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Protein

Asporin

Gene

Aspn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds calcium and plays a role in osteoblast-driven collagen biomineralization activity (By similarity). Critical regulator of TGF-beta in articular cartilage and plays an essential role in cartilage homeostasis and osteoarthritis (OA) pathogenesis. Negatively regulates chondrogenesis in the articular cartilage by blocking the TGF-beta/receptor interaction on the cell surface and inhibiting the canonical TGF-beta/Smad signal. Negatively regulates periodontal ligament (PDL) differentiation and mineralization to ensure that the PDL is not ossified and to maintain homeostasis of the tooth-supporting system. Inhibits BMP2-induced cytodifferentiation of PDL cells by preventing its binding to BMPR1B/BMP type-1B receptor, resulting in inhibition of BMP-dependent activation of SMAD proteins. Inhibits the interaction between TGFB1 and TGF-beta receptor type II in the presence of heparin/heparan sulfate in vitro.By similarity4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Biomineralization

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Asporin
Alternative name(s):
Periodontal ligament-associated protein 1
Short name:
PLAP-1
Gene namesi
Name:Aspn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1913945. Aspn.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi170 – 1701R → E: Partial inhibition of BMP2-induced cytodifferentiation; when associated with E-219. 1 Publication
Mutagenesisi194 – 1941E → G or K: Rescues the inhibitory effects of ASPN on BMP2-induced cytodifferentiation. 1 Publication
Mutagenesisi219 – 2191R → E: Partial inhibition of BMP2-induced cytodifferentiation; when associated with E-170. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence analysisAdd
BLAST
Propeptidei16 – 3217Sequence analysisPRO_0000032729Add
BLAST
Chaini33 – 373341AsporinPRO_0000032730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi48 – 481O-linked (GalNAc...)By similarity
Disulfide bondi68 ↔ 74By similarity
Disulfide bondi72 ↔ 81By similarity
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence analysis
Disulfide bondi326 ↔ 359By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ99MQ4.
PaxDbiQ99MQ4.
PRIDEiQ99MQ4.

PTM databases

PhosphoSiteiQ99MQ4.

Expressioni

Tissue specificityi

Higher expression in heart, also detected in kidney, stomach, testes, and skin but only weakly in lung, skeletal muscle, small intestine, and thymus. Expressed specifically and predominantly in the periodontal ligament (PDL). During tooth development, strong expression is seen in the dental follicle, which is the progenitor tissue that forms cementum, alveolar bone, and the PDL. Expressed in the perichondria of the maxilla, mandible, vertebrae, and long bones. Predominantly expressed in the perichondrium/periosteum of long bones (at protein level).2 Publications

Developmental stagei

At 12.5 dpc, it is present in the mandibular as well as maxillary components of the first branchial arch. Also detected in the thoracic body wall adjacent to the heart. At 13.5 dpc, it is detected in the mesenchyme lateral to Meckel's cartilage. Pronounced expression is observed in the perichondrium of the humerus, ribs, and scapula. At 14.5 dpc, it is detected in the mesenchymal condensations lateral to Meckel's cartilage, in the perichondrium surrounding the central cartilaginous elements of the vertebra and also in the dermal mesenchyme. At 15.5 dpc, it is expressed in the perichondrium/periosteum of the long bones (i.e. femur, tibia, and fibula), some of the flat bones at the base of the skull (i.e. sphenoid bone), ribs, clavicle, and vertebrae. Also detected in the intramembranous bones of the maxilla and mandible (alveolar bone) and a strong expression is observed in sagittal sections of the subcutaneous muscles or panniculus carnosus of the thorax, trunk, and head/ neck (platysma muscle) region. Very little expression is detected in the major parenchymal organs (with the exception of the large bronchi of the lung). Its expression is prominent in the developing mouse skeleton, particularly in the perichondrium/periosteum of cartilage/bone, and is also found in other specialized connective tissues such as tendon, sclera, the connective tissue sheath surrounding muscle and dermis. In the sclera of the eye it is first detected at 15.5 dpc and stronger expression was detected at 17.5 dpc.1 Publication

Inductioni

By TGFB1. Induction requires ALK5 kinase activity and SMAD3.1 Publication

Gene expression databases

BgeeiENSMUSG00000021388.
CleanExiMM_ASPN.
ExpressionAtlasiQ99MQ4. baseline and differential.
GenevisibleiQ99MQ4. MM.

Interactioni

Subunit structurei

Interacts with type I collagen. DCN can inhibit collagen binding (By similarity). Interacts with TGFB1, TGFB2 and TGFB3. DCN, BGN, and FMOD inhibit binding to TGFB1. Interacts with BMP2. Interacts in vitro with type II collagen.By similarity3 Publications

Protein-protein interaction databases

IntActiQ99MQ4. 1 interaction.
MINTiMINT-4088506.
STRINGi10090.ENSMUSP00000021820.

Structurei

3D structure databases

ProteinModelPortaliQ99MQ4.
SMRiQ99MQ4. Positions 68-370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 9537LRRNTAdd
BLAST
Repeati96 – 11722LRR 1Add
BLAST
Repeati120 – 14122LRR 2Add
BLAST
Repeati144 – 16623LRR 3Add
BLAST
Repeati167 – 18620LRR 4Add
BLAST
Repeati189 – 21224LRR 5Add
BLAST
Repeati235 – 25521LRR 6Add
BLAST
Repeati259 – 28022LRR 7Add
BLAST
Repeati283 – 30523LRR 8Add
BLAST
Repeati306 – 32722LRR 9Add
BLAST
Repeati328 – 34922LRR 10Add
BLAST
Repeati350 – 37324LRR 11Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni159 – 20547Interaction with TGFB1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi36 – 4611Poly-AspAdd
BLAST
Compositional biasi68 – 8114Cys-richAdd
BLAST

Domaini

The repeats LRR 9, LRR 10 and LRR 11 are involved in binding type I collagen. The poly-Asp region is involved in binding calcium (By similarity). The LRR 5 repeat can inhibit BMP2-induced cytodifferentiation and may be involved in the interaction with BMP2.By similarity1 Publication

Sequence similaritiesi

Contains 11 LRR (leucine-rich) repeats.Curated
Contains 1 LRRNT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000261690.
HOVERGENiHBG016052.
InParanoidiQ99MQ4.
KOiK08120.
OMAiDFIRYKN.
OrthoDBiEOG091G044B.
PhylomeDBiQ99MQ4.
TreeFamiTF334562.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR028548. Asporin.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR016352. SLRP_I_decor/aspor/byglycan.
[Graphical view]
PANTHERiPTHR24369:SF10. PTHR24369:SF10. 1 hit.
PfamiPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
PIRSFiPIRSF002490. SLRP_I. 1 hit.
SMARTiSM00369. LRR_TYP. 7 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99MQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEYVMLLLL AVCSAKPFFS PSHTALKNMM LKDMEDTDDD DNDDDDNSLF
60 70 80 90 100
PTKEPVNPFF PFDLFPTCPF GCQCYSRVVH CSDLGLTSVP NNIPFDTRMV
110 120 130 140 150
DLQNNKIKEI KENDFKGLTS LYALILNNNK LTKIHPKTFL TTKKLRRLYL
160 170 180 190 200
SHNQLSEIPL NLPKSLAELR IHDNKVKKIQ KDTFKGMNAL HVLEMSANPL
210 220 230 240 250
ENNGIEPGAF EGVTVFHIRI AEAKLTSIPK GLPPTLLELH LDFNKISTVE
260 270 280 290 300
LEDLKRYREL QRLGLGNNRI TDIENGTFAN IPRVREIHLE HNKLKKIPSG
310 320 330 340 350
LQELKYLQII FLHYNSIAKV GVNDFCPTVP KMKKSLYSAI SLFNNPMKYW
360 370
EIQPATFRCV LGRMSVQLGN VGK
Length:373
Mass (Da):42,573
Last modified:June 1, 2001 - v1
Checksum:iA50C4C82AABCFC35
GO

Sequence cautioni

The sequence AK014504 differs from that shown. Reason: Erroneous termination at position 238. Translated as Glu.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF316825 mRNA. Translation: AAK35162.1.
AK014504 mRNA. No translation available.
BC034888 mRNA. Translation: AAH34888.1.
CCDSiCCDS26503.1.
RefSeqiNP_001165952.1. NM_001172481.1.
NP_079987.2. NM_025711.3.
UniGeneiMm.383216.

Genome annotation databases

EnsembliENSMUST00000021820; ENSMUSP00000021820; ENSMUSG00000021388.
ENSMUST00000177948; ENSMUSP00000136728; ENSMUSG00000021388.
GeneIDi66695.
KEGGimmu:66695.
UCSCiuc007qjm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF316825 mRNA. Translation: AAK35162.1.
AK014504 mRNA. No translation available.
BC034888 mRNA. Translation: AAH34888.1.
CCDSiCCDS26503.1.
RefSeqiNP_001165952.1. NM_001172481.1.
NP_079987.2. NM_025711.3.
UniGeneiMm.383216.

3D structure databases

ProteinModelPortaliQ99MQ4.
SMRiQ99MQ4. Positions 68-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99MQ4. 1 interaction.
MINTiMINT-4088506.
STRINGi10090.ENSMUSP00000021820.

PTM databases

PhosphoSiteiQ99MQ4.

Proteomic databases

MaxQBiQ99MQ4.
PaxDbiQ99MQ4.
PRIDEiQ99MQ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021820; ENSMUSP00000021820; ENSMUSG00000021388.
ENSMUST00000177948; ENSMUSP00000136728; ENSMUSG00000021388.
GeneIDi66695.
KEGGimmu:66695.
UCSCiuc007qjm.2. mouse.

Organism-specific databases

CTDi54829.
MGIiMGI:1913945. Aspn.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000261690.
HOVERGENiHBG016052.
InParanoidiQ99MQ4.
KOiK08120.
OMAiDFIRYKN.
OrthoDBiEOG091G044B.
PhylomeDBiQ99MQ4.
TreeFamiTF334562.

Miscellaneous databases

PROiQ99MQ4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021388.
CleanExiMM_ASPN.
ExpressionAtlasiQ99MQ4. baseline and differential.
GenevisibleiQ99MQ4. MM.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR028548. Asporin.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR016352. SLRP_I_decor/aspor/byglycan.
[Graphical view]
PANTHERiPTHR24369:SF10. PTHR24369:SF10. 1 hit.
PfamiPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
PIRSFiPIRSF002490. SLRP_I. 1 hit.
SMARTiSM00369. LRR_TYP. 7 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 7 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiASPN_MOUSE
AccessioniPrimary (citable) accession number: Q99MQ4
Secondary accession number(s): Q9D6A2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: June 1, 2001
Last modified: September 7, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.