TICN1_HUMAN
ID TICN1_HUMAN Reviewed; 439 AA.
AC Q08629; B3KSW3; Q59EW0; Q8N630; Q9UCL8;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Testican-1;
DE AltName: Full=Protein SPOCK;
DE Flags: Precursor;
GN Name=SPOCK1; Synonyms=SPOCK, TIC1, TICN1;
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], AND PROTEIN SEQUENCE OF 344-347 AND 370-393.
RC TISSUE=Testis;
RX PubMed=8389704; DOI=10.1111/j.1432-1033.1993.tb17930.x;
RA Alliel P.M., Perin J.-P., Jolles P., Bonnet F.J.;
RT "Testican, a multidomain testicular proteoglycan resembling modulators of
RT cell social behaviour.";
RL Eur. J. Biochem. 214:347-350(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9272383; DOI=10.3109/10623329709053399;
RA Marr H.S., Basalamah M.A., Edgell C.J.;
RT "Endothelial cell expression of testican mRNA.";
RL Endothelium 5:209-219(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
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 370-392, GLYCOSYLATION, AND STRUCTURE OF CARBOHYDRATES.
RC TISSUE=Seminal plasma;
RX PubMed=1463459; DOI=10.1042/bj2880565;
RA Bonnet F., Perin J.-P., Maillet P., Jolles P., Alliel P.M.;
RT "Characterization of a human seminal plasma glycosaminoglycan-bearing
RT polypeptide.";
RL Biochem. J. 288:565-569(1992).
RN [8]
RP GLYCOSYLATION AT THR-228, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
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 -!- INTERACTION:
CC Q08629; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-2682560, EBI-747430;
CC Q08629; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2682560, EBI-6942903;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- PTM: O-glycosylated. Glycosaminoglycan that contains chondroitin
CC sulfate and heparan sulfate. {ECO:0000269|PubMed:1463459,
CC ECO:0000269|PubMed:23234360}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92938.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X73608; CAA51999.1; -; mRNA.
DR EMBL; AF231124; AAF43687.1; -; mRNA.
DR EMBL; AK094489; BAG52875.1; -; mRNA.
DR EMBL; AB209701; BAD92938.1; ALT_INIT; mRNA.
DR EMBL; AC005213; AAC24945.1; -; Genomic_DNA.
DR EMBL; AC091818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030691; AAH30691.1; -; mRNA.
DR CCDS; CCDS4191.1; -.
DR PIR; S33293; S33293.
DR RefSeq; NP_004589.1; NM_004598.3.
DR AlphaFoldDB; Q08629; -.
DR SMR; Q08629; -.
DR BioGRID; 112573; 6.
DR IntAct; Q08629; 5.
DR STRING; 9606.ENSP00000378401; -.
DR MEROPS; I31.006; -.
DR GlyConnect; 719; 1 O-Linked glycan (1 site).
DR GlyGen; Q08629; 5 sites, 2 O-linked glycans (1 site).
DR iPTMnet; Q08629; -.
DR PhosphoSitePlus; Q08629; -.
DR BioMuta; SPOCK1; -.
DR DMDM; 24212472; -.
DR jPOST; Q08629; -.
DR MassIVE; Q08629; -.
DR MaxQB; Q08629; -.
DR PaxDb; Q08629; -.
DR PeptideAtlas; Q08629; -.
DR PRIDE; Q08629; -.
DR ProteomicsDB; 58637; -.
DR TopDownProteomics; Q08629; -.
DR Antibodypedia; 26517; 131 antibodies from 23 providers.
DR DNASU; 6695; -.
DR Ensembl; ENST00000394945.6; ENSP00000378401.1; ENSG00000152377.14.
DR GeneID; 6695; -.
DR KEGG; hsa:6695; -.
DR MANE-Select; ENST00000394945.6; ENSP00000378401.1; NM_004598.4; NP_004589.1.
DR UCSC; uc003lbp.4; human.
DR CTD; 6695; -.
DR DisGeNET; 6695; -.
DR GeneCards; SPOCK1; -.
DR HGNC; HGNC:11251; SPOCK1.
DR HPA; ENSG00000152377; Tissue enhanced (brain).
DR MIM; 602264; gene.
DR neXtProt; NX_Q08629; -.
DR OpenTargets; ENSG00000152377; -.
DR PharmGKB; PA36081; -.
DR VEuPathDB; HostDB:ENSG00000152377; -.
DR eggNOG; KOG3555; Eukaryota.
DR GeneTree; ENSGT00940000158371; -.
DR InParanoid; Q08629; -.
DR OMA; PNCDEDP; -.
DR OrthoDB; 1235834at2759; -.
DR PhylomeDB; Q08629; -.
DR TreeFam; TF317779; -.
DR PathwayCommons; Q08629; -.
DR SignaLink; Q08629; -.
DR BioGRID-ORCS; 6695; 8 hits in 1068 CRISPR screens.
DR ChiTaRS; SPOCK1; human.
DR GeneWiki; SPOCK1; -.
DR GenomeRNAi; 6695; -.
DR Pharos; Q08629; Tbio.
DR PRO; PR:Q08629; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q08629; protein.
DR Bgee; ENSG00000152377; Expressed in stromal cell of endometrium and 189 other tissues.
DR ExpressionAtlas; Q08629; baseline and differential.
DR Genevisible; Q08629; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0033268; C:node of Ranvier; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; NAS:UniProtKB.
DR GO; GO:0016528; C:sarcoplasm; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0021953; P:central nervous system neuron differentiation; ISS:UniProtKB.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IDA:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; 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 Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Heparan sulfate; Proteoglycan; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..439
FT /note="Testican-1"
FT /id="PRO_0000026699"
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 415..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..439
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 228
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:23234360"
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 86..97
FT /evidence="ECO:0000250"
FT DISULFID 91..107
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 CONFLICT 62
FT /note="D -> DEVE (in Ref. 4; BAD92938)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="Q -> K (in Ref. 6; AAH30691)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 49124 MW; 1971601D90F1D0AD CRC64;
MPAIAVLAAA AAAWCFLQVE SRHLDALAGG AGPNHGNFLD NDQWLSTVSQ YDRDKYWNRF
RDDDYFRNWN PNKPFDQALD PSKDPCLKVK CSPHKVCVTQ DYQTALCVSR KHLLPRQKKG
NVAQKHWVGP SNLVKCKPCP VAQSAMVCGS DGHSYTSKCK LEFHACSTGK SLATLCDGPC
PCLPEPEPPK HKAERSACTD KELRNLASRL KDWFGALHED ANRVIKPTSS NTAQGRFDTS
ILPICKDSLG WMFNKLDMNY DLLLDPSEIN AIYLDKYEPC IKPLFNSCDS FKDGKLSNNE
WCYCFQKPGG LPCQNEMNRI QKLSKGKSLL GAFIPRCNEE GYYKATQCHG STGQCWCVDK
YGNELAGSRK QGAVSCEEEQ ETSGDFGSGG SVVLLDDLEY ERELGPKDKE GKLRVHTRAV
TEDDEDEDDD KEDEVGYIW
