SPON2_RAT
ID SPON2_RAT Reviewed; 330 AA.
AC Q9WV75;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Spondin-2;
DE AltName: Full=Mindin;
DE Flags: Precursor;
GN Name=Spon2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=10409509; DOI=10.1242/dev.126.16.3637;
RA Feinstein Y., Borrell V., Garcia C., Burstyn-Cohen T., Tzarfaty V.,
RA Frumkin A., Nose A., Okamoto H., Higashijima S., Soriano A., Klar A.;
RT "F-spondin and mindin: two structurally and functionally related genes
RT expressed in the hippocampus that promote outgrowth of embryonic
RT hippocampal neurons.";
RL Development 126:3637-3648(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Cell adhesion protein that promotes adhesion and outgrowth of
CC hippocampal embryonic neurons. Binds directly to bacteria and their
CC components and functions as an opsonin for macrophage phagocytosis of
CC bacteria. Essential in the initiation of the innate immune response and
CC represents a unique pattern-recognition molecule in the ECM for
CC microbial pathogens (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10409509}.
CC -!- SUBUNIT: Monomer. Interacts with integrin (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the developing hippocampus.
CC {ECO:0000269|PubMed:10409509}.
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; AF155196; AAD38195.1; -; mRNA.
DR EMBL; BC078734; AAH78734.1; -; mRNA.
DR RefSeq; NP_612542.1; NM_138533.3.
DR RefSeq; XP_017454551.1; XM_017599062.1.
DR RefSeq; XP_017454552.1; XM_017599063.1.
DR RefSeq; XP_017460311.1; XM_017604822.1.
DR RefSeq; XP_017460312.1; XM_017604823.1.
DR AlphaFoldDB; Q9WV75; -.
DR SMR; Q9WV75; -.
DR STRING; 10116.ENSRNOP00000008262; -.
DR GlyGen; Q9WV75; 1 site.
DR PaxDb; Q9WV75; -.
DR PRIDE; Q9WV75; -.
DR Ensembl; ENSRNOT00000008262; ENSRNOP00000008262; ENSRNOG00000006033.
DR GeneID; 171569; -.
DR KEGG; rno:171569; -.
DR CTD; 10417; -.
DR RGD; 708584; Spon2.
DR eggNOG; KOG3539; Eukaryota.
DR GeneTree; ENSGT00940000159900; -.
DR HOGENOM; CLU_034407_0_0_1; -.
DR InParanoid; Q9WV75; -.
DR OMA; PQDRITQ; -.
DR OrthoDB; 517669at2759; -.
DR PhylomeDB; Q9WV75; -.
DR Reactome; R-RNO-5173214; O-glycosylation of TSR domain-containing proteins.
DR PRO; PR:Q9WV75; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000006033; Expressed in esophagus and 18 other tissues.
DR Genevisible; Q9WV75; RN.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0003823; F:antigen binding; ISO:RGD.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IDA:RGD.
DR GO; GO:0007155; P:cell adhesion; IDA:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0050832; P:defense response to fungus; ISO:RGD.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0043152; P:induction of bacterial agglutination; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; ISO:RGD.
DR GO; GO:0002448; P:mast cell mediated immunity; ISO:RGD.
DR GO; GO:0008228; P:opsonization; ISO:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR Gene3D; 2.20.100.10; -; 1.
DR Gene3D; 2.60.40.2130; -; 1.
DR InterPro; IPR009465; Spondin_N.
DR InterPro; IPR038678; Spondin_N_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR044004; TSP1_spondin_dom.
DR Pfam; PF06468; Spond_N; 1.
DR Pfam; PF19028; TSP1_spondin; 1.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS51020; SPONDIN; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Immunity; Innate immunity; Metal-binding; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..330
FT /note="Spondin-2"
FT /id="PRO_0000035872"
FT DOMAIN 30..220
FT /note="Spondin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00364"
FT DOMAIN 276..330
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q9BUD6"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9BUD6"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9BUD6"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9BUD6"
FT SITE 140
FT /note="Important for metal ion-dependent interaction with
FT integrin"
FT /evidence="ECO:0000250|UniProtKB:Q9BUD6"
FT CARBOHYD 282
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:Q9BUD6"
FT DISULFID 34..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 330 AA; 36015 MW; ECBCF07A0345A83A CRC64;
MENVSFSLDR TLWVFLLAML GSTAGQPLGG ESVCTARPLA RYSITFTGKW SQTAFPKQYP
LFRPPAQWSS LLGAAHSSDY SMWRKNEYVS NGLRDFAERG EAWALMKEIE AAGEKLQSVH
AVFSAPAVPS GTGQTSAELE VHPRHSLVSF VVRIVPSPDW FVGIDSLDLC EGGRWKEQVV
LDLYPHDAGT DSGFTFSSPN FATIPQDTVT EITASSPSHP ANSFYYPRLK SLPPIAKVTF
VRLRQSPRAF APPSLDLASR GNEIVDSLSV PETPLDCEVS LWSSWGLCGG PCGKLGAKSR
TRYVRVQPAN NGTPCPELEE EAECAPDNCV
