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 27-NOV-2024, entry version 198. 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; 7. DR IntAct; Q9BXN1; 2. DR STRING; 9606.ENSP00000364694; -. DR GlyConnect; 1019; 46 N-Linked glycans (1 site). DR GlyCosmos; Q9BXN1; 3 sites, 45 glycans. DR GlyGen; Q9BXN1; 4 sites, 123 N-linked glycans (1 site), 2 O-linked glycans (2 sites). 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; 199 antibodies from 26 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 FunFam; 3.80.10.10:FF:000038; Biglycan; 1. 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; IPR050333; SLRP. 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. PE 1: Evidence at protein level; KW Biomineralization; Calcium; Direct protein sequencing; Disulfide bond; KW Extracellular matrix; Glycoprotein; Leucine-rich repeat; KW Proteomics identification; Reference proteome; Repeat; Secreted; Signal; KW 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 //