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O57460 (TLL1_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dorsal-ventral patterning tolloid-like protein 1

EC=3.4.24.-
Alternative name(s):
Mini fin protein
Gene names
Name:tll1
Synonyms:mfn, tld, tolloid
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length1022 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. Ref.1 Ref.2

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. Ref.1 Ref.2

Sequence similarities

Belongs to the peptidase M12A family.

Contains 5 CUB domains.

Contains 2 EGF-like domains.

Ontologies

Keywords
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionDevelopmental protein
Hydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood vessel development

Inferred from mutant phenotype Ref.2. Source: ZFIN

determination of ventral identity

Inferred from mutant phenotype Ref.2PubMed 9007231Ref.1. Source: ZFIN

dorsal/ventral pattern formation

Inferred from mutant phenotype PubMed 11969259PubMed 16530746. Source: ZFIN

embryonic caudal fin morphogenesis

Inferred from mutant phenotype Ref.2Ref.1. Source: ZFIN

embryonic hemopoiesis

Inferred from mutant phenotype Ref.1. Source: ZFIN

endothelial cell development

Inferred from mutant phenotype Ref.2. Source: ZFIN

mesoderm formation

Inferred from mutant phenotype Ref.2. Source: ZFIN

positive regulation of BMP signaling pathway

Inferred from mutant phenotype Ref.2Ref.1. Source: ZFIN

post-anal tail morphogenesis

Inferred from mutant phenotype PubMed 21610036. Source: ZFIN

proteolysis

Inferred from direct assay PubMed 16518392Ref.1. Source: ZFIN

   Cellular_componentextracellular region

Non-traceable author statement Ref.2. Source: ZFIN

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

metallopeptidase activity

Inferred from direct assay Ref.1. Source: ZFIN

peptidase activity

Inferred from direct assay PubMed 16518392. Source: ZFIN

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Propeptide33 – 156124 Potential
PRO_0000028901
Chain157 – 1022866Dorsal-ventral patterning tolloid-like protein 1
PRO_0000028902

Regions

Domain358 – 470113CUB 1
Domain471 – 583113CUB 2
Domain583 – 62442EGF-like 1; calcium-binding Potential
Domain627 – 739113CUB 3
Domain739 – 77941EGF-like 2; calcium-binding Potential
Domain783 – 895113CUB 4
Domain896 – 1012117CUB 5
Region157 – 357201Metalloprotease By similarity

Sites

Active site2501 By similarity
Metal binding2491Zinc; catalytic By similarity
Metal binding2531Zinc; catalytic By similarity
Metal binding2591Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1291N-linked (GlcNAc...) Potential
Glycosylation1781N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation3991N-linked (GlcNAc...) Potential
Glycosylation6351N-linked (GlcNAc...) Potential
Disulfide bond358 ↔ 384 By similarity
Disulfide bond411 ↔ 433 By similarity
Disulfide bond471 ↔ 497 By similarity
Disulfide bond524 ↔ 546 By similarity
Disulfide bond587 ↔ 599 By similarity
Disulfide bond595 ↔ 608 By similarity
Disulfide bond610 ↔ 623 By similarity
Disulfide bond627 ↔ 653 By similarity
Disulfide bond680 ↔ 702 By similarity
Disulfide bond743 ↔ 754 By similarity
Disulfide bond750 ↔ 763 By similarity
Disulfide bond765 ↔ 778 By similarity
Disulfide bond783 ↔ 809 By similarity
Disulfide bond836 ↔ 858 By similarity
Disulfide bond896 ↔ 926 By similarity
Disulfide bond953 ↔ 975 By similarity

Sequences

Sequence LengthMass (Da)Tools
O57460 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: A68CA1D0E41793F9

FASTA1,022115,536
        10         20         30         40         50         60 
MDYLYSALTS KMNWIALLLA GLTFCCKVSV HSCLDYDDSY DYYEEEKTET IDYKDPCKAA 

        70         80         90        100        110        120 
VFWGDIALDD EDLKMFHIDG TIDLKQQTHG RQGHTSGGLG EHVPTKKRGS LYLLLDRIRR 

       130        140        150        160        170        180 
LGFESWPVNS SKDVSSIKTG IRRVNSARNV KSRVPRAATS RAEKIWPGGV IPYVIGGNFT 

       190        200        210        220        230        240 
GSQRAMLKQA MRHWEKQTCV TFIEKTDEES YIVFTYRPCG CCSYVGRRGN GPQAISIGKN 

       250        260        270        280        290        300 
CDKFGIVVHE LGHVIGFWHE HTRPDRDDHV TIIRDNIQPG QEYNFIKMEP GDVNSLGEPY 

       310        320        330        340        350        360 
DFDSIMHYAR NTFSRGMFLD TILPSRDENG VRPAIGQRTR LSKGDISQAK KLYRCPACGE 

       370        380        390        400        410        420 
TLQDSVGNFS SPGYPNGYPS YTHCVWRISV TPGEKIVLNF TTMDLYKSSL CWYDYIEVRD 

       430        440        450        460        470        480 
GYWRKAPLLG RFCGDKIPEV LVSTDSRMWI EFRSSSNWVG KGFAAVYEAI CGGEISKDSG 

       490        500        510        520        530        540 
QIQSPNYPDD YRPSKECVWR ITVSEGYSVG LSFQVFEIER HDSCAYDYLE VRDGLSENSP 

       550        560        570        580        590        600 
LIGRFCGYDK PEDIRSTSNN LWMKFVSDGT VNKAGFAANF FKEEDECLKP DNGGCEQRCV 

       610        620        630        640        650        660 
NTLGSFKCAC DPGYELAPDK KSCEAACGGL LTKLNGTITT PGWPKEYPPN KNCVWQVVAP 

       670        680        690        700        710        720 
TQYRISMQFE AFELEGNEVC KYDYVEVRSG LSSDSKLHGK YCGTEVPEVI TSQYNNMRIE 

       730        740        750        760        770        780 
FKSDNTVSKK GFKAHFFSDK DECSKDNGGC QHECINTIGS YVCQCRNGFI LHENKHDCKE 

       790        800        810        820        830        840 
AECEHKIHST TGTISSPNWP DKYPSRKECT WDITATPGHR VKISFNEFEI EQHQECAYDH 

       850        860        870        880        890        900 
LEAFDGDSDK TPILSRLCGN KIPEPLISTG NKMYLRFISD ASVQRKGFQA THSTECGGRL 

       910        920        930        940        950        960 
KAEARQKNLY SHAQFGDNNY PGHTDCEWLI VAESGYGIEL TFTTFEVEEE ADCGYDYIEL 

       970        980        990       1000       1010       1020 
YDGYDTGAHK IGRFCGSGPR EELYSAGDAV LIHFHSDDTI SKKGFHIRYT STKFQEALHT 


RK 

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References

[1]"Cleavage of the BMP-4 antagonist chordin by zebrafish Tolloid."
Blader P., Rastegar S., Fischer N., Straehle U.
Science 278:1937-1940(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Embryo.
[2]"The role of tolloid/mini fin in dorsoventral pattern formation of the zebrafish embryo."
Connors S.A., Trout J., Ekker M., Mullins M.C.
Development 126:3119-3130(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF027596 mRNA. Translation: AAC60304.1.
RefSeqNP_571085.1. NM_131010.1.
UniGeneDr.75803.

3D structure databases

ProteinModelPortalO57460.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM12.016.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000054472; ENSDARP00000054471; ENSDARG00000037429.
GeneID474335.
KEGGdre:474335.

Organism-specific databases

CTD7092.
ZFINZDB-GENE-041020-1. tll1.

Phylogenomic databases

eggNOGNOG70307.
GeneTreeENSGT00750000117289.
HOGENOMHOG000236339.
HOVERGENHBG004859.
InParanoidO57460.
KOK09608.
OMAYDYTFDG.
OrthoDBEOG7N8ZTV.
PhylomeDBO57460.
TreeFamTF314351.

Gene expression databases

BgeeO57460.

Family and domain databases

Gene3D2.60.120.290. 5 hits.
3.40.390.10. 1 hit.
InterProIPR015446. BMP_1/tolloid-like.
IPR000859. CUB_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
[Graphical view]
PfamPF01400. Astacin. 1 hit.
PF00431. CUB. 5 hits.
[Graphical view]
PIRSFPIRSF001199. BMP_1/tolloid-like. 1 hit.
PRINTSPR00480. ASTACIN.
SMARTSM00042. CUB. 5 hits.
SM00179. EGF_CA. 2 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF49854. SSF49854. 5 hits.
PROSITEPS00010. ASX_HYDROXYL. 2 hits.
PS01180. CUB. 5 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 2 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20850399.
PROO57460.

Entry information

Entry nameTLL1_DANRE
AccessionPrimary (citable) accession number: O57460
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries