TLL1_XENLA
ID TLL1_XENLA Reviewed; 1007 AA.
AC Q8JI28;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Tolloid-like protein 1;
DE EC=3.4.24.-;
DE AltName: Full=Metalloprotease xolloid-like;
DE AltName: Full=Xenopus tolloid-like protein 1;
DE AltName: Full=Xlr;
DE Flags: Precursor;
GN Name=tll1; Synonyms=xlr;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, CHARACTERIZATION, AND
RP FUNCTION.
RX PubMed=12464431; DOI=10.1016/s0925-4773(02)00359-3;
RA Dale L., Evans W., Goodman S.A.;
RT "Xolloid-related: a novel BMP1/Tolloid-related metalloprotease is expressed
RT during early Xenopus development.";
RL Mech. Dev. 119:177-190(2002).
CC -!- FUNCTION: Protease which processes procollagen C-propeptides, such as
CC chordin. Required for the embryonic development. Predominant protease,
CC which in the development, influences dorsal-ventral patterning and
CC skeletogenesis. {ECO:0000269|PubMed:12464431}.
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 -!- INTERACTION:
CC Q8JI28; Q91713: chrd; NbExp=2; IntAct=EBI-1997794, EBI-1997746;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the marginal zone of mid-gastrulae,
CC and in ventral and lateral sectors. At neurula stages, strongly
CC expressed around the blastopore and in the pharyngeal endoderm, and
CC more weakly expressed throughout the ventral half of the embryo.
CC Transcripts are detected in the nervous system, particularly the
CC hindbrain and spinal cord, and tailbud of tailbud stage embryos, with
CC weaker expression in the anterior nervous system, otic vesicle, heart,
CC and pronephric duct. Transcription is increased by BMP4 and decreased
CC by Noggin and tBR, indicating that it is regulated by BMP signaling.
CC {ECO:0000269|PubMed:12464431}.
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DR EMBL; AF393242; AAM73675.1; -; mRNA.
DR RefSeq; NP_001083894.1; NM_001090425.1.
DR AlphaFoldDB; Q8JI28; -.
DR SMR; Q8JI28; -.
DR IntAct; Q8JI28; 2.
DR MEROPS; M12.016; -.
DR GeneID; 399178; -.
DR KEGG; xla:399178; -.
DR CTD; 399178; -.
DR Xenbase; XB-GENE-865326; tll1.S.
DR OrthoDB; 170905at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 399178; Expressed in neurula embryo and 12 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 2.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein 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..25
FT /evidence="ECO:0000255"
FT PROPEP 26..142
FT /evidence="ECO:0000250"
FT /id="PRO_0000046029"
FT CHAIN 143..1007
FT /note="Tolloid-like protein 1"
FT /id="PRO_0000046030"
FT DOMAIN 143..342
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 344..456
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 457..569
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 569..610
FT /note="EGF-like 1; calcium-binding"
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 REGION 115..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
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 185..341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 205..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 207..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 344..370
FT /evidence="ECO:0000250"
FT DISULFID 397..419
FT /evidence="ECO:0000250"
FT DISULFID 457..483
FT /evidence="ECO:0000250"
FT DISULFID 510..532
FT /evidence="ECO:0000250"
FT DISULFID 573..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 1007 AA; 114365 MW; 3F33C686A7EF230C CRC64;
MNMPSWLIFL LTGWTFCGNF FACGGLDYDY PNYENEEEKN EAIDYKDPCK AVVFWGDIAL
DEEDLKMFHI DRTIDLTQHS NEKLGHTTGG LEEHDLSKKR GALYQLIERI RRFGSGQENT
TANSQKVDNN QSGKSKKIRI PRAATSRTER IWPGGVIPYV IGGNFTGSQR AMFKQAMRHW
EKHTCVTFIE RTDEESYIVF TYRPCGCCSY VGRRGNGPQA ISIGKNCDKF GIVVHELGHV
IGFWHEHTRP DRDDHVTIIR ENIQPGQEYN FLKMEPGEVH SLGESYDFDS IMHYARNTFS
RGMFLDTILP SRDENGLRPP IGQRTRLSKG DIAQARKLYR CPACGETLQE STGNFSSPGF
PNGYPSYTHC IWRISVTPGE KIVLNFTTMD LYKSSLCWYD YIEVRDGYWK KSPLLGRFCG
DKLPDVLTST DSRMWIEFRS SSNWVGKGFA AVYEAICGGE IHKDAGQIQS PNYPDDYRPL
KECVWKITVA ENYNVGLTFQ AFEIERHDNC AYDYLEVRDG SSENSPLIGH FCGYDKPEDI
RSTSNTLWMK FVSDGTVNKA GFAANFLKEE DECARPDNGG CEQRCVNTLG SYKCSCDPGY
ELAPDKKSCE AACGGLLTKL NGTITTPAWP KEYPPNKNCV WQVVAPSQYR ISMKFDYFEL
EGNEVCKYDY VEVRSGLSSD SKLHGKFCGT EVPEVITSQF NNMRIEFKSD NTVSKKGFRA
HFFSDKDECS KDNGGCQHEC INTIGSYVCQ CRNGFVLHDN KHDCKEAECE HRIHSSNGVI
TSPNWPDKYP SRKECTWEIS ATPGHRVKLS FSEFEIEQHQ ECAYDHLEVF DGETEKSSIL
GRLCGSKVPE PLVATGNEMF IRFVSDASVQ RKGFQATHST ECGGRLKAEA KPRDLFSHAQ
FGDNNYPVQA DCEWILMTER GLRIELNFQT FEVEEEADCG YDFMELFDGH DASAMRLGRF
CGSGPPEEIV STGDAVLIHF HTDDTISKKG FHIRYRSVKY QDILHTK
