ID G3PNC6_GASAC Unreviewed; 1035 AA.
AC G3PNC6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif, 3 {ECO:0000313|Ensembl:ENSGACP00000019109.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000019109.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000019109.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000019109.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; G3PNC6; -.
DR STRING; 69293.ENSGACP00000019109; -.
DR MEROPS; M12.220; -.
DR Ensembl; ENSGACT00000019147.1; ENSGACP00000019109.1; ENSGACG00000014484.1.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000156085; -.
DR InParanoid; G3PNC6; -.
DR OMA; GYCDANK; -.
DR TreeFam; TF313537; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000014484; Expressed in liver.
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:0030198; P:extracellular matrix organization; 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; IPR013273; ADAMTS/ADAMTS-like.
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:SF158; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 3; 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; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 3.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
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; 4.
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:UP000007635};
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 212..416
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1000..1035
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT ACT_SITE 355
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 354
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 358
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 364
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 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 289..338
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 332..411
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 371..397
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 438..463
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 449..472
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 458..491
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 485..496
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 519..556
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 523..561
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 534..546
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1035 AA; 116008 MW; 8B344BCE20F6656E CRC64;
LITPFSTDSH GRYLSHLLSA AHKQRTKREA PPPGGAEQEL FFNISAFGEE FHLRLRPNNR
LVAPGAVVEW HDADDGGEQG GNQTERNPHR ELLKTDCTFI GDITDVPGAS VAINNCDGLA
GMIRTDADEY FIEPLERGTQ ELEHQGRVHV VYRRSALLQP PADPPGDDDD LPPGYPMASE
DLRSVAFAAG AITERFNMQQ DNRDKHAGED DYNIEILLGV DDSVVRFHGK EHVQNYLLTL
MNIVNEIYHD ESLGVHINVV LVRMIMLGYA KSISLIERGN PSRSLENVCR WAFVQQKSDS
EHAEHHDHAI FLTRQGFGPT GMQGYAPVTG MCHPVRSCTL NHEDGFSSAF VVAHETGHVL
GMEHDGQGNR CGDETAMGSV MAPLVQAAFH RYHWSMCSGR ELKRYISTYD CLLDDPFKHD
WPQLPELPGI NYSMDEQCRF DFGVGYKICT SFRTFDPCKQ LWCSHPDNPY FCKTKKGPPL
DGTECNPGKW CYKGHCMWKN PNQVKQDGAW GSWSKYGSCS RSCGTGVRFR TRQCSSPPPS
NGGQDCPGLN YEAALCNADD CPKHYEDFRA QQCQLRNSHF EFQNAKHHWL PYEHPDASKR
CHLYCQSKES GDVAYMKQLV HDGTRCSYKD AYSICARGEC LKVGCDREIG SSKAEDRCGV
CGGDNSHCRT VKGSFTRAPK KPVGEGSLKM FLIPPGARRV IVQEHEASPH ILAIKNQATG
HYILNGRGEE AASRSFIDLG VEWNYILEDQ VEMLHTDGPL HDPVLVLVII PKDNETRSTL
MYKYIIHEDS VPVNNNNVIQ EDTYEWALKS WSPCSKPCAG GFQYTKYGCR KKGDTKMVHR
GYCDAGKKPK PIRRMCNLQD CTQPQWSSDD WEHCTKTCGS LGFQIRTVRC VQCLSDGTNR
SVHSKYCSGE KPESRRPCGR VSCPAQWRTG AWSECSVTCG EGMERRLVTC RIGDQCNGDK
PETVRFCRPA ACHDILPFSS QQQYNVAVIR FQPAPSSPRS DEPCSGDKSI FCQMEVLARY
CSIPGYSKLC CDSCS
//
