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Tolloid-like protein 1 (EC 3.4.24.-) (Chicken tolloid-like protein 1) (Metalloprotease colloid)

 TLL1_CHICK              Reviewed;        1008 AA.
Q9DER7;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 104.
RecName: Full=Tolloid-like protein 1;
EC=3.4.24.-;
AltName: Full=Chicken tolloid-like protein 1;
AltName: Full=Metalloprotease colloid;
Flags: Precursor;
Name=TLL1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
PubMed=10940628; DOI=10.1016/S0925-4773(00)00382-8;
Liaubet L., Bertrand N., Medevielle F., Pituello F.;
"Identification by differential display of a chicken tolloid-related
metalloprotease specifically expressed in the caudal notochord.";
Mech. Dev. 96:101-105(2000).
-!- FUNCTION: Protease which processes procollagen C-propeptides, such
as chordin, probiglycan and prolysyl oxidase. Required for the
embryonic development. Predominant protease, which in the
development, influences dorsal-ventral patterning and
skeletogenesis (By similarity). {ECO:0000250}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10940628}.
-!- DEVELOPMENTAL STAGE: Expressed at HH stage-10, with a restricted
expression to the caudal notochord expanding between Hensen node
and the last individualized somite. No expression in the ventral
midline of the neural plate. The regionalized expression in the
notochord persists at least until HH-stage 15. At HH stage-13,
expression can be observed in the roof of the caudal diencephalon
and expands, at HH stage-15, caudally to the mesencephalon.
{ECO:0000269|PubMed:10940628}.
-!- SIMILARITY: Belongs to the peptidase M12A family. {ECO:0000305}.
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EMBL; AJ012462; CAC08820.1; -; mRNA.
UniGene; Gga.239; -.
ProteinModelPortal; Q9DER7; -.
SMR; Q9DER7; -.
STRING; 9031.ENSGALP00000015567; -.
MEROPS; M12.016; -.
PaxDb; Q9DER7; -.
eggNOG; KOG3714; Eukaryota.
eggNOG; ENOG410ZPX7; LUCA.
HOGENOM; HOG000236339; -.
HOVERGEN; HBG004859; -.
InParanoid; Q9DER7; -.
PhylomeDB; Q9DER7; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
CDD; cd00041; CUB; 5.
CDD; cd04281; ZnMc_BMP1_TLD; 1.
Gene3D; 2.60.120.290; -; 5.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR015446; BMP_1/tolloid-like.
InterPro; IPR000859; CUB_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001506; Peptidase_M12A.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR035914; Sperma_CUB_dom_sf.
InterPro; IPR034036; ZnMP_TLD/BMP1.
Pfam; PF01400; Astacin; 1.
Pfam; PF00431; CUB; 5.
PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
PRINTS; PR00480; ASTACIN.
SMART; SM00042; CUB; 5.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 2.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF49854; SSF49854; 5.
PROSITE; PS01180; CUB; 5.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Calcium; Complete proteome; Developmental protein; Differentiation;
Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase;
Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 26 {ECO:0000255}.
PROPEP 27 143 {ECO:0000250}.
/FTId=PRO_0000046027.
CHAIN 144 1008 Tolloid-like protein 1.
/FTId=PRO_0000046028.
DOMAIN 345 457 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 458 570 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 570 610 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 613 725 CUB 3. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 725 765 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 769 881 CUB 4. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 882 998 CUB 5. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
REGION 144 344 Metalloprotease. {ECO:0000250}.
ACT_SITE 237 237 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 236 236 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 240 240 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 246 246 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 355 355 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 386 386 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 621 621 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 345 371 {ECO:0000250}.
DISULFID 398 420 {ECO:0000250}.
DISULFID 458 484 {ECO:0000250}.
DISULFID 511 533 {ECO:0000250}.
DISULFID 574 585 {ECO:0000250}.
DISULFID 581 594 {ECO:0000250}.
DISULFID 596 609 {ECO:0000250}.
DISULFID 613 639 {ECO:0000250}.
DISULFID 666 688 {ECO:0000250}.
DISULFID 729 740 {ECO:0000250}.
DISULFID 736 749 {ECO:0000250}.
DISULFID 751 764 {ECO:0000250}.
DISULFID 769 795 {ECO:0000250}.
DISULFID 822 844 {ECO:0000250}.
DISULFID 882 912 {ECO:0000250}.
DISULFID 939 961 {ECO:0000250}.
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


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