SPON2_MOUSE
ID SPON2_MOUSE Reviewed; 330 AA.
AC Q8BMS2; Q6SJD8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Spondin-2;
DE AltName: Full=Mindin;
DE Flags: Precursor;
GN Name=Spon2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP FUNCTION.
RC TISSUE=Thymus;
RX PubMed=14691481; DOI=10.1038/ni1021;
RA He Y.-W., Li H., Zhang J., Hsu C.-L., Lin E., Zhang N., Guo J.,
RA Forbush K.A., Bevan M.J.;
RT "The extracellular matrix protein mindin is a pattern-recognition molecule
RT for microbial pathogens.";
RL Nat. Immunol. 5:88-97(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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. Binds bacterial lipopolysaccharide. Essential in the
CC initiation of the innate immune response and represents a unique
CC pattern-recognition molecule in the ECM for microbial pathogens.
CC {ECO:0000269|PubMed:14691481}.
CC -!- SUBUNIT: Monomer. Interacts with integrin (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:14691481}.
CC -!- TISSUE SPECIFICITY: Detected in heart, lung, thymus, spleen and lymph
CC node. {ECO:0000269|PubMed:14691481}.
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DR EMBL; AK028987; BAC26226.1; -; mRNA.
DR EMBL; AY457639; AAR20834.1; -; mRNA.
DR CCDS; CCDS19200.1; -.
DR RefSeq; NP_598664.3; NM_133903.3.
DR RefSeq; XP_006503685.1; XM_006503622.2.
DR AlphaFoldDB; Q8BMS2; -.
DR SMR; Q8BMS2; -.
DR STRING; 10090.ENSMUSP00000042701; -.
DR GlyGen; Q8BMS2; 1 site.
DR iPTMnet; Q8BMS2; -.
DR PhosphoSitePlus; Q8BMS2; -.
DR CPTAC; non-CPTAC-3948; -.
DR MaxQB; Q8BMS2; -.
DR PaxDb; Q8BMS2; -.
DR PRIDE; Q8BMS2; -.
DR ProteomicsDB; 261575; -.
DR Antibodypedia; 22210; 310 antibodies from 35 providers.
DR DNASU; 100689; -.
DR Ensembl; ENSMUST00000046186; ENSMUSP00000042701; ENSMUSG00000037379.
DR GeneID; 100689; -.
DR KEGG; mmu:100689; -.
DR UCSC; uc008xai.2; mouse.
DR CTD; 10417; -.
DR MGI; MGI:1923724; Spon2.
DR VEuPathDB; HostDB:ENSMUSG00000037379; -.
DR eggNOG; KOG3539; Eukaryota.
DR GeneTree; ENSGT00940000159900; -.
DR HOGENOM; CLU_034407_0_0_1; -.
DR InParanoid; Q8BMS2; -.
DR OMA; PQDRITQ; -.
DR OrthoDB; 517669at2759; -.
DR PhylomeDB; Q8BMS2; -.
DR TreeFam; TF326913; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 100689; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8BMS2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BMS2; protein.
DR Bgee; ENSMUSG00000037379; Expressed in epithelium of lens and 117 other tissues.
DR ExpressionAtlas; Q8BMS2; baseline and differential.
DR Genevisible; Q8BMS2; MM.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0003823; F:antigen binding; IDA:MGI.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR GO; GO:0050832; P:defense response to fungus; IMP:MGI.
DR GO; GO:0051607; P:defense response to virus; IMP:MGI.
DR GO; GO:0043152; P:induction of bacterial agglutination; IDA:MGI.
DR GO; GO:0045087; P:innate immune response; IMP:MGI.
DR GO; GO:0002448; P:mast cell mediated immunity; IMP:MGI.
DR GO; GO:0008228; P:opsonization; IDA:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:MGI.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IDA:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
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_0000035871"
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"
FT CONFLICT 242
FT /note="R -> Q (in Ref. 2; BAC26226)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 35965 MW; 581F16E6A55F9A07 CRC64;
MENVSLALGR ALWVFLLAMI GSTTSQPLGG ESVCTARPLA RYSITFIGKW SQTAFPKQYP
LFRPPAQWSS LLGAAHSSDY SMWRKNEYVS NGLRDFAERG EAWALMKEIE AAGEKLQSVH
AVFSAPAIPS GTGQTSTELE VHPRHSLVSF VVRIVPSPDW FVGIDSLDLC EGGRWKEQVV
LDLYPHDAGT DSGFTFSSPN FATIPQDTVT EITASSPSHP ANSFYYPRLK SLPPIAKVTF
VRLQQSPRAF APPSLDLASR GNEIVDSLSV PETPLDCEVS LWSSWGLCGG PCGKLGAKSR
TRYVRVQPAN NGTPCPELEE EAECAPDNCV
