TLL2_XENLA
ID TLL2_XENLA Reviewed; 1019 AA.
AC O57382;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Tolloid-like protein 2;
DE EC=3.4.24.-;
DE AltName: Full=Metalloprotease xolloid;
DE AltName: Full=Xenopus tolloid;
DE Flags: Precursor;
GN Name=tll2; Synonyms=xld;
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, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Ovary;
RX PubMed=9520331; DOI=10.1006/dbio.1997.8840;
RA Goodman S.A., Albano R., Wardle F.C., Matthews G., Tannahill D., Dale L.;
RT "BMP1-related metalloproteinases promote the development of ventral
RT mesoderm in early Xenopus embryos.";
RL Dev. Biol. 195:144-157(1998).
CC -!- FUNCTION: Protease which specifically processes prolysyl oxidase and
CC maybe also chordin. Required for the embryonic development. Predominant
CC protease, which in the development, influences dorsal-ventral
CC patterning and skeletogenesis. In embryos, inhibits the development of
CC dorsoanterior structures and ventralizes activin-induced dorsal
CC mesoderm in animal caps. {ECO:0000269|PubMed:9520331}.
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:9520331}.
CC -!- DEVELOPMENTAL STAGE: Initial uniform expression becomes localized to
CC two posterior ectodermal patches flanking the neural plate and later to
CC the inner ectoderm of the developing tailbud. Also expressed in dorsal
CC regions of the brain during tailbud stages and is especially abundant
CC in the ventricular layer of the dorsal hindbrain caudal to the otic
CC vesicle. {ECO:0000269|PubMed:9520331}.
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; Y09661; CAA70854.1; -; mRNA.
DR RefSeq; NP_001084377.1; NM_001090908.1.
DR AlphaFoldDB; O57382; -.
DR SMR; O57382; -.
DR MEROPS; M12.015; -.
DR PRIDE; O57382; -.
DR GeneID; 399469; -.
DR KEGG; xla:399469; -.
DR CTD; 399469; -.
DR Xenbase; XB-GENE-478934; tll2.L.
DR OrthoDB; 170905at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 399469; Expressed in spleen 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 Pfam; PF00008; EGF; 1.
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 2: Evidence at transcript level;
KW Calcium; Cleavage on pair of basic residues; Developmental protein;
KW Differentiation; Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT PROPEP 32..152
FT /evidence="ECO:0000250"
FT /id="PRO_0000046040"
FT CHAIN 153..1019
FT /note="Tolloid-like protein 2"
FT /id="PRO_0000046041"
FT DOMAIN 153..352
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DOMAIN 354..466
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 467..579
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 579..620
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 623..735
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 735..775
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 779..891
FT /note="CUB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 892..1008
FT /note="CUB 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 83..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 246
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 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 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 195..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 215..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 217..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 354..380
FT /evidence="ECO:0000250"
FT DISULFID 407..429
FT /evidence="ECO:0000250"
FT DISULFID 467..493
FT /evidence="ECO:0000250"
FT DISULFID 520..542
FT /evidence="ECO:0000250"
FT DISULFID 583..595
FT /evidence="ECO:0000250"
FT DISULFID 591..604
FT /evidence="ECO:0000250"
FT DISULFID 606..619
FT /evidence="ECO:0000250"
FT DISULFID 623..649
FT /evidence="ECO:0000250"
FT DISULFID 676..698
FT /evidence="ECO:0000250"
FT DISULFID 739..750
FT /evidence="ECO:0000250"
FT DISULFID 746..759
FT /evidence="ECO:0000250"
FT DISULFID 761..774
FT /evidence="ECO:0000250"
FT DISULFID 779..805
FT /evidence="ECO:0000250"
FT DISULFID 832..854
FT /evidence="ECO:0000250"
FT DISULFID 892..922
FT /evidence="ECO:0000250"
FT DISULFID 949..971
FT /evidence="ECO:0000250"
SQ SEQUENCE 1019 AA; 114892 MW; 50CCE8B7E3B42C6E CRC64;
MSCGSPQVMM TLWTLTCVGL ILLGAIRLSL GLDYDLESFD YLMEDNPEEF DYKDPCKAAA
YWGDIALDED DLKWIFKNKS NDLRNTRHNQ THPTTDNFSE KLGTGSQNET SSNLNSKKVK
KGSRLKLLIA EKAATETNST FQVQTSNDRV RRAATSRTER IWPGGIIPYA IAGNFTGTQR
AIFKQAMRHW KKHTCVTFVE RTDEESFIVF TYRPCGCCSY VGRRGGGPQA ISIGKNCDKF
GIVVHELGHV VGFWHEHTRP DRDEHVSIIR ENIQPGQEYN FLKMEPGEVS SLGETYDFDS
IMHYARNTFS RGVFLDTILP RRIDTSVRPT IGQRIRLSQG DIAQAKKLYK CPACGETLQD
SSGNFSAPGY PSGYPSYTHC IWRISVTPGE KIILNFTTMD LFKSRLCWYD YIEIRDGYWR
KAALLGRLCG DKLPDPIISS DSKLWIEFRS SSNILGKGFF AAYEAICGGD IKKDSGQIQS
PNYPDDYRPA KECIWKITVS EGFLVGLSFQ AFEIERHDNC AYDYLEVRDG FSEDHALIGR
FCGYEKPEDI KSTSNKLWIK FASDGSINKA GFSANFFKEM DECSRPDNGG CSQRCVNTLG
SYKCVCEPGF ELTADKKSCE AACGGFITQL NGTITSPGWP KEYPTNKNCV WQVVAPAQYR
ISLQFEVFEL EGNDVCKYDY LEIRSGLSSE SKLHGKFCGP EKPEVITSQG NTVRIEFKSD
NTVSKKGFKA NFFSDKDECS KDNGGCQHDC VNTFGSYICQ CKNGFILHEN GHDCKEAGCE
QKLLNAEGTI SSPNWPEKYP SRKECTWDIS VTAGHRVKLV FTDFEIEQHQ ECAYDHLELY
DGPNGKAAIL GRFCGSKEPS PVVASTNNMF LRFYSDASVQ RKGFQAKYSP ECGGRLKAEI
QTNDIYSHAQ FGDNNYPVQS NCEWVIVAED GYGVELIFQT FEIEEESDCG YDYMEVYDGY
DSTAPRLGRY CGSGPPEEMY SAGDSIMIRF HTDDTINKKG FHGQYTSTKF QDALHMRRK
