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Database: UniProt
Entry: O57460
LinkDB: O57460
Original site: O57460 
ID   TLL1_DANRE              Reviewed;        1022 AA.
AC   O57460;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   13-FEB-2019, entry version 148.
DE   RecName: Full=Dorsal-ventral patterning tolloid-like protein 1;
DE            EC=3.4.24.-;
DE   AltName: Full=Mini fin protein;
DE   Flags: Precursor;
GN   Name=tll1; Synonyms=mfn, tld, tolloid;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   PubMed=9395394; DOI=10.1126/science.278.5345.1937;
RA   Blader P., Rastegar S., Fischer N., Straehle U.;
RT   "Cleavage of the BMP-4 antagonist chordin by zebrafish Tolloid.";
RL   Science 278:1937-1940(1997).
RN   [2]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=10375503;
RA   Connors S.A., Trout J., Ekker M., Mullins M.C.;
RT   "The role of tolloid/mini fin in dorsoventral pattern formation of the
RT   zebrafish embryo.";
RL   Development 126:3119-3130(1999).
CC   -!- FUNCTION: Required for patterning ventral tissues of the tail. May
CC       increase bone morphogenetic protein (BMP) activity at the end of
CC       gastrulation by proteolytic cleavage of chordin and release of BMP
CC       from inactive complexes. {ECO:0000269|PubMed:10375503,
CC       ECO:0000269|PubMed:9395394}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU01211};
CC   -!- TISSUE SPECIFICITY: During gastrulation, accumulates around the
CC       closing blastopore with greater expression ventrally. At the
CC       animal pole, expressed in the ectoderm flanking the anterior
CC       neural plate. At the 10-somite stage, expressed in the developing
CC       tailbud and cranial neural crest. At the 20-somite stage, also
CC       expressed in the hematopoietic system.
CC       {ECO:0000269|PubMed:10375503, ECO:0000269|PubMed:9395394}.
DR   EMBL; AF027596; AAC60304.1; -; mRNA.
DR   RefSeq; NP_571085.1; NM_131010.1.
DR   UniGene; Dr.75803; -.
DR   ProteinModelPortal; O57460; -.
DR   SMR; O57460; -.
DR   STRING; 7955.ENSDARP00000054471; -.
DR   PaxDb; O57460; -.
DR   PRIDE; O57460; -.
DR   Ensembl; ENSDART00000054472; ENSDARP00000054471; ENSDARG00000037429.
DR   Ensembl; ENSDART00000181526; ENSDARP00000153079; ENSDARG00000113847.
DR   Ensembl; ENSDART00000182810; ENSDARP00000146714; ENSDARG00000037429.
DR   GeneID; 474335; -.
DR   KEGG; dre:474335; -.
DR   CTD; 7092; -.
DR   ZFIN; ZDB-GENE-041020-1; tll1.
DR   eggNOG; KOG3714; Eukaryota.
DR   eggNOG; ENOG410ZPX7; LUCA.
DR   GeneTree; ENSGT00940000157225; -.
DR   HOGENOM; HOG000236339; -.
DR   HOVERGEN; HBG004859; -.
DR   InParanoid; O57460; -.
DR   KO; K09608; -.
DR   OMA; GHFCGYD; -.
DR   OrthoDB; 170905at2759; -.
DR   PhylomeDB; O57460; -.
DR   TreeFam; TF314351; -.
DR   Reactome; R-DRE-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-DRE-1650814; Collagen biosynthesis and modifying enzymes.
DR   Reactome; R-DRE-2214320; Anchoring fibril formation.
DR   PRO; PR:O57460; -.
DR   Proteomes; UP000000437; Chromosome 1.
DR   Bgee; ENSDARG00000037429; Expressed in 20 organ(s), highest expression level in multi-cellular organism.
DR   ExpressionAtlas; O57460; baseline.
DR   GO; GO:0005576; C:extracellular region; NAS:ZFIN.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IDA:ZFIN.
DR   GO; GO:0008233; F:peptidase activity; IDA:ZFIN.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001568; P:blood vessel development; IMP:ZFIN.
DR   GO; GO:0048264; P:determination of ventral identity; IMP:ZFIN.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
DR   GO; GO:0035124; P:embryonic caudal fin morphogenesis; IMP:ZFIN.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IMP:ZFIN.
DR   GO; GO:0001885; P:endothelial cell development; IMP:ZFIN.
DR   GO; GO:0001707; P:mesoderm formation; IMP:ZFIN.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:ZFIN.
DR   GO; GO:0036342; P:post-anal tail morphogenesis; IMP:ZFIN.
DR   GO; GO:0006508; P:proteolysis; IDA:ZFIN.
DR   CDD; cd00041; CUB; 5.
DR   CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR   Gene3D; 2.60.120.290; -; 5.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR015446; BMP_1/tolloid-like.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR034036; ZnMP_TLD/BMP1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 5.
DR   PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00042; CUB; 5.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49854; SSF49854; 5.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01180; CUB; 5.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Complete proteome; Developmental protein; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Repeat; Signal; Zinc;
KW   Zymogen.
FT   SIGNAL        1     32       {ECO:0000255}.
FT   PROPEP       33    156       {ECO:0000255}.
FT                                /FTId=PRO_0000028901.
FT   CHAIN       157   1022       Dorsal-ventral patterning tolloid-like
FT                                protein 1.
FT                                /FTId=PRO_0000028902.
FT   DOMAIN      157    356       Peptidase M12A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01211}.
FT   DOMAIN      358    470       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      471    583       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      583    624       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      627    739       CUB 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      739    779       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      783    895       CUB 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      896   1012       CUB 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   ACT_SITE    250    250       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       249    249       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       253    253       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   METAL       259    259       Zinc; via tele nitrogen; catalytic.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   CARBOHYD    129    129       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    178    178       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    368    368       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    399    399       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    635    635       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    199    355       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    219    241       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    221    222       {ECO:0000255|PROSITE-ProRule:PRU01211}.
FT   DISULFID    358    384       {ECO:0000250}.
FT   DISULFID    411    433       {ECO:0000250}.
FT   DISULFID    471    497       {ECO:0000250}.
FT   DISULFID    524    546       {ECO:0000250}.
FT   DISULFID    587    599       {ECO:0000250}.
FT   DISULFID    595    608       {ECO:0000250}.
FT   DISULFID    610    623       {ECO:0000250}.
FT   DISULFID    627    653       {ECO:0000250}.
FT   DISULFID    680    702       {ECO:0000250}.
FT   DISULFID    743    754       {ECO:0000250}.
FT   DISULFID    750    763       {ECO:0000250}.
FT   DISULFID    765    778       {ECO:0000250}.
FT   DISULFID    783    809       {ECO:0000250}.
FT   DISULFID    836    858       {ECO:0000250}.
FT   DISULFID    896    926       {ECO:0000250}.
FT   DISULFID    953    975       {ECO:0000250}.
SQ   SEQUENCE   1022 AA;  115536 MW;  A68CA1D0E41793F9 CRC64;
     MDYLYSALTS KMNWIALLLA GLTFCCKVSV HSCLDYDDSY DYYEEEKTET IDYKDPCKAA
     VFWGDIALDD EDLKMFHIDG TIDLKQQTHG RQGHTSGGLG EHVPTKKRGS LYLLLDRIRR
     LGFESWPVNS SKDVSSIKTG IRRVNSARNV KSRVPRAATS RAEKIWPGGV IPYVIGGNFT
     GSQRAMLKQA MRHWEKQTCV TFIEKTDEES YIVFTYRPCG CCSYVGRRGN GPQAISIGKN
     CDKFGIVVHE LGHVIGFWHE HTRPDRDDHV TIIRDNIQPG QEYNFIKMEP GDVNSLGEPY
     DFDSIMHYAR NTFSRGMFLD TILPSRDENG VRPAIGQRTR LSKGDISQAK KLYRCPACGE
     TLQDSVGNFS SPGYPNGYPS YTHCVWRISV TPGEKIVLNF TTMDLYKSSL CWYDYIEVRD
     GYWRKAPLLG RFCGDKIPEV LVSTDSRMWI EFRSSSNWVG KGFAAVYEAI CGGEISKDSG
     QIQSPNYPDD YRPSKECVWR ITVSEGYSVG LSFQVFEIER HDSCAYDYLE VRDGLSENSP
     LIGRFCGYDK PEDIRSTSNN LWMKFVSDGT VNKAGFAANF FKEEDECLKP DNGGCEQRCV
     NTLGSFKCAC DPGYELAPDK KSCEAACGGL LTKLNGTITT PGWPKEYPPN KNCVWQVVAP
     TQYRISMQFE AFELEGNEVC KYDYVEVRSG LSSDSKLHGK YCGTEVPEVI TSQYNNMRIE
     FKSDNTVSKK GFKAHFFSDK DECSKDNGGC QHECINTIGS YVCQCRNGFI LHENKHDCKE
     AECEHKIHST TGTISSPNWP DKYPSRKECT WDITATPGHR VKISFNEFEI EQHQECAYDH
     LEAFDGDSDK TPILSRLCGN KIPEPLISTG NKMYLRFISD ASVQRKGFQA THSTECGGRL
     KAEARQKNLY SHAQFGDNNY PGHTDCEWLI VAESGYGIEL TFTTFEVEEE ADCGYDYIEL
     YDGYDTGAHK IGRFCGSGPR EELYSAGDAV LIHFHSDDTI SKKGFHIRYT STKFQEALHT
     RK
//
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