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Testican-3 (SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 3)

 TICN3_MOUSE             Reviewed;         436 AA.
Q8BKV0; Q9ER59;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 2.
30-AUG-2017, entry version 117.
RecName: Full=Testican-3;
AltName: Full=SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 3;
Flags: Precursor;
Name=Spock3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Mueller R., Paulsson M., Maurer P., Hartmann U.;
"Cloning of mouse testican-3.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Hippocampus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: May participate in diverse steps of neurogenesis.
Inhibits the processing of pro-matrix metalloproteinase 2 (MMP-2)
by MT1-MMP and MT3-MMP. May interfere with tumor invasion (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8BKV0-1; Sequence=Displayed;
Name=2;
IsoId=Q8BKV0-2; Sequence=VSP_013633;
-!- TISSUE SPECIFICITY: Expressed in brain.
-!- PTM: Contains chondroitin sulfate and heparan sulfate O-linked
oligosaccharides. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AJ278998; CAC08506.1; -; mRNA.
EMBL; AK013644; BAB28935.1; -; mRNA.
EMBL; AK049843; BAC33951.1; -; mRNA.
EMBL; BC017601; AAH17601.1; -; mRNA.
EMBL; BC053334; AAH53334.1; -; mRNA.
CCDS; CCDS22326.1; -. [Q8BKV0-1]
CCDS; CCDS57622.1; -. [Q8BKV0-2]
RefSeq; NP_001239549.1; NM_001252620.1. [Q8BKV0-1]
RefSeq; NP_001239550.1; NM_001252621.1. [Q8BKV0-2]
RefSeq; NP_076178.1; NM_023689.3. [Q8BKV0-1]
RefSeq; XP_006509581.1; XM_006509518.1. [Q8BKV0-2]
UniGene; Mm.334552; -.
ProteinModelPortal; Q8BKV0; -.
SMR; Q8BKV0; -.
STRING; 10090.ENSMUSP00000091192; -.
MEROPS; I31.007; -.
iPTMnet; Q8BKV0; -.
PhosphoSitePlus; Q8BKV0; -.
PaxDb; Q8BKV0; -.
PRIDE; Q8BKV0; -.
Ensembl; ENSMUST00000093480; ENSMUSP00000091192; ENSMUSG00000054162. [Q8BKV0-1]
Ensembl; ENSMUST00000117377; ENSMUSP00000113797; ENSMUSG00000054162. [Q8BKV0-2]
Ensembl; ENSMUST00000118003; ENSMUSP00000113683; ENSMUSG00000054162. [Q8BKV0-1]
Ensembl; ENSMUST00000119068; ENSMUSP00000112930; ENSMUSG00000054162. [Q8BKV0-1]
GeneID; 72902; -.
KEGG; mmu:72902; -.
UCSC; uc009lur.1; mouse. [Q8BKV0-2]
UCSC; uc009lus.2; mouse. [Q8BKV0-1]
CTD; 50859; -.
MGI; MGI:1920152; Spock3.
eggNOG; KOG3555; Eukaryota.
eggNOG; ENOG410Y6A8; LUCA.
GeneTree; ENSGT00510000046429; -.
HOGENOM; HOG000293295; -.
HOVERGEN; HBG026595; -.
InParanoid; Q8BKV0; -.
KO; K08136; -.
OMA; RLTHSMK; -.
OrthoDB; EOG091G086I; -.
TreeFam; TF317779; -.
Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
PRO; PR:Q8BKV0; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000054162; -.
Genevisible; Q8BKV0; MM.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISO:MGI.
GO; GO:0010951; P:negative regulation of endopeptidase activity; ISO:MGI.
GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IDA:MGI.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 4.10.800.10; -; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR002350; Kazal_dom.
InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
InterPro; IPR000716; Thyroglobulin_1.
Pfam; PF07648; Kazal_2; 1.
Pfam; PF10591; SPARC_Ca_bdg; 1.
Pfam; PF00086; Thyroglobulin_1; 1.
SMART; SM00280; KAZAL; 1.
SMART; SM00211; TY; 1.
SUPFAM; SSF100895; SSF100895; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF57610; SSF57610; 1.
PROSITE; PS51465; KAZAL_2; 1.
PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
2: Evidence at transcript level;
Alternative splicing; Calcium; Complete proteome; Disulfide bond;
Extracellular matrix; Glycoprotein; Heparan sulfate;
Metalloenzyme inhibitor; Metalloprotease inhibitor;
Protease inhibitor; Proteoglycan; Reference proteome; Secreted;
Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 436 Testican-3.
/FTId=PRO_0000026704.
DOMAIN 133 185 Kazal-like. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 314 380 Thyroglobulin type-1.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
COMPBIAS 394 436 Asp-rich.
CARBOHYD 387 387 O-linked (Xyl...) (glycosaminoglycan)
serine. {ECO:0000255}.
CARBOHYD 392 392 O-linked (Xyl...) (glycosaminoglycan)
serine. {ECO:0000255}.
DISULFID 90 101 {ECO:0000250}.
DISULFID 95 111 {ECO:0000250}.
DISULFID 139 169 {ECO:0000250}.
DISULFID 142 162 {ECO:0000250}.
DISULFID 151 183 {ECO:0000250}.
DISULFID 317 341 {ECO:0000250}.
DISULFID 352 359 {ECO:0000250}.
DISULFID 361 380 {ECO:0000250}.
VAR_SEQ 64 66 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_013633.
SEQUENCE 436 AA; 49098 MW; 6FFD8A13815E9BC5 CRC64;
MLKVSALLCV CAAAWCSQTL AAAAAVAVAG GRSDGGNFLD EKQWLTTISQ YDKEVGQWNK
FRDEVEDDYF RTWNPGKPFD QALDPAKDPC LKTKCSRHKV CITQDAQTAL CISHRRLTHS
MKEVGGSHKQ WRGLPSSTCK PCPIAYASPV CGSDGHSYSS QCKLEYQACV LGKQISIKCE
GRCPCPSDKS MNIGRNVKRA CSDLEFREVA NRLRDWFKAL HESGSQNKKT KALLRPERSR
FDTSILPICK DSLGWMFNRL DTNYDLLLDQ SELGSIYLDK NEQCTKAFFN SCDTYKDSLI
SNNEWCYCFQ RQQDPPCHTE LSNIQKRQGI KKLLGQYIPL CDEDGYYKPT QCHGSVGQCW
CVDRYGNEVV GSRINGVADC AIDFEISGDF ASGDFREWTD DEGEEDDIMN DKDDIEDDDE
DEGDDDDDGD VHDGYI


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