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Database: UniProt
Entry: G1KY76_ANOCA
LinkDB: G1KY76_ANOCA
Original site: G1KY76_ANOCA 
ID   G1KY76_ANOCA            Unreviewed;      1100 AA.
AC   G1KY76;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 3.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 6 {ECO:0000313|Ensembl:ENSACAP00000020687.3};
GN   Name=ADAMTS6 {ECO:0000313|Ensembl:ENSACAP00000020687.3};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000020687.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000020687.3, ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000020687.3,
RC   ECO:0000313|Proteomes:UP000001646};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000020687.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR   AlphaFoldDB; G1KY76; -.
DR   STRING; 28377.ENSACAP00000020687; -.
DR   Ensembl; ENSACAT00000025788.3; ENSACAP00000020687.3; ENSACAG00000027734.3.
DR   eggNOG; KOG3538; Eukaryota.
DR   GeneTree; ENSGT00940000156571; -.
DR   HOGENOM; CLU_000660_5_1_1; -.
DR   Proteomes; UP000001646; Chromosome 2.
DR   Bgee; ENSACAG00000027734; Expressed in forelimb bud and 10 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR   Gene3D; 2.60.120.830; -; 1.
DR   Gene3D; 3.40.1620.60; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 4.
DR   InterPro; IPR041645; ADAMTS_CR_2.
DR   InterPro; IPR045371; ADAMTS_CR_3.
DR   InterPro; IPR010294; ADAMTS_spacer1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR010909; PLAC.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR13723:SF27; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 6; 1.
DR   PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR   Pfam; PF17771; ADAMTS_CR_2; 1.
DR   Pfam; PF19236; ADAMTS_CR_3; 1.
DR   Pfam; PF05986; ADAMTS_spacer1; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF08686; PLAC; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   Pfam; PF19030; TSP1_ADAMTS; 4.
DR   SMART; SM00209; TSP1; 4.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS50092; TSP1; 5.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00276}; Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1100
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5033068992"
FT   DOMAIN          231..449
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          1062..1100
FT                   /note="PLAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50900"
FT   ACT_SITE        385
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         384
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         394
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   1100 AA;  123995 MW;  AA83EF98CE44CC9F CRC64;
     ERYHINILKW ALLLCYCPEF LSYLEHYQLT VPIRVDHNGA FLSFTVKNTK STRRKKRSTY
     DQELAVSNLF FKLSAYGKHF HLNLTLNTDL VSKHFTVEYW GKDGPQWKHD FLDNCHYTGY
     LHGEHGTTKV ALSNCNGLHG VIATEDEEYF IEPLRNLTEN SSNFSYESGH PHVIYKKSAI
     YHHLTAWSAV TFPWKHKPWW LNNTDAFPTL HPVNHTLSSN HRLKRSISTE RFVETLVVAD
     KMMVGYHGRK DIEHYILSVM NIVAKLYRDS SLGNVVNIIV TRLIVLTEDQ PNLEINHHAD
     KSLDSFCKWQ KSILSHQSDG NTISENGIAH HDNAVLITRY DICTYKNKPC GTLGLASVAG
     MCEPERSCSI NEDIGLGSAF TIAHEIGHNF GMNHDGIGNS CGTKGHEAAK LMAAHITANT
     NPFSWSACSR DYITSFLDSG RGTCLDNEPP KRDFLYPAVA PGQVYDADEQ CRFQYGATSR
     QCKYGEVCRE LWCLSKSNRC VTNSIPAAEG TLCQTGSIEK GWCYQGDCVP FGTWPQSIDG
     GWGPWNCEKC MVFSLLLLLF FQMYKICNMF SRPSGGGKYC LGERKRYRSC NTDPCPFGAR
     DFREKQCADF DNMPFRGKYY NWKPYTGGGV KPCALNCLAE GYNFYTERAP AVIDGTQCNA
     DSLDICINGE CKHVGCDNIL GSEAKEDRCR VCGGDGSTCE VIEGFFNDTL PRGGYMEVVQ
     IPKGSVHIEI KEVTVSKNYI ALKSEEDDYY INGAWTIDWP RKFDVAGTAF HYKRPADEAE
     SLEALGPTSE NLIVMILLQE QNLGIRYKFN VPISRTGSGD NEVGFTWNHL PWSECSATCA
     GGSQKQEIVC KRLDDNSIVQ NNYCDLDNKP PENQRTCNTE PCPTEWFIGD WSECSKTCDG
     GMRSRTVLCI RKIGPSEEET LDSIHCLTHR PIEKESCNNQ SCPPQWIPLD WSECTPKCGP
     GFKHRIVLCK SSDLSKTFPV AHCQEENKPP VRMRCSLGRC PPPRWIMGDW GQCSAQCGLG
     QQMRTVQCLS YTGQASSDCP DTLRPPSMQQ CESKCDSTPI SNTEECKDVN KVAYCPLVLK
     FKFCSRAYFR QMCCKTCQGH
//
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