ID TLL1_CHICK Reviewed; 1008 AA. AC Q9DER7; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=Tolloid-like protein 1; DE EC=3.4.24.-; DE AltName: Full=Chicken tolloid-like protein 1; DE AltName: Full=Metalloprotease colloid; DE Flags: Precursor; GN Name=TLL1; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX PubMed=10940628; DOI=10.1016/s0925-4773(00)00382-8; RA Liaubet L., Bertrand N., Medevielle F., Pituello F.; RT "Identification by differential display of a chicken tolloid-related RT metalloprotease specifically expressed in the caudal notochord."; RL Mech. Dev. 96:101-105(2000). CC -!- FUNCTION: Protease which processes procollagen C-propeptides, such as CC chordin, probiglycan and prolysyl oxidase. Required for the embryonic CC development. Predominant protease, which in the development, influences CC dorsal-ventral patterning and skeletogenesis (By similarity). CC {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU01211}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE- CC ProRule:PRU01211}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10940628}. CC -!- DEVELOPMENTAL STAGE: Expressed at HH stage-10, with a restricted CC expression to the caudal notochord expanding between Hensen node and CC the last individualized somite. No expression in the ventral midline of CC the neural plate. The regionalized expression in the notochord persists CC at least until HH-stage 15. At HH stage-13, expression can be observed CC in the roof of the caudal diencephalon and expands, at HH stage-15, CC caudally to the mesencephalon. {ECO:0000269|PubMed:10940628}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ012462; CAC08820.1; -; mRNA. DR AlphaFoldDB; Q9DER7; -. DR SMR; Q9DER7; -. DR STRING; 9031.ENSGALP00000061751; -. DR MEROPS; M12.016; -. DR GlyCosmos; Q9DER7; 5 sites, No reported glycans. DR PaxDb; 9031-ENSGALP00000015567; -. DR VEuPathDB; HostDB:geneid_395441; -. DR eggNOG; KOG3714; Eukaryota. DR InParanoid; Q9DER7; -. DR PhylomeDB; Q9DER7; -. DR Proteomes; UP000000539; Unassembled WGS sequence. 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:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central. DR GO; GO:0016485; P:protein processing; IBA:GO_Central. 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; PS01180; CUB; 5. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 2. DR PROSITE; PS01187; EGF_CA; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 2: Evidence at transcript level; KW Calcium; Developmental protein; Differentiation; Disulfide bond; KW EGF-like domain; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; KW Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT PROPEP 27..143 FT /evidence="ECO:0000250" FT /id="PRO_0000046027" FT CHAIN 144..1008 FT /note="Tolloid-like protein 1" FT /id="PRO_0000046028" FT DOMAIN 144..343 FT /note="Peptidase M12A" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211" FT DOMAIN 345..457 FT /note="CUB 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059" FT DOMAIN 458..570 FT /note="CUB 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059" FT DOMAIN 570..610 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 613..725 FT /note="CUB 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059" FT DOMAIN 725..765 FT /note="EGF-like 2; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 769..881 FT /note="CUB 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059" FT DOMAIN 882..998 FT /note="CUB 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059" FT ACT_SITE 237 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211" FT BINDING 236 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211" FT BINDING 240 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211" FT BINDING 246 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211" FT CARBOHYD 122 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 165 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 355 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 386 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 621 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 186..342 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211" FT DISULFID 206..228 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211" FT DISULFID 208..209 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211" FT DISULFID 345..371 FT /evidence="ECO:0000250" FT DISULFID 398..420 FT /evidence="ECO:0000250" FT DISULFID 458..484 FT /evidence="ECO:0000250" FT DISULFID 511..533 FT /evidence="ECO:0000250" FT DISULFID 574..585 FT /evidence="ECO:0000250" FT DISULFID 581..594 FT /evidence="ECO:0000250" FT DISULFID 596..609 FT /evidence="ECO:0000250" FT DISULFID 613..639 FT /evidence="ECO:0000250" FT DISULFID 666..688 FT /evidence="ECO:0000250" FT DISULFID 729..740 FT /evidence="ECO:0000250" FT DISULFID 736..749 FT /evidence="ECO:0000250" FT DISULFID 751..764 FT /evidence="ECO:0000250" FT DISULFID 769..795 FT /evidence="ECO:0000250" FT DISULFID 822..844 FT /evidence="ECO:0000250" FT DISULFID 882..912 FT /evidence="ECO:0000250" FT DISULFID 939..961 FT /evidence="ECO:0000250" SQ SEQUENCE 1008 AA; 114891 MW; 857A78A033B48413 CRC64; MKMLCWRLAL WLAAWAVCGK PSFCSALDYD YTYDFTEEDK AEAIDYKDPC KAAVFWGDIA LDDEDLKIFQ IDRTIDLTQH SNERLGHNTG GFGEHGMSKK RGALYQLIER IRRFGSGFEQ NNTSKGRTTV KFSGKNEKNR FPRAATSRTE RIWPGGVIPY VIGGNFTGTQ RAMFKQAMRH WEKYTCVTFI ERSDEESYIV FTYRPCGCCS YVGRRGNGPQ AISIGKNCDK FGIVVHELGH VIGFWHEHTR PDRDDHVTII RENIQPGQEY NFLKMEPGEV NSLGEPYDFD SIMHYARNTF SRGMFLDTIL PSRDDNGIRP AIGQRTRLSK GDIAQARKLY RCPACGETLQ ESTGNFSSPG FPNGYPSYTH CIWRISVTPG EKIVLNFTTM DLYKSSLCWY DYIEVRDGYW RKSPLLGRFC GDKLPEVLAS SDSRMWIEFR SSSNWVGKGF AAVYEAICGG EIHKNEGQIQ SPNYPDDYRP MKECVWKITV SENYNVGLTF QAFEIERHDN CAYDYLEIRD GMNENSPLIG HFCGYDKPED IRSTSNTLWM KFVSDGTVNK AGFAANFFKE EMMCQPDNGG CEQRCVNTLG SYQCACDPGY ELGPDKKSCE AACGGLLTKL NGTIPTPGWP KEYPPNKNCV WQVVAPTQYR ISMKFEFFEL EGNEVCKYDY VEIRSGLSSD SKLHGKFCGT EVPEVITSQY NNMRIEFRSD NTVSKKGFKA HFFSDKDECS KDNGGCQHEC INTVGSYVCQ CRNGFVLHEN KHDCKEAECE QKIHSPNGII MSPNWPDKYP SRKECTWEIS ATPGQRVKLT FNEFEIEQHQ ECAYDHLEVF DGESEKSPIL GRLCGSKIPE PLIATGNKMF LRFISDASVQ RKGFQATHST ECGGRLKAET KPKDLYSHAQ FGDNNYPVQA DCDWLLVAER GYRVELMFQT FEVEEEADCG YDYVELFDGH DKTAMRLGRF CGSGPPEEIY SAGETLLLHF HTDDTINKKG FHIRYRSIKY PDSVHTKK //