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O57460

- TLL1_DANRE

UniProt

O57460 - TLL1_DANRE

Protein

Dorsal-ventral patterning tolloid-like protein 1

Gene

tll1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi249 – 2491Zinc; catalyticPROSITE-ProRule annotation
    Active sitei250 – 2501PROSITE-ProRule annotation
    Metal bindingi253 – 2531Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi259 – 2591Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. metalloendopeptidase activity Source: InterPro
    3. metallopeptidase activity Source: ZFIN
    4. peptidase activity Source: ZFIN
    5. protein binding Source: ZFIN
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. blood vessel development Source: ZFIN
    2. determination of ventral identity Source: ZFIN
    3. dorsal/ventral pattern formation Source: ZFIN
    4. embryonic caudal fin morphogenesis Source: ZFIN
    5. embryonic hemopoiesis Source: ZFIN
    6. endothelial cell development Source: ZFIN
    7. mesoderm formation Source: ZFIN
    8. positive regulation of BMP signaling pathway Source: ZFIN
    9. post-anal tail morphogenesis Source: ZFIN
    10. proteolysis Source: ZFIN

    Keywords - Molecular functioni

    Developmental protein, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_212272. Anchoring fibril formation.
    REACT_218692. Crosslinking of collagen fibrils.
    REACT_222767. Collagen biosynthesis and modifying enzymes.

    Protein family/group databases

    MEROPSiM12.016.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dorsal-ventral patterning tolloid-like protein 1 (EC:3.4.24.-)
    Alternative name(s):
    Mini fin protein
    Gene namesi
    Name:tll1
    Synonyms:mfn, tld, tolloid
    OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
    Taxonomic identifieri7955 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
    ProteomesiUP000000437: Chromosome 1

    Organism-specific databases

    ZFINiZDB-GENE-041020-1. tll1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: ZFIN

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Sequence AnalysisAdd
    BLAST
    Propeptidei33 – 156124Sequence AnalysisPRO_0000028901Add
    BLAST
    Chaini157 – 1022866Dorsal-ventral patterning tolloid-like protein 1PRO_0000028902Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi358 ↔ 384By similarity
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi399 – 3991N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi411 ↔ 433By similarity
    Disulfide bondi471 ↔ 497By similarity
    Disulfide bondi524 ↔ 546By similarity
    Disulfide bondi587 ↔ 599By similarity
    Disulfide bondi595 ↔ 608By similarity
    Disulfide bondi610 ↔ 623By similarity
    Disulfide bondi627 ↔ 653By similarity
    Glycosylationi635 – 6351N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi680 ↔ 702By similarity
    Disulfide bondi743 ↔ 754By similarity
    Disulfide bondi750 ↔ 763By similarity
    Disulfide bondi765 ↔ 778By similarity
    Disulfide bondi783 ↔ 809By similarity
    Disulfide bondi836 ↔ 858By similarity
    Disulfide bondi896 ↔ 926By similarity
    Disulfide bondi953 ↔ 975By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Expressioni

    Tissue specificityi

    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.2 Publications

    Gene expression databases

    BgeeiO57460.

    Structurei

    3D structure databases

    ProteinModelPortaliO57460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini358 – 470113CUB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini471 – 583113CUB 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini583 – 62442EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini627 – 739113CUB 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini739 – 77941EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini783 – 895113CUB 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini896 – 1012117CUB 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni157 – 357201MetalloproteaseBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M12A family.Curated
    Contains 5 CUB domains.PROSITE-ProRule annotation
    Contains 2 EGF-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG70307.
    GeneTreeiENSGT00750000117289.
    HOGENOMiHOG000236339.
    HOVERGENiHBG004859.
    InParanoidiO57460.
    KOiK09608.
    OMAiGEPYDFD.
    OrthoDBiEOG7N8ZTV.
    PhylomeDBiO57460.
    TreeFamiTF314351.

    Family and domain databases

    Gene3Di2.60.120.290. 5 hits.
    3.40.390.10. 1 hit.
    InterProiIPR015446. 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]
    PfamiPF01400. Astacin. 1 hit.
    PF00431. CUB. 5 hits.
    [Graphical view]
    PIRSFiPIRSF001199. BMP_1/tolloid-like. 1 hit.
    PRINTSiPR00480. ASTACIN.
    SMARTiSM00042. CUB. 5 hits.
    SM00179. EGF_CA. 2 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49854. SSF49854. 5 hits.
    PROSITEiPS00010. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O57460-1 [UniParc]FASTAAdd to Basket

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    MDYLYSALTS KMNWIALLLA GLTFCCKVSV HSCLDYDDSY DYYEEEKTET     50
    IDYKDPCKAA VFWGDIALDD EDLKMFHIDG TIDLKQQTHG RQGHTSGGLG 100
    EHVPTKKRGS LYLLLDRIRR LGFESWPVNS SKDVSSIKTG IRRVNSARNV 150
    KSRVPRAATS RAEKIWPGGV IPYVIGGNFT GSQRAMLKQA MRHWEKQTCV 200
    TFIEKTDEES YIVFTYRPCG CCSYVGRRGN GPQAISIGKN CDKFGIVVHE 250
    LGHVIGFWHE HTRPDRDDHV TIIRDNIQPG QEYNFIKMEP GDVNSLGEPY 300
    DFDSIMHYAR NTFSRGMFLD TILPSRDENG VRPAIGQRTR LSKGDISQAK 350
    KLYRCPACGE TLQDSVGNFS SPGYPNGYPS YTHCVWRISV TPGEKIVLNF 400
    TTMDLYKSSL CWYDYIEVRD GYWRKAPLLG RFCGDKIPEV LVSTDSRMWI 450
    EFRSSSNWVG KGFAAVYEAI CGGEISKDSG QIQSPNYPDD YRPSKECVWR 500
    ITVSEGYSVG LSFQVFEIER HDSCAYDYLE VRDGLSENSP LIGRFCGYDK 550
    PEDIRSTSNN LWMKFVSDGT VNKAGFAANF FKEEDECLKP DNGGCEQRCV 600
    NTLGSFKCAC DPGYELAPDK KSCEAACGGL LTKLNGTITT PGWPKEYPPN 650
    KNCVWQVVAP TQYRISMQFE AFELEGNEVC KYDYVEVRSG LSSDSKLHGK 700
    YCGTEVPEVI TSQYNNMRIE FKSDNTVSKK GFKAHFFSDK DECSKDNGGC 750
    QHECINTIGS YVCQCRNGFI LHENKHDCKE AECEHKIHST TGTISSPNWP 800
    DKYPSRKECT WDITATPGHR VKISFNEFEI EQHQECAYDH LEAFDGDSDK 850
    TPILSRLCGN KIPEPLISTG NKMYLRFISD ASVQRKGFQA THSTECGGRL 900
    KAEARQKNLY SHAQFGDNNY PGHTDCEWLI VAESGYGIEL TFTTFEVEEE 950
    ADCGYDYIEL YDGYDTGAHK IGRFCGSGPR EELYSAGDAV LIHFHSDDTI 1000
    SKKGFHIRYT STKFQEALHT RK 1022
    Length:1,022
    Mass (Da):115,536
    Last modified:June 1, 1998 - v1
    Checksum:iA68CA1D0E41793F9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF027596 mRNA. Translation: AAC60304.1.
    RefSeqiNP_571085.1. NM_131010.1.
    UniGeneiDr.75803.

    Genome annotation databases

    EnsembliENSDART00000054472; ENSDARP00000054471; ENSDARG00000037429.
    GeneIDi474335.
    KEGGidre:474335.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF027596 mRNA. Translation: AAC60304.1 .
    RefSeqi NP_571085.1. NM_131010.1.
    UniGenei Dr.75803.

    3D structure databases

    ProteinModelPortali O57460.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M12.016.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSDART00000054472 ; ENSDARP00000054471 ; ENSDARG00000037429 .
    GeneIDi 474335.
    KEGGi dre:474335.

    Organism-specific databases

    CTDi 7092.
    ZFINi ZDB-GENE-041020-1. tll1.

    Phylogenomic databases

    eggNOGi NOG70307.
    GeneTreei ENSGT00750000117289.
    HOGENOMi HOG000236339.
    HOVERGENi HBG004859.
    InParanoidi O57460.
    KOi K09608.
    OMAi GEPYDFD.
    OrthoDBi EOG7N8ZTV.
    PhylomeDBi O57460.
    TreeFami TF314351.

    Enzyme and pathway databases

    Reactomei REACT_212272. Anchoring fibril formation.
    REACT_218692. Crosslinking of collagen fibrils.
    REACT_222767. Collagen biosynthesis and modifying enzymes.

    Miscellaneous databases

    NextBioi 20850399.
    PROi O57460.

    Gene expression databases

    Bgeei O57460.

    Family and domain databases

    Gene3Di 2.60.120.290. 5 hits.
    3.40.390.10. 1 hit.
    InterProi IPR015446. 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 ]
    Pfami PF01400. Astacin. 1 hit.
    PF00431. CUB. 5 hits.
    [Graphical view ]
    PIRSFi PIRSF001199. BMP_1/tolloid-like. 1 hit.
    PRINTSi PR00480. ASTACIN.
    SMARTi SM00042. CUB. 5 hits.
    SM00179. EGF_CA. 2 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49854. SSF49854. 5 hits.
    PROSITEi PS00010. 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 ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiTLL1_DANRE
    AccessioniPrimary (citable) accession number: O57460
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3