TICN2_MOUSE
ID TICN2_MOUSE Reviewed; 423 AA.
AC Q9ER58;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Testican-2;
DE AltName: Full=SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 2;
DE Flags: Precursor;
GN Name=Spock2; Synonyms=Ticn2;
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].
RC TISSUE=Brain;
RA Hartmann U., Paulsson M., Maurer P.;
RT "Cloning of mouse testican-2.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May participate in diverse steps of neurogenesis. Binds
CC calcium (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Brain specific.
CC -!- PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate.
CC {ECO:0000250}.
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DR EMBL; AJ278999; CAC08507.1; -; mRNA.
DR EMBL; BC057324; AAH57324.1; -; mRNA.
DR CCDS; CCDS35910.1; -.
DR RefSeq; NP_443720.1; NM_052994.2.
DR AlphaFoldDB; Q9ER58; -.
DR SMR; Q9ER58; -.
DR STRING; 10090.ENSMUSP00000113115; -.
DR MEROPS; I31.954; -.
DR GlyConnect; 2758; 7 N-Linked glycans (1 site).
DR GlyGen; Q9ER58; 3 sites, 7 N-linked glycans (1 site).
DR PhosphoSitePlus; Q9ER58; -.
DR MaxQB; Q9ER58; -.
DR PaxDb; Q9ER58; -.
DR PRIDE; Q9ER58; -.
DR ProteomicsDB; 259024; -.
DR Antibodypedia; 29217; 101 antibodies from 24 providers.
DR DNASU; 94214; -.
DR Ensembl; ENSMUST00000121820; ENSMUSP00000113115; ENSMUSG00000058297.
DR GeneID; 94214; -.
DR KEGG; mmu:94214; -.
DR UCSC; uc007fek.1; mouse.
DR CTD; 9806; -.
DR MGI; MGI:1891351; Spock2.
DR VEuPathDB; HostDB:ENSMUSG00000058297; -.
DR eggNOG; KOG3555; Eukaryota.
DR GeneTree; ENSGT00940000157107; -.
DR HOGENOM; CLU_037217_1_0_1; -.
DR InParanoid; Q9ER58; -.
DR OMA; SACKLEQ; -.
DR OrthoDB; 1235834at2759; -.
DR PhylomeDB; Q9ER58; -.
DR TreeFam; TF317779; -.
DR BioGRID-ORCS; 94214; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9ER58; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9ER58; protein.
DR Bgee; ENSMUSG00000058297; Expressed in habenula and 199 other tissues.
DR ExpressionAtlas; Q9ER58; baseline and differential.
DR Genevisible; Q9ER58; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IDA:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; 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 1: Evidence at protein level;
KW Calcium; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Heparan sulfate; Phosphoprotein; Proteoglycan; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..423
FT /note="Testican-2"
FT /id="PRO_0000026702"
FT DOMAIN 130..182
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 309..375
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 387..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..416
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92563"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
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 136..166
FT /evidence="ECO:0000250"
FT DISULFID 139..159
FT /evidence="ECO:0000250"
FT DISULFID 148..180
FT /evidence="ECO:0000250"
FT DISULFID 312..336
FT /evidence="ECO:0000250"
FT DISULFID 347..354
FT /evidence="ECO:0000250"
FT DISULFID 356..375
FT /evidence="ECO:0000250"
SQ SEQUENCE 423 AA; 46863 MW; 20D73E3DB3BC1A15 CRC64;
MRAPGSGRLA LPLLLLAVVA LAEGDAKGLK EGETPGNFME DEQWLSSISQ YSGKIKHWNR
FRDEVEDDYI KSWEDNQQGD EALDTTKDPC QKVKCSRHKV CVAQGYQRAM CISRKKLEHR
IKQPSLKLHG GKDSVCKPCH MAQLASVCGS DGHTYSSVCK LEQQACLSSK QLAVRCEGPC
PCPTEQSTAS TTDSKSETCT GQDLADLGDR LRDWFQLLRE NSKQNGSANS ATNPAGLDKS
LGASCKDSIG WMFSKLDTSG DLFLDQTELA AINLDKYEVC IRPFFNSCDT YKDGRVSTAE
WCFCFWREKP PCLAELERTQ IQEAAKKKPG VFIPSCDEDG YYRKMQCDQS RGDCWCVDQL
GLELTGTRMH GTPDCDDIVG FSGDFGSGVG WEDEEEKETE EAGEEAEEEE GEAGEADDGG
YIW
