TICN2_HUMAN
ID TICN2_HUMAN Reviewed; 424 AA.
AC Q92563; C9J767; Q6UW87;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Testican-2;
DE AltName: Full=SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 2;
DE Flags: Precursor;
GN Name=SPOCK2; Synonyms=KIAA0275, TICN2; ORFNames=UNQ269/PRO306;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP CALCIUM-BINDING.
RC TISSUE=Brain;
RX PubMed=10386950; DOI=10.1046/j.1471-4159.1999.0730012.x;
RA Vannahme C., Schuebel S., Herud M., Goesling S., Hulsmann H., Paulsson M.,
RA Hartmann U., Maurer P.;
RT "Molecular cloning of testican-2: defining a novel calcium-binding
RT proteoglycan family expressed in brain.";
RL J. Neurochem. 73:12-20(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [7]
RP PROTEIN SEQUENCE OF 23-37.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP PHOSPHORYLATION AT SER-72.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
CC -!- FUNCTION: May participate in diverse steps of neurogenesis. Binds
CC calcium.
CC -!- INTERACTION:
CC Q92563; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-311086, EBI-744099;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92563-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92563-2; Sequence=VSP_045668, VSP_045669;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Also found in lung and
CC testis. {ECO:0000269|PubMed:10386950}.
CC -!- PTM: Contains chondroitin sulfate and heparan sulfate O-linked
CC oligosaccharides. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13404.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ001453; CAA04774.1; -; mRNA.
DR EMBL; D87465; BAA13404.2; ALT_INIT; mRNA.
DR EMBL; AY358921; AAQ89280.1; -; mRNA.
DR EMBL; AK307091; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC022392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023558; AAH23558.1; -; mRNA.
DR CCDS; CCDS44431.1; -. [Q92563-2]
DR CCDS; CCDS7313.1; -. [Q92563-1]
DR RefSeq; NP_001127906.1; NM_001134434.1. [Q92563-2]
DR RefSeq; NP_001231879.1; NM_001244950.1. [Q92563-1]
DR RefSeq; NP_055582.1; NM_014767.2. [Q92563-1]
DR RefSeq; XP_016872474.1; XM_017016985.1. [Q92563-2]
DR AlphaFoldDB; Q92563; -.
DR SASBDB; Q92563; -.
DR BioGRID; 115146; 54.
DR IntAct; Q92563; 4.
DR STRING; 9606.ENSP00000362201; -.
DR MEROPS; I31.954; -.
DR GlyGen; Q92563; 6 sites, 3 O-linked glycans (2 sites).
DR iPTMnet; Q92563; -.
DR PhosphoSitePlus; Q92563; -.
DR BioMuta; SPOCK2; -.
DR DMDM; 24212500; -.
DR EPD; Q92563; -.
DR jPOST; Q92563; -.
DR MassIVE; Q92563; -.
DR MaxQB; Q92563; -.
DR PaxDb; Q92563; -.
DR PeptideAtlas; Q92563; -.
DR PRIDE; Q92563; -.
DR ProteomicsDB; 75319; -. [Q92563-1]
DR ProteomicsDB; 8867; -.
DR Antibodypedia; 29217; 101 antibodies from 24 providers.
DR DNASU; 9806; -.
DR Ensembl; ENST00000317376.8; ENSP00000321108.4; ENSG00000107742.14. [Q92563-1]
DR Ensembl; ENST00000373109.7; ENSP00000362201.2; ENSG00000107742.14. [Q92563-1]
DR Ensembl; ENST00000412663.5; ENSP00000397715.1; ENSG00000107742.14. [Q92563-2]
DR GeneID; 9806; -.
DR KEGG; hsa:9806; -.
DR MANE-Select; ENST00000373109.7; ENSP00000362201.2; NM_001244950.2; NP_001231879.1.
DR UCSC; uc001jso.3; human. [Q92563-1]
DR CTD; 9806; -.
DR DisGeNET; 9806; -.
DR GeneCards; SPOCK2; -.
DR HGNC; HGNC:13564; SPOCK2.
DR HPA; ENSG00000107742; Tissue enhanced (brain, lymphoid tissue).
DR MIM; 607988; gene.
DR neXtProt; NX_Q92563; -.
DR OpenTargets; ENSG00000107742; -.
DR PharmGKB; PA128394560; -.
DR VEuPathDB; HostDB:ENSG00000107742; -.
DR eggNOG; KOG3555; Eukaryota.
DR GeneTree; ENSGT00940000157107; -.
DR HOGENOM; CLU_037217_1_0_1; -.
DR InParanoid; Q92563; -.
DR OMA; SACKLEQ; -.
DR OrthoDB; 1235834at2759; -.
DR PhylomeDB; Q92563; -.
DR TreeFam; TF317779; -.
DR PathwayCommons; Q92563; -.
DR SignaLink; Q92563; -.
DR BioGRID-ORCS; 9806; 13 hits in 1072 CRISPR screens.
DR ChiTaRS; SPOCK2; human.
DR GeneWiki; SPOCK2; -.
DR GenomeRNAi; 9806; -.
DR Pharos; Q92563; Tbio.
DR PRO; PR:Q92563; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q92563; protein.
DR Bgee; ENSG00000107742; Expressed in paraflocculus and 173 other tissues.
DR ExpressionAtlas; Q92563; baseline and differential.
DR Genevisible; Q92563; HS.
DR GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; TAS:ParkinsonsUK-UCL.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; NAS:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; TAS:ParkinsonsUK-UCL.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IEA:Ensembl.
DR GO; GO:2000147; P:positive regulation of cell motility; TAS:ParkinsonsUK-UCL.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0045595; P:regulation of cell differentiation; NAS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; NAS: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 1: Evidence at protein level;
KW Alternative splicing; Calcium; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Heparan sulfate; Phosphoprotein;
KW Proteoglycan; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 23..424
FT /note="Testican-2"
FT /id="PRO_0000026701"
FT DOMAIN 130..182
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 310..376
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REGION 387..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..417
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
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 313..337
FT /evidence="ECO:0000250"
FT DISULFID 348..355
FT /evidence="ECO:0000250"
FT DISULFID 357..376
FT /evidence="ECO:0000250"
FT VAR_SEQ 64..77
FT /note="EVEDDYIKSWEDNQ -> VPSSDPPSTTQATP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045668"
FT VAR_SEQ 78..424
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045669"
FT VARIANT 353
FT /note="G -> S (in dbSNP:rs2306322)"
FT /id="VAR_022020"
FT CONFLICT 357
FT /note="C -> R (in Ref. 3; AAQ89280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 46779 MW; B7894E657FC2257F CRC64;
MRAPGCGRLV LPLLLLAAAA LAEGDAKGLK EGETPGNFME DEQWLSSISQ YSGKIKHWNR
FRDEVEDDYI KSWEDNQQGD EALDTTKDPC QKVKCSRHKV CIAQGYQRAM CISRKKLEHR
IKQPTVKLHG NKDSICKPCH MAQLASVCGS DGHTYSSVCK LEQQACLSSK QLAVRCEGPC
PCPTEQAATS TADGKPETCT GQDLADLGDR LRDWFQLLHE NSKQNGSASS VAGPASGLDK
SLGASCKDSI GWMFSKLDTS ADLFLDQTEL AAINLDKYEV CIRPFFNSCD TYKDGRVSTA
EWCFCFWREK PPCLAELERI QIQEAAKKKP GIFIPSCDED GYYRKMQCDQ SSGDCWCVDQ
LGLELTGTRT HGSPDCDDIV GFSGDFGSGV GWEDEEEKET EEAGEEAEEE EGEAGEADDG
GYIW
