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
//