ASPN_HUMAN
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 03-AUG-2022, entry version 186.
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};
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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; 5.
DR STRING; 9606.ENSP00000364694; -.
DR GlyConnect; 1019; 46 N-Linked glycans (1 site).
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; Q9BXN1; -.
DR PeptideAtlas; Q9BXN1; -.
DR PRIDE; Q9BXN1; -.
DR ProteomicsDB; 79461; -.
DR Antibodypedia; 2015; 201 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 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; DFIRYKN; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9BXN1; -.
DR TreeFam; TF334562; -.
DR PathwayCommons; Q9BXN1; -.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR BioGRID-ORCS; 54829; 1 hit in 230 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 179 other tissues.
DR ExpressionAtlas; Q9BXN1; baseline and differential.
DR Genevisible; Q9BXN1; HS.
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:0005518; F:collagen binding; IEA:InterPro.
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; -; 1.
DR InterPro; IPR028548; Asporin.
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:SF2; PTHR45712:SF2; 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 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 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
