ID   TSK_DANRE               Reviewed;         347 AA.
AC   Q58A48; Q7ZUT1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Tsukushi {ECO:0000303|PubMed:15363410};
DE   AltName: Full=Leucine-rich repeat-containing protein 54;
DE   AltName: Full=Z-TSK;
DE   Flags: Precursor;
GN   Name=tsku; Synonyms=lrcc54, tsk; ORFNames=zgc:56201;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=15363410; DOI=10.1016/j.devcel.2004.08.014;
RA   Ohta K., Lupo G., Kuriyama S., Keynes R., Holt C.E., Harris W.A.,
RA   Tanaka H., Ohnuma S.;
RT   "Tsukushi functions as an organizer inducer by inhibition of BMP activity
RT   in cooperation with chordin.";
RL   Dev. Cell 7:347-358(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Contributes to various developmental events through its
CC       interactions with multiple signaling pathways (By similarity).
CC       Dorsalizing factor which functions as an inhibitor of bone
CC       morphogenetic proteins during gastrulation (PubMed:15363410).
CC       {ECO:0000250|UniProtKB:Q65Z91, ECO:0000269|PubMed:15363410}.
CC   -!- SUBUNIT: Forms a ternary complex with chordin/CHRD and BMP4.
CC       {ECO:0000250|UniProtKB:Q65Z91}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q65Z91}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the germ ring including the shield at
CC       shield stage and in the tailbud at 10-somite stage.
CC       {ECO:0000269|PubMed:15363410}.
CC   -!- MISCELLANEOUS: This factor is named 'Tsukushi' because its expression
CC       pattern in chick embryos is similar to the shape of the Japanese
CC       horsetail plant, tsukushi. {ECO:0000250|UniProtKB:Q65Z91}.
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DR   EMBL; AB100034; BAD93182.1; -; mRNA.
DR   EMBL; BC047843; AAH47843.1; -; mRNA.
DR   AlphaFoldDB; Q58A48; -.
DR   SMR; Q58A48; -.
DR   STRING; 7955.ENSDARP00000110663; -.
DR   PaxDb; Q58A48; -.
DR   ZFIN; ZDB-GENE-030131-4683; tsku.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; Q58A48; -.
DR   Reactome; R-DRE-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-DRE-430116; GP1b-IX-V activation signalling.
DR   Reactome; R-DRE-75892; Platelet Adhesion to exposed collagen.
DR   Reactome; R-DRE-76009; Platelet Aggregation (Plug Formation).
DR   PRO; PR:Q58A48; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0098868; P:bone growth; ISS:UniProtKB.
DR   GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR   GO; GO:0003431; P:growth plate cartilage chondrocyte development; ISS:UniProtKB.
DR   Gene3D; 3.80.10.10; -; 3.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   Pfam; PF13855; LRR_8; 2.
DR   SMART; SM00369; LRR_TYP; 6.
DR   PROSITE; PS51450; LRR; 8.
PE   2: Evidence at transcript level;
KW   Developmental protein; Glycoprotein; Leucine-rich repeat;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..347
FT                   /note="Tsukushi"
FT                   /id="PRO_0000240411"
FT   DOMAIN          20..61
FT                   /note="LRRNT"
FT   REPEAT          62..83
FT                   /note="LRR 1"
FT   REPEAT          88..109
FT                   /note="LRR 2"
FT   REPEAT          112..133
FT                   /note="LRR 3"
FT   REPEAT          135..156
FT                   /note="LRR 4"
FT   REPEAT          160..175
FT                   /note="LRR 5"
FT   REPEAT          185..205
FT                   /note="LRR 6"
FT   REPEAT          206..227
FT                   /note="LRR 7"
FT   REPEAT          230..252
FT                   /note="LRR 8"
FT   REPEAT          255..277
FT                   /note="LRR 9"
FT   REPEAT          280..301
FT                   /note="LRR 10"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        73
FT                   /note="T -> I (in Ref. 1; BAD93182)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265
FT                   /note="S -> R (in Ref. 1; BAD93182)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        273
FT                   /note="N -> D (in Ref. 1; BAD93182)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        321
FT                   /note="M -> K (in Ref. 1; BAD93182)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        334
FT                   /note="P -> H (in Ref. 1; BAD93182)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   347 AA;  37776 MW;  1EB5446DD0871B80 CRC64;
     MASLLCLFFS LLGLAAIGAV KNCHPQCRCE VETFGLFDSF SLTKVDCSRI GPGNTPVPIP
     LDTSHLDLSL NSTTSISDTM LSGPGYTTLV SLDLSSNLIA QISPKAFSKL RYLETLDLSS
     NALEGLSDGC FTGLPLVELD LSENQFKEFN LDLFTTRTQD LPIMVDLSRN LLTSIFRRTP
     GHPLYIKSLM LAGNQLKTVP KLNGIPLQYL NLDGNLISSI DTGAFDSLTE LVHLSLSGLS
     ELTLIHPGAF RSLKNLQALD LSNNSQLKTL NPNVFSGLVS LQELNLSNTA VTPLSRTVFM
     QMPNIKSITL GPNVHCWKTH MQGQFHRQIG QAKPNDILTC DNAGLIL