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   24-JAN-2024, entry version 209.
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.
DR   AlphaFoldDB; Q92563; -.
DR   SASBDB; Q92563; -.
DR   BioGRID; 115146; 54.
DR   IntAct; Q92563; 5.
DR   STRING; 9606.ENSP00000321108; -.
DR   MEROPS; I31.954; -.
DR   GlyCosmos; Q92563; 5 sites, 3 glycans.
DR   GlyGen; Q92563; 7 sites, 4 O-linked glycans (3 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; 9606-ENSP00000362201; -.
DR   PeptideAtlas; Q92563; -.
DR   ProteomicsDB; 75319; -. [Q92563-1]
DR   ProteomicsDB; 8867; -.
DR   Antibodypedia; 29217; 128 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   AGR; HGNC:13564; -.
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; CDEVMGY; -.
DR   OrthoDB; 4174283at2759; -.
DR   PhylomeDB; Q92563; -.
DR   TreeFam; TF317779; -.
DR   PathwayCommons; Q92563; -.
DR   SignaLink; Q92563; -.
DR   BioGRID-ORCS; 9806; 13 hits in 1149 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 175 other cell types or tissues.
DR   ExpressionAtlas; Q92563; baseline and differential.
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: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; cd16238; EFh_SPARC_TICN2; 1.
DR   CDD; cd00104; KAZAL_FS; 1.
DR   CDD; cd00191; TY; 1.
DR   Gene3D; 3.30.60.30; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 4.10.800.10; Thyroglobulin type-1; 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   PANTHER; PTHR13866; SPARC OSTEONECTIN; 1.
DR   PANTHER; PTHR13866:SF18; TESTICAN-2; 1.
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; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
DR   Genevisible; Q92563; HS.
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
//