TICN3_MOUSE
ID TICN3_MOUSE Reviewed; 436 AA.
AC Q8BKV0; Q9ER59;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Testican-3;
DE AltName: Full=SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 3;
DE Flags: Precursor;
GN Name=Spock3;
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] (ISOFORM 1).
RC TISSUE=Brain;
RA Mueller R., Paulsson M., Maurer P., Hartmann U.;
RT "Cloning of mouse testican-3.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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: May participate in diverse steps of neurogenesis. Inhibits
CC the processing of pro-matrix metalloproteinase 2 (MMP-2) by MT1-MMP and
CC MT3-MMP. May interfere with tumor invasion (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BKV0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BKV0-2; Sequence=VSP_013633;
CC -!- TISSUE SPECIFICITY: Expressed in brain.
CC -!- PTM: Contains chondroitin sulfate and heparan sulfate O-linked
CC oligosaccharides. {ECO:0000250}.
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DR EMBL; AJ278998; CAC08506.1; -; mRNA.
DR EMBL; AK013644; BAB28935.1; -; mRNA.
DR EMBL; AK049843; BAC33951.1; -; mRNA.
DR EMBL; BC017601; AAH17601.1; -; mRNA.
DR EMBL; BC053334; AAH53334.1; -; mRNA.
DR CCDS; CCDS22326.1; -. [Q8BKV0-1]
DR CCDS; CCDS57622.1; -. [Q8BKV0-2]
DR RefSeq; NP_001239549.1; NM_001252620.1. [Q8BKV0-1]
DR RefSeq; NP_001239550.1; NM_001252621.1. [Q8BKV0-2]
DR RefSeq; NP_076178.1; NM_023689.3. [Q8BKV0-1]
DR RefSeq; XP_006509581.1; XM_006509518.1.
DR AlphaFoldDB; Q8BKV0; -.
DR SMR; Q8BKV0; -.
DR STRING; 10090.ENSMUSP00000112930; -.
DR MEROPS; I01.980; -.
DR MEROPS; I31.007; -.
DR GlyGen; Q8BKV0; 2 sites.
DR iPTMnet; Q8BKV0; -.
DR PhosphoSitePlus; Q8BKV0; -.
DR MaxQB; Q8BKV0; -.
DR PaxDb; Q8BKV0; -.
DR PRIDE; Q8BKV0; -.
DR ProteomicsDB; 259388; -. [Q8BKV0-1]
DR ProteomicsDB; 259389; -. [Q8BKV0-2]
DR Antibodypedia; 28345; 133 antibodies from 19 providers.
DR DNASU; 72902; -.
DR Ensembl; ENSMUST00000093480; ENSMUSP00000091192; ENSMUSG00000054162. [Q8BKV0-1]
DR Ensembl; ENSMUST00000117377; ENSMUSP00000113797; ENSMUSG00000054162. [Q8BKV0-2]
DR Ensembl; ENSMUST00000118003; ENSMUSP00000113683; ENSMUSG00000054162. [Q8BKV0-1]
DR Ensembl; ENSMUST00000119068; ENSMUSP00000112930; ENSMUSG00000054162. [Q8BKV0-1]
DR GeneID; 72902; -.
DR KEGG; mmu:72902; -.
DR UCSC; uc009lur.1; mouse. [Q8BKV0-2]
DR UCSC; uc009lus.2; mouse. [Q8BKV0-1]
DR CTD; 50859; -.
DR MGI; MGI:1920152; Spock3.
DR VEuPathDB; HostDB:ENSMUSG00000054162; -.
DR eggNOG; KOG3555; Eukaryota.
DR GeneTree; ENSGT00940000157828; -.
DR HOGENOM; CLU_037217_1_0_1; -.
DR InParanoid; Q8BKV0; -.
DR OMA; LDKNEHC; -.
DR OrthoDB; 1235834at2759; -.
DR PhylomeDB; Q8BKV0; -.
DR TreeFam; TF317779; -.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 72902; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Spock3; mouse.
DR PRO; PR:Q8BKV0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BKV0; protein.
DR Bgee; ENSMUSG00000054162; Expressed in caudate-putamen and 129 other tissues.
DR Genevisible; Q8BKV0; MM.
DR GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; ISO:MGI.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IDA:MGI.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF10591; SPARC_Ca_bdg; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR SMART; SM00280; KAZAL; 1.
DR SMART; SM00211; TY; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF57610; SSF57610; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Heparan sulfate; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Protease inhibitor; Proteoglycan;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..436
FT /note="Testican-3"
FT /id="PRO_0000026704"
FT DOMAIN 133..185
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 314..380
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 393..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..436
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 387
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT DISULFID 90..101
FT /evidence="ECO:0000250"
FT DISULFID 95..111
FT /evidence="ECO:0000250"
FT DISULFID 139..169
FT /evidence="ECO:0000250"
FT DISULFID 142..162
FT /evidence="ECO:0000250"
FT DISULFID 151..183
FT /evidence="ECO:0000250"
FT DISULFID 317..341
FT /evidence="ECO:0000250"
FT DISULFID 352..359
FT /evidence="ECO:0000250"
FT DISULFID 361..380
FT /evidence="ECO:0000250"
FT VAR_SEQ 64..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013633"
SQ 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
