 37:138-144(2005).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY TGFB1, AND TISSUE SPECIFICITY.
RX   PubMed=17827158; DOI=10.1074/jbc.m700522200;
RA   Nakajima M., Kizawa H., Saitoh M., Kou I., Miyazono K., Ikegawa S.;
RT   "Mechanisms for asporin function and regulation in articular cartilage.";
RL   J. Biol. Chem. 282:32185-32192(2007).
RN   [10]
RP   INVOLVEMENT IN SUSCEPTIBILITY TO IDD.
RX   PubMed=18304494; DOI=10.1016/j.ajhg.2007.12.017;
RA   Song Y.Q., Cheung K.M., Ho D.W., Poon S.C., Chiba K., Kawaguchi Y.,
RA   Hirose Y., Alini M., Grad S., Yee A.F., Leong J.C., Luk K.D., Yip S.P.,
RA   Karppinen J., Cheah K.S., Sham P., Ikegawa S., Chan D.;
RT   "Association of the asporin D14 allele with lumbar-disc degeneration in
RT   Asians.";
RL   Am. J. Hum. Genet. 82:744-747(2008).
RN   [11]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH TYPE I
RP   COLLAGEN, DISULFIDE BOND, AND DOMAIN.
RX   PubMed=19589127; DOI=10.1042/bj20090542;
RA   Kalamajski S., Aspberg A., Lindblom K., Heinegaard D., Oldberg A.;
RT   "Asporin competes with decorin for collagen binding, binds calcium and
RT   promotes osteoblast collagen mineralization.";
RL   Biochem. J. 423:53-59(2009).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-282.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
CC   -!- FUNCTION: Negatively regulates periodontal ligament (PDL)
CC       differentiation and mineralization to ensure that the PDL is not
CC       ossified and to maintain homeostasis of the tooth-supporting system.
CC       Inhibits BMP2-induced cytodifferentiation of PDL cells by preventing
CC       its binding to BMPR1B/BMP type-1B receptor, resulting in inhibition of
CC       BMP-dependent activation of SMAD proteins (By similarity). Critical
CC       regulator of TGF-beta in articular cartilage and plays an essential
CC       role in cartilage homeostasis and osteoarthritis (OA) pathogenesis.
CC       Negatively regulates chondrogenesis in the articular cartilage by
CC       blocking the TGF-beta/receptor interaction on the cell surface and
CC       inhibiting the canonical TGF-beta/Smad signal. Binds calcium and plays
CC       a role in osteoblast-driven collagen biomineralization activity.
CC       {ECO:0000250, ECO:0000269|PubMed:17827158,
CC       ECO:0000269|PubMed:19589127}.
CC   -!- SUBUNIT: Interacts with TGFB1, TGFB2 and TGFB3. DCN, BGN, and FMOD
CC       inhibit binding to TGFB1. Interacts with BMP2. Interacts in vitro with
CC       type II collagen (By similarity). Interacts with type I collagen. DCN
CC       can inhibit collagen binding. {ECO:0000250,
CC       ECO:0000269|PubMed:19589127}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000269|PubMed:17827158}.
CC   -!- TISSUE SPECIFICITY: Higher levels in osteoarthritic articular
CC       cartilage, aorta, uterus. Moderate expression in small intestine,
CC       heart, liver, bladder, ovary, stomach, and in the adrenal, thyroid, and
CC       mammary glands. Low expression in trachea, bone marrow, and lung.
CC       Colocalizes with TGFB1 in chondrocytes within osteoarthritic (OA)
CC       lesions of articular cartilage. {ECO:0000269|PubMed:17827158}.
CC   -!- INDUCTION: By TGFB1. {ECO:0000269|PubMed:17827158}.
CC   -!- DOMAIN: The LRR 5 repeat can inhibit BMP2-induced cytodifferentiation
CC       and may be involved in the interaction with BMP2 (By similarity). The
CC       repeats LRR 10, LRR 11 and LRR 12 are involved in binding type I
CC       collagen. The poly-Asp region is involved in binding calcium.
CC       {ECO:0000250, ECO:0000269|PubMed:19589127}.
CC   -!- PTM: There is no serine/glycine dipeptide sequence expected for the
CC       attachment of O-linked glycosaminoglycans and this is probably not a
CC       proteoglycan. The O-linked polysaccharide on 54-Ser is probably the
CC       mucin type linked to GalNAc.
CC   -!- PTM: The N-linked glycan at Asn-282 is composed of variable structures
CC       of GlcNAc, mannose, fucose, HexNAc and hexose.
CC       {ECO:0000269|PubMed:11152692, ECO:0000269|PubMed:19159218}.
CC   -!- POLYMORPHISM: The poly-Asp region of ASPN is polymorphic and ranges at
CC       least from 11 to 17 Asp (PubMed:11152692).
CC       {ECO:0000269|PubMed:11152692}.
CC   -!- DISEASE: Osteoarthritis 3 (OS3) [MIM:607850]: A degenerative disease of
CC       the joints characterized by degradation of the hyaline articular
CC       cartilage and remodeling of the subchondral bone with sclerosis.
CC       Clinical symptoms include pain and joint stiffness often leading to
CC       significant disability and joint replacement. Note=Disease
CC       susceptibility is associated with variants affecting the gene
CC       represented in this entry. Susceptibility to osteoarthritis is
CC       conferred by a triplet repeat expansion polymorphism. ASPN allele
CC       having 14 aspartic acid repeats in the N-terminal region of the protein
CC       (D14), is overrepresented relative to the common allele having 13
CC       aspartic acid repeats (D13). The frequency of the D14 allele increases
CC       with disease severity. The D14 allele is also overrepresented in
CC       individuals with hip osteoarthritis.
CC   -!- DISEASE: Intervertebral disc disease (IDD) [MIM:603932]: A common
CC       musculo-skeletal disorder caused by degeneration of intervertebral
CC       disks of the lumbar spine. It results in low-back pain and unilateral
CC       leg pain. {ECO:0000269|PubMed:18304494}. Note=Disease susceptibility is
CC       associated with variants affecting the gene represented in this entry.
CC       Susceptibility to intervertebral disk disease, particularly lumbar disk
CC       degeneration, is conferred by a triplet repeat expansion polymorphism.
CC       ASPN allele having 14 aspartic acid repeats in the N-terminal region of
CC       the protein (D14), is associated with the disorder in some populations
CC       (PubMed:18304494). {ECO:0000269|PubMed:18304494}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class I subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA90967.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF316824; AAK35161.1; -; mRNA.
DR   EMBL; AY029191; AAK31800.1; -; mRNA.
DR   EMBL; AK000136; BAA90967.1; ALT_INIT; mRNA.
DR   EMBL; AK027359; BAB55060.1; -; mRNA.
DR   EMBL; AY358329; AAQ88695.1; -; mRNA.
DR   EMBL; AL137848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471089; EAW62822.1; -; Genomic_DNA.
DR   RefSeq; NP_001180264.1; NM_001193335.1.
DR   RefSeq; NP_060150.4; NM_017680.4.
DR   AlphaFoldDB; Q9BXN1; -.
DR   SMR; Q9BXN1; -.
DR   BioGRID; 120183; 6.
DR   STRING; 9606.ENSP00000364694; -.
DR   GlyConnect; 1019; 46 N-Linked glycans (1 site).
DR   GlyCosmos; Q9BXN1; 3 sites, 45 glycans.
DR   GlyGen; Q9BXN1; 3 sites, 44 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BXN1; -.
DR   PhosphoSitePlus; Q9BXN1; -.
DR   BioMuta; ASPN; -.
DR   DMDM; 209572589; -.
DR   jPOST; Q9BXN1; -.
DR   MassIVE; Q9BXN1; -.
DR   PaxDb; 9606-ENSP00000364694; -.
DR   PeptideAtlas; Q9BXN1; -.
DR   ProteomicsDB; 79461; -.
DR   Antibodypedia; 2015; 215 antibodies from 27 providers.
DR   DNASU; 54829; -.
DR   Ensembl; ENST00000375544.7; ENSP00000364694.3; ENSG00000106819.13.
DR   GeneID; 54829; -.
DR   KEGG; hsa:54829; -.
DR   UCSC; uc004ase.3; human.
DR   AGR; HGNC:14872; -.
DR   CTD; 54829; -.
DR   DisGeNET; 54829; -.
DR   GeneCards; ASPN; -.
DR   HGNC; HGNC:14872; ASPN.
DR   HPA; ENSG00000106819; Tissue enhanced (heart muscle, smooth muscle).
DR   MalaCards; ASPN; -.
DR   MIM; 603932; phenotype.
DR   MIM; 607850; phenotype.
DR   MIM; 608135; gene.
DR   neXtProt; NX_Q9BXN1; -.
DR   OpenTargets; ENSG00000106819; -.
DR   PharmGKB; PA25057; -.
DR   VEuPathDB; HostDB:ENSG00000106819; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000157444; -.
DR   HOGENOM; CLU_000288_186_0_1; -.
DR   InParanoid; Q9BXN1; -.
DR   OMA; NRIQKDA; -.
DR   OrthoDB; 3953748at2759; -.
DR   PhylomeDB; Q9BXN1; -.
DR   TreeFam; TF334562; -.
DR   PathwayCommons; Q9BXN1; -.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   BioGRID-ORCS; 54829; 2 hits in 289 CRISPR screens.
DR   ChiTaRS; ASPN; human.
DR   GeneWiki; Asporin; -.
DR   GenomeRNAi; 54829; -.
DR   Pharos; Q9BXN1; Tbio.
DR   PRO; PR:Q9BXN1; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q9BXN1; Protein.
DR   Bgee; ENSG00000106819; Expressed in tendon of biceps brachii and 181 other cell types or tissues.
DR   ExpressionAtlas; Q9BXN1; baseline and differential.
DR   GO; GO:0042995; C:cell projection; IEA:Ensembl.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0030282; P:bone mineralization; IDA:UniProtKB.
DR   GO; GO:0070171; P:negative regulation of tooth mineralization; ISS:UniProtKB.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:1902617; P:response to fluoride; IEA:Ensembl.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000372; LRRNT.
DR   InterPro; IPR016352; SLRP_I_decor/aspor/byglycan.
DR   PANTHER; PTHR45712; AGAP008170-PA; 1.
DR   PANTHER; PTHR45712:SF2; ASPORIN; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF01462; LRRNT; 1.
DR   PIRSF; PIRSF002490; SLRP_I; 1.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 7.
DR   Genevisible; Q9BXN1; HS.
PE   1: Evidence at protein level;
KW   Biomineralization; Calcium; Direct protein sequencing; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW   Reference proteome; Repeat; Secreted; Signal; Triplet repeat expansion.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   PROPEP          15..32
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000032727"
FT   CHAIN           33..380
FT                   /note="Asporin"
FT                   /id="PRO_0000032728"
FT   DOMAIN          66..102
FT                   /note="LRRNT"
FT   REPEAT          103..124
FT                   /note="LRR 1"
FT   REPEAT          127..148
FT                   /note="LRR 2"
FT   REPEAT          151..173
FT                   /note="LRR 3"
FT   REPEAT          174..193
FT                   /note="LRR 4"
FT   REPEAT          196..219
FT                   /note="LRR 5"
FT   REPEAT          242..263
FT                   /note="LRR 6"
FT   REPEAT          266..287
FT                   /note="LRR 7"
FT   REPEAT          290..312
FT                   /note="LRR 8"
FT   REPEAT          313..334
FT                   /note="LRR 9"
FT   REPEAT          335..357
FT                   /note="LRR 10"
FT   REPEAT          358..380
FT                   /note="LRR 11"
FT   REGION          35..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..212
FT                   /note="Interaction with TGFB1"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        35..55
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        55
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000305|PubMed:11152692"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:11152692,
FT                   ECO:0000269|PubMed:19159218"
FT   DISULFID        75..81
FT                   /evidence="ECO:0000269|PubMed:19589127"
FT   DISULFID        79..88
FT                   /evidence="ECO:0000269|PubMed:19589127"
FT   DISULFID        333..366
FT                   /evidence="ECO:0000269|PubMed:19589127"
FT   CONFLICT        238..243
FT                   /note="GLPPTL -> DNLPSF (in Ref. 3; BAB55060)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   380 AA;  43417 MW;  2746A977FDCEBA5F CRC64;
     MKEYVLLLFL ALCSAKPFFS PSHIALKNMM LKDMEDTDDD DDDDDDDDDD DEDNSLFPTR
     EPRSHFFPFD LFPMCPFGCQ CYSRVVHCSD LGLTSVPTNI PFDTRMLDLQ NNKIKEIKEN
     DFKGLTSLYG LILNNNKLTK IHPKAFLTTK KLRRLYLSHN QLSEIPLNLP KSLAELRIHE
     NKVKKIQKDT FKGMNALHVL EMSANPLDNN GIEPGAFEGV TVFHIRIAEA KLTSVPKGLP
     PTLLELHLDY NKISTVELED FKRYKELQRL GLGNNKITDI ENGSLANIPR VREIHLENNK
     LKKIPSGLPE LKYLQIIFLH SNSIARVGVN DFCPTVPKMK KSLYSAISLF NNPVKYWEMQ
     PATFRCVLSR MSVQLGNFGM
//