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Database: UniProt
Entry: H9GFS0_ANOCA
LinkDB: H9GFS0_ANOCA
Original site: H9GFS0_ANOCA 
ID   H9GFS0_ANOCA            Unreviewed;      1100 AA.
AC   H9GFS0;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 17 {ECO:0000313|Ensembl:ENSACAP00000009703.3};
GN   Name=ADAMTS17 {ECO:0000313|Ensembl:ENSACAP00000009703.3};
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:ENSACAP00000009703.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000009703.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000009703.3};
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:ENSACAP00000009703.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
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; H9GFS0; -.
DR   STRING; 28377.ENSACAP00000009703; -.
DR   MEROPS; M12.027; -.
DR   Ensembl; ENSACAT00000009901.3; ENSACAP00000009703.3; ENSACAG00000009834.3.
DR   eggNOG; KOG3538; Eukaryota.
DR   GeneTree; ENSGT00940000158773; -.
DR   HOGENOM; CLU_000660_8_0_1; -.
DR   TreeFam; TF313537; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000009834; Expressed in hindlimb bud and 6 other cell types or tissues.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
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; 5.
DR   InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR   InterPro; IPR041645; ADAMTS_CR_2.
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   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR13723:SF151; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 17; 1.
DR   PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR   Pfam; PF17771; ADAMTS_CR_2; 1.
DR   Pfam; PF05986; ADAMTS_spacer1; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   Pfam; PF19030; TSP1_ADAMTS; 4.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   SMART; SM00209; TSP1; 5.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS50092; TSP1; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR613273-3};
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,
KW   ECO:0000256|PIRSR:PIRSR613273-2};
KW   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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT   DOMAIN          224..444
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          1053..1092
FT                   /note="PLAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50900"
FT   REGION          188..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        382
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         227
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         227
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         329
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         381
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         385
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         391
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         439
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   DISULFID        300..365
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        340..347
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        359..439
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   DISULFID        398..423
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        468..499
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        479..507
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        494..526
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        520..531
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        554..591
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        558..596
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        569..581
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ   SEQUENCE   1100 AA;  123158 MW;  9480088B1E60F53C CRC64;
     MLLFLTKPRN EDIWRVIFTI SFSPSLSPFT ASDDVEVVIP EWVPQERIHF LQAERSQVWG
     GRSRRSASFD PEEEDAEAAL FIRLPAGSGL HLDSDLYLSL RPNAQFLAPG FSVQEIPEDP
     SVERNAGVDR SCFYTGHVLN RSVDSFASLS TCNGLVGLIQ IGSEQVQIHP VNTSETLFDG
     KEHFLRRKRS ARSTRPARPG RQKKAKLTDD WRERRNAIRL MNEYTVETLV VADSDMVQYH
     GADAAQRFIL TVMNMVYNMF QHQSLGVKVN IRVTKLVLLR RRPAKLSIGH HGERSLESFC
     HWQNEEFGGA KYLGNNQVPG ARDDTPPVDA AVFVTRTDFC VHKDEPCDTV GIAYLGGICS
     AKRKCVLAED NGLNLAFTIA HELGHNMGMS HDDDHLSCAG RSHIMSGEWV KGRNPSDLSW
     SSCSRDDLEK FLKSKVSTCL LVTDPRSRYA VRLPYKLPGM HYSADEQCQI LFGTNATFCK
     NMEPFPILLA HLMCAGLWCL VEGDASCKTK LDPPLDGTEC GADKWCRTGE CVSKTPIPEH
     VDGDWNMWSQ WSMCSRTCGT GARFRQRKCD NPPPGPGGKN CRGASVEHTV CENVPCPKGA
     PTFRDQQCQS HDRYTKKKSL WTAVIMDGPQ FGRGPEEGDS VMNHGPCSPA QDIKIGCDGI
     IGSAAREDRC GICNGDGKTC KVVKGDFNHT KGMGYIEAAV IPAGARRIRV MEDKPAHSFL
     ALKDSSKKSI NSDWKIELPG EFQIAGTTVR YVRRGLWEKI SAKGPTKIPL HLMVLLFHDQ
     NYGIHYEYTI PVNYSAENRS EPEHQQESLY IWTHSGWEGC SVQCGGGERK TIVSCTQIVN
     KTMMLVNDSA CQRVTRPEPQ VRRCNVHPCQ SRWVAGQWSP CSATCAKGTQ RREVTCVYQL
     QNGSYVNTRD LYCLGPKPTA VQSCEGRDCV SIWEASEWSK CSSSCGRGKQ KRTVTCTNSQ
     GKCDAATRPR DEEECEDHTG CYEWKTGDWS KCSSTCGKGL QSRVVQCMHK VTGRHGNECP
     TLSKPAAYRQ CHQEACNEKI NVNTITSPRL AALTYKCAGD QWTVYCRVIR EKNLCQDMRW
     YQRCCQTCRD FYASKMQQKS
//
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