TICN1_MOUSE
ID TICN1_MOUSE Reviewed; 442 AA.
AC Q62288; E9PYW3;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Testican-1;
DE AltName: Full=Protein SPOCK;
DE Flags: Precursor;
GN Name=Spock1; Synonyms=Spock, Ticn1;
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 STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8626787; DOI=10.1074/jbc.271.8.4373;
RA Bonnet F., Perin J.-P., Charbonnier F., Camuzat A., Roussel G.,
RA Nussbaum J.-L., Alliel P.M.;
RT "Structure and cellular distribution of mouse brain testican. Association
RT with the postsynaptic area of hippocampus pyramidal cells.";
RL J. Biol. Chem. 271:4373-4380(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: May play a role in cell-cell and cell-matrix interactions.
CC May contribute to various neuronal mechanisms in the central nervous
CC system.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the postsynaptic area of
CC pyramidal neurons.
CC -!- PTM: Contains chondroitin sulfate and heparan sulfate O-linked
CC oligosaccharides.
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DR EMBL; X92864; CAA63448.1; -; mRNA.
DR EMBL; AC142258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT010428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS79195.1; -.
DR AlphaFoldDB; Q62288; -.
DR SMR; Q62288; -.
DR STRING; 10090.ENSMUSP00000140409; -.
DR MEROPS; I31.006; -.
DR GlyGen; Q62288; 2 sites.
DR PhosphoSitePlus; Q62288; -.
DR MaxQB; Q62288; -.
DR PaxDb; Q62288; -.
DR PeptideAtlas; Q62288; -.
DR PRIDE; Q62288; -.
DR ProteomicsDB; 259188; -.
DR MGI; MGI:105371; Spock1.
DR eggNOG; KOG3555; Eukaryota.
DR InParanoid; Q62288; -.
DR ChiTaRS; Spock1; mouse.
DR PRO; PR:Q62288; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q62288; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
DR GO; GO:0033268; C:node of Ranvier; IDA:UniProtKB.
DR GO; GO:0016528; C:sarcoplasm; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0021953; P:central nervous system neuron differentiation; IEP:UniProtKB.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IEP:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IEP:UniProtKB.
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 Disulfide bond; Extracellular matrix; Glycoprotein; Heparan sulfate;
KW Proteoglycan; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..442
FT /note="Testican-1"
FT /id="PRO_0000026700"
FT DOMAIN 133..185
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 313..379
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 375..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..442
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 386
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT DISULFID 89..100
FT /evidence="ECO:0000250"
FT DISULFID 94..110
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 316..340
FT /evidence="ECO:0000250"
FT DISULFID 351..358
FT /evidence="ECO:0000250"
FT DISULFID 360..379
FT /evidence="ECO:0000250"
FT CONFLICT 63..65
FT /note="GIQ -> EVE (in Ref. 1; CAA63448)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="P -> G (in Ref. 1; CAA63448)"
FT /evidence="ECO:0000305"
FT CONFLICT 406..407
FT /note="EL -> DV (in Ref. 1; CAA63448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 49551 MW; CEEE011B799E5154 CRC64;
MPAIAVLAAA AAAWCFLQVD SRHLDALAGG AALNNANFLD NDQWLSTVSQ YDRDKYWNRF
RDGIQDDYFR NWNPNKPFDQ ALDPSKDPCL KVKCSPHKVC VTQDYQTALC VSRKHLLPRQ
KKGNVAHKHW LGPSNLVKCK PCPVAQSAMV CGSDGHTYTS KCKLEFHACS TGKSLNSLCD
GPCPCLPEPE PLKPKAEKSA CTDKELRNLA SRLKDWFGAL HEDANRVIKP TSSDPAQGRF
DTSILPICKD SLGWMFNKLD MNYDLLLDHS EINAIYLDKY EPCIKPLFNS CDSFKDGKLS
NNEWCYCFQK PAGLPCQNEM NRIQKLSKGK SLLGAFIPRC NEEGYYKATQ CHGSTGQCWC
VDKYGNELAG SRKQGTVSCE EEQETSGDFG SGGSVVLLDD LEDERELGPK DKEGKLRVRT
RAVREDDEDE DDDKEDEVGY IW
