ID   ASPN_BOVIN              Reviewed;         370 AA.
AC   Q3ZBN5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Asporin;
DE   Flags: Precursor;
GN   Name=ASPN;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class I subfamily. {ECO:0000305}.
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DR   EMBL; BC103199; AAI03200.1; -; mRNA.
DR   RefSeq; NP_001029481.1; NM_001034309.2.
DR   AlphaFoldDB; Q3ZBN5; -.
DR   SMR; Q3ZBN5; -.
DR   STRING; 9913.ENSBTAP00000034926; -.
DR   PaxDb; Q3ZBN5; -.
DR   PeptideAtlas; Q3ZBN5; -.
DR   Ensembl; ENSBTAT00000035046; ENSBTAP00000034926; ENSBTAG00000011847.
DR   GeneID; 507990; -.
DR   KEGG; bta:507990; -.
DR   CTD; 54829; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011847; -.
DR   VGNC; VGNC:26222; ASPN.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000157444; -.
DR   HOGENOM; CLU_000288_186_0_1; -.
DR   InParanoid; Q3ZBN5; -.
DR   OMA; DFIRYKN; -.
DR   OrthoDB; 826997at2759; -.
DR   TreeFam; TF334562; -.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000011847; Expressed in uterine cervix and 104 other tissues.
DR   GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0005518; F:collagen binding; IEA:InterPro.
DR   GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR   GO; GO:0070171; P:negative regulation of tooth mineralization; IEA:Ensembl.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; 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; 8.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS51450; LRR; 7.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..370
FT                   /note="Asporin"
FT                   /id="PRO_0000287716"
FT   DOMAIN          56..92
FT                   /note="LRRNT"
FT   REPEAT          93..114
FT                   /note="LRR 1"
FT   REPEAT          117..138
FT                   /note="LRR 2"
FT   REPEAT          141..163
FT                   /note="LRR 3"
FT   REPEAT          164..183
FT                   /note="LRR 4"
FT   REPEAT          186..209
FT                   /note="LRR 5"
FT   REPEAT          232..253
FT                   /note="LRR 6"
FT   REPEAT          256..277
FT                   /note="LRR 7"
FT   REPEAT          280..302
FT                   /note="LRR 8"
FT   REPEAT          303..324
FT                   /note="LRR 9"
FT   REPEAT          332..354
FT                   /note="LRR 10"
FT   REPEAT          355..370
FT                   /note="LRR 11"
FT   CARBOHYD        45
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        65..71
FT                   /evidence="ECO:0000250|UniProtKB:P21809"
FT   DISULFID        69..78
FT                   /evidence="ECO:0000250|UniProtKB:P21809"
FT   DISULFID        323..356
FT                   /evidence="ECO:0000250|UniProtKB:P21809"
SQ   SEQUENCE   370 AA;  42119 MW;  DDBDA88F5F8DC190 CRC64;
     MKVYVLLVFL TLCSAKPLFH PSYLTLKNLM LKDMEDEGDS DADNSLFPTR EPINPFFPFD
     LFSTCPFGCQ CYSRVVHCSD LGLSSVPSNI PFDTRMVDLQ NNKIKEIKEN DFKGLTSLYA
     LILNNNKLTK IHPKAFLTTK KLRRLYLSHN QLSEIPLNLP KSLAELRIHD NKVKKIQKAT
     FKGMNALHVL EMSANPLDNN GIEPGAFEGV TVFHIRIAEA KLTSIPKELP STLLELHLDY
     NKISVVELED FKRYKDLQRL GLGNNRITDI ENGSLANIPR VREIHLENNK LKKVPSGLQE
     LKYLQIIFLH SNSITKVGVN DFCPTVPKMK KSLYSAISLS NNPVKYWEVQ PATFRCVLSR
     MSVQLGNFRK