ID A0A3B3ZV76_9GOBI Unreviewed; 1183 AA.
AC A0A3B3ZV76;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPMGP00000008191.1};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000008191.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000008191.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B3ZV76; -.
DR STRING; 409849.ENSPMGP00000008191; -.
DR Ensembl; ENSPMGT00000008718.1; ENSPMGP00000008191.1; ENSPMGG00000006787.1.
DR Proteomes; UP000261520; Unplaced.
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 Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 2.
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; 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:SF167; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 18; 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; 3.
DR Pfam; PF00090; TSP_1; 2.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00209; TSP1; 6.
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.
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 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 284..470
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1140..1182
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 202..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 360..407
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 386..393
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 401..465
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 425..449
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 493..518
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 504..525
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 513..544
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 538..549
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 573..610
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 577..615
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 588..600
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1183 AA; 131580 MW; B74C768337AFC34B CRC64;
TQLLMHRDLL HISPGPGPQW ALLLNNACKL RAPIPQVITA CALYYVFVSP VEVDSEGLYL
SHDLSRNSHR SRRSLSSFSP SSSLHYHLSA FGRDMQLDLR PSSVVGPGFT VQTLSSGGIS
TVTVDSAYHS CLYQGIVHNV SSSSAAISTC AGLSGLIRIS QEEYLISPLP DHLAQKHNYN
APEGHHPHVV YKRSAEHIIN RRSAEPSSTN SSTADSPYRH DHHHPHHHDN QQDKMHFCGR
RKQYAPKPPT VDRFIMPDEF ATPGEEGAGR SKRSPILSNR VGSLNVETLV VADRKMLEKH
GRDNVTTYVL TVMNMVSSLF KDGTIGTDIN VVVVSLLLLE QDPVGLTINH HADQSLNSFC
QWQSGLMGKG GKRHDHAVLL TGLDICSWKN EPCDTLAKSF CTLSQSCHFS FVNFGMIHDG
EGNPCRKTEG NIMSPTLAGN NGVFSWSTCS RQYLSRFLGT AQASCLVDEP RQIGQYKYPE
QLPGQLYDAD IQCKWQFGVK AKLCSLDFVK DICKSLWCHR TGQRCETKFM PAAEGTTCGP
DMWCRRGQCV KYGEHGPKAV HGQWSAWSEW SECSRTCGGG VMYRERSCNS PRPQNNGKFC
EGSSRLNQLC NTRPCPPNAV DFRAQQCAEY NSKPFRGWYY KWKPYTKVDD EDVCKLYCIA
EDYDFFFAMS SKVKDGTSCS EHKEDVCIDG VCEAVGCDQM LGSKASLDAC GVCKGDNSSC
KFFKGQYTLQ HRANEYYSMV TVPAGARSIR IQEKEVSTSY LAARSLKRKY YLTGDWTVDW
PGKFHFGGTV FDYQRSFNKP ESLYAAGPTN ETLVFEILLQ GKNPGVVWEY TLPRTERKPD
YSWGVVRSDC SAPCAGGRIS TKAICLQDQK VQVNSSMCNP HTKPTLGSHL CNTQPCPAYW
SAGEWETCSR SCGGGQQARV LRCFRRVTYQ REEAVVQSLC PVMSPAQVQP CNTQACPPEW
STGAWSQCSK TCGRGMRKRS VFCRSTDPGA SAVVVPDSMC RQHHRPKAQE ICVLRRCPKS
DRLLWTPTPW GECSRSCGSG VQKRELFVEL PSRRCRNMAK PLLDLQQPCN RGACPEPPHI
SPGRHPSSSM VSGWYSSPWQ QCSVTCGGGV QTRAVQCLRQ GRPTAGCLPH QKPVTSRACN
THFCPAVPPV PGHSWCHLVP QHGVCNHKFY GQQCCKSCSS KRH
//
