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Dorsal-ventral patterning tolloid-like protein 1 (EC 3.4.24.-) (Mini fin protein)

 TLL1_DANRE              Reviewed;        1022 AA.
O57460;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
22-NOV-2017, entry version 140.
RecName: Full=Dorsal-ventral patterning tolloid-like protein 1;
EC=3.4.24.-;
AltName: Full=Mini fin protein;
Flags: Precursor;
Name=tll1; Synonyms=mfn, tld, tolloid;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Embryo;
PubMed=9395394; DOI=10.1126/science.278.5345.1937;
Blader P., Rastegar S., Fischer N., Straehle U.;
"Cleavage of the BMP-4 antagonist chordin by zebrafish Tolloid.";
Science 278:1937-1940(1997).
[2]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10375503;
Connors S.A., Trout J., Ekker M., Mullins M.C.;
"The role of tolloid/mini fin in dorsoventral pattern formation of the
zebrafish embryo.";
Development 126:3119-3130(1999).
-!- FUNCTION: Required for patterning ventral tissues of the tail. May
increase bone morphogenetic protein (BMP) activity at the end of
gastrulation by proteolytic cleavage of chordin and release of BMP
from inactive complexes. {ECO:0000269|PubMed:10375503,
ECO:0000269|PubMed:9395394}.
-!- TISSUE SPECIFICITY: During gastrulation, accumulates around the
closing blastopore with greater expression ventrally. At the
animal pole, expressed in the ectoderm flanking the anterior
neural plate. At the 10-somite stage, expressed in the developing
tailbud and cranial neural crest. At the 20-somite stage, also
expressed in the hematopoietic system.
{ECO:0000269|PubMed:10375503, ECO:0000269|PubMed:9395394}.
-!- SIMILARITY: Belongs to the peptidase M12A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF027596; AAC60304.1; -; mRNA.
RefSeq; NP_571085.1; NM_131010.1.
UniGene; Dr.75803; -.
ProteinModelPortal; O57460; -.
SMR; O57460; -.
STRING; 7955.ENSDARP00000054471; -.
PaxDb; O57460; -.
Ensembl; ENSDART00000054472; ENSDARP00000054471; ENSDARG00000037429.
GeneID; 474335; -.
KEGG; dre:474335; -.
CTD; 7092; -.
ZFIN; ZDB-GENE-041020-1; tll1.
eggNOG; KOG3714; Eukaryota.
eggNOG; ENOG410ZPX7; LUCA.
GeneTree; ENSGT00760000119018; -.
HOGENOM; HOG000236339; -.
HOVERGEN; HBG004859; -.
InParanoid; O57460; -.
KO; K09608; -.
OMA; NMRIEFR; -.
OrthoDB; EOG091G009U; -.
PhylomeDB; O57460; -.
TreeFam; TF314351; -.
Reactome; R-DRE-1474228; Degradation of the extracellular matrix.
Reactome; R-DRE-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-DRE-2214320; Anchoring fibril formation.
Reactome; R-DRE-2243919; Crosslinking of collagen fibrils.
PRO; PR:O57460; -.
Proteomes; UP000000437; Chromosome 1.
Bgee; ENSDARG00000037429; -.
ExpressionAtlas; O57460; baseline.
GO; GO:0005576; C:extracellular region; NAS:ZFIN.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; IDA:ZFIN.
GO; GO:0008233; F:peptidase activity; IDA:ZFIN.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001568; P:blood vessel development; IMP:ZFIN.
GO; GO:0048264; P:determination of ventral identity; IMP:ZFIN.
GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
GO; GO:0035124; P:embryonic caudal fin morphogenesis; IMP:ZFIN.
GO; GO:0035162; P:embryonic hemopoiesis; IMP:ZFIN.
GO; GO:0001885; P:endothelial cell development; IMP:ZFIN.
GO; GO:0001707; P:mesoderm formation; IMP:ZFIN.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:ZFIN.
GO; GO:0036342; P:post-anal tail morphogenesis; IMP:ZFIN.
GO; GO:0006508; P:proteolysis; IDA:ZFIN.
CDD; cd00041; CUB; 5.
CDD; cd04281; ZnMc_BMP1_TLD; 1.
Gene3D; 2.60.120.290; -; 5.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR015446; BMP_1/tolloid-like.
InterPro; IPR000859; CUB_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001506; Peptidase_M12A.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR035914; Sperma_CUB_dom_sf.
InterPro; IPR034036; ZnMP_TLD/BMP1.
Pfam; PF01400; Astacin; 1.
Pfam; PF00431; CUB; 5.
PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
PRINTS; PR00480; ASTACIN.
SMART; SM00042; CUB; 5.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 2.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF49854; SSF49854; 5.
PROSITE; PS00010; ASX_HYDROXYL; 2.
PROSITE; PS01180; CUB; 5.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS01187; EGF_CA; 2.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Calcium; Complete proteome; Developmental protein; Disulfide bond;
EGF-like domain; Glycoprotein; Hydrolase; Metal-binding;
Metalloprotease; Protease; Reference proteome; Repeat; Signal; Zinc;
Zymogen.
SIGNAL 1 32 {ECO:0000255}.
PROPEP 33 156 {ECO:0000255}.
/FTId=PRO_0000028901.
CHAIN 157 1022 Dorsal-ventral patterning tolloid-like
protein 1.
/FTId=PRO_0000028902.
DOMAIN 358 470 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 471 583 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 583 624 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 627 739 CUB 3. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 739 779 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 783 895 CUB 4. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 896 1012 CUB 5. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
REGION 157 357 Metalloprotease. {ECO:0000250}.
ACT_SITE 250 250 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 249 249 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 253 253 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 259 259 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 399 399 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 635 635 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 358 384 {ECO:0000250}.
DISULFID 411 433 {ECO:0000250}.
DISULFID 471 497 {ECO:0000250}.
DISULFID 524 546 {ECO:0000250}.
DISULFID 587 599 {ECO:0000250}.
DISULFID 595 608 {ECO:0000250}.
DISULFID 610 623 {ECO:0000250}.
DISULFID 627 653 {ECO:0000250}.
DISULFID 680 702 {ECO:0000250}.
DISULFID 743 754 {ECO:0000250}.
DISULFID 750 763 {ECO:0000250}.
DISULFID 765 778 {ECO:0000250}.
DISULFID 783 809 {ECO:0000250}.
DISULFID 836 858 {ECO:0000250}.
DISULFID 896 926 {ECO:0000250}.
DISULFID 953 975 {ECO:0000250}.
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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