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 27-MAR-2024, entry version 169.
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 Danionidae; Danioninae; 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; DOI=10.1242/dev.126.14.3119;
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 from
CC 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 closing
CC blastopore with greater expression ventrally. At the animal pole,
CC expressed in the ectoderm flanking the anterior neural plate. At the
CC 10-somite stage, expressed in the developing tailbud and cranial neural
CC crest. At the 20-somite stage, also expressed in the hematopoietic
CC system. {ECO:0000269|PubMed:10375503, ECO:0000269|PubMed:9395394}.
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DR EMBL; AF027596; AAC60304.1; -; mRNA.
DR RefSeq; NP_571085.1; NM_131010.1.
DR AlphaFoldDB; O57460; -.
DR SMR; O57460; -.
DR STRING; 7955.ENSDARP00000054471; -.
DR MEROPS; M12.016; -.
DR GlyCosmos; O57460; 5 sites, No reported glycans.
DR PaxDb; 7955-ENSDARP00000054471; -.
DR GeneID; 474335; -.
DR KEGG; dre:474335; -.
DR AGR; ZFIN:ZDB-GENE-041020-1; -.
DR CTD; 7092; -.
DR ZFIN; ZDB-GENE-041020-1; tll1.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_005140_0_0_1; -.
DR InParanoid; O57460; -.
DR OMA; VWKIMVS; -.
DR OrthoDB; 2873870at2759; -.
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-2243919; Crosslinking of collagen fibrils.
DR PRO; PR:O57460; -.
DR Proteomes; UP000000437; Alternate scaffold 1.
DR Proteomes; UP000000437; Chromosome 1.
DR Bgee; ENSDARG00000037429; Expressed in retina and 10 other cell types or tissues.
DR ExpressionAtlas; O57460; baseline and differential.
DR GO; GO:0005576; C:extracellular region; NAS:ZFIN.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
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:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:ZFIN.
DR CDD; cd00041; CUB; 5.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 5.
DR InterPro; IPR015446; BMP_1/tolloid-like.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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 PANTHER; PTHR24251:SF42; BONE MORPHOGENETIC PROTEIN 1; 1.
DR PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 5.
DR Pfam; PF14670; FXa_inhibition; 2.
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; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 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; Developmental protein; Disulfide bond; EGF-like domain;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Signal; Zinc; Zymogen.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT PROPEP 33..156
FT /evidence="ECO:0000255"
FT /id="PRO_0000028901"
FT CHAIN 157..1022
FT /note="Dorsal-ventral patterning tolloid-like protein 1"
FT /id="PRO_0000028902"
FT DOMAIN 157..356
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 358..470
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 471..583
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 583..624
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 627..739
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 739..779
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 783..895
FT /note="CUB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 896..1012
FT /note="CUB 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT ACT_SITE 250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 199..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 219..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 221..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 358..384
FT /evidence="ECO:0000250"
FT DISULFID 411..433
FT /evidence="ECO:0000250"
FT DISULFID 471..497
FT /evidence="ECO:0000250"
FT DISULFID 524..546
FT /evidence="ECO:0000250"
FT DISULFID 587..599
FT /evidence="ECO:0000250"
FT DISULFID 595..608
FT /evidence="ECO:0000250"
FT DISULFID 610..623
FT /evidence="ECO:0000250"
FT DISULFID 627..653
FT /evidence="ECO:0000250"
FT DISULFID 680..702
FT /evidence="ECO:0000250"
FT DISULFID 743..754
FT /evidence="ECO:0000250"
FT DISULFID 750..763
FT /evidence="ECO:0000250"
FT DISULFID 765..778
FT /evidence="ECO:0000250"
FT DISULFID 783..809
FT /evidence="ECO:0000250"
FT DISULFID 836..858
FT /evidence="ECO:0000250"
FT DISULFID 896..926
FT /evidence="ECO:0000250"
FT DISULFID 953..975
FT /evidence="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
//
