TLL1_CHICK
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 03-AUG-2022, entry version 117.
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;
CC Evidence={ECO:0000255|PROSITE-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}.
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DR EMBL; AJ012462; CAC08820.1; -; mRNA.
DR AlphaFoldDB; Q9DER7; -.
DR SMR; Q9DER7; -.
DR STRING; 9031.ENSGALP00000015567; -.
DR MEROPS; M12.016; -.
DR PaxDb; Q9DER7; -.
DR VEuPathDB; HostDB:geneid_395441; -.
DR eggNOG; KOG3714; Eukaryota.
DR InParanoid; Q9DER7; -.
DR OrthoDB; 170905at2759; -.
DR PhylomeDB; Q9DER7; -.
DR Proteomes; UP000000539; Unplaced.
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; cd04281; ZnMc_BMP1_TLD; 1.
DR Gene3D; 2.60.120.290; -; 5.
DR Gene3D; 3.40.390.10; -; 1.
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 Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 5.
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; SSF49854; SSF49854; 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
