ID A0A3Q0GPH5_ALLSI Unreviewed; 797 AA.
AC A0A3Q0GPH5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9-like {ECO:0000313|RefSeq:XP_025061671.1};
GN Name=LOC102369047 {ECO:0000313|RefSeq:XP_025061671.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025061671.1};
RN [1] {ECO:0000313|RefSeq:XP_025061671.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_025061671.1; XM_025205886.1.
DR AlphaFoldDB; A0A3Q0GPH5; -.
DR KEGG; asn:102369047; -.
DR InParanoid; A0A3Q0GPH5; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0016020; C:membrane; 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:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF122; ADAM METALLOPEPTIDASE DOMAIN 9; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..797
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018225909"
FT TRANSMEM 694..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..408
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 416..502
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 638..672
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 725..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..797
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 354
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 474..494
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 662..671
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 797 AA; 88222 MW; 04CCB9CB69AED4F8 CRC64;
MLKCCLLLFI FGLTLLGKCV LTAGALSRQM SSVSAFEIII PQHLMGREKR NTHFPEEHSD
DNLSYSVQTE NGTYILELKK NKKLVSEDFV LNTYSKNGQL EATHSKIKTH CYYRGVVEGV
AESMLALSTC DGLRGILYVG DKWYGIEPLD GSATFEHMFY QLEHAQQTSF LCGVPNDNLH
HEIHVKNFLL HSEISHANFS SEKLLRKKRS ALPQKNYVEL FVVVDNNRYL QKLSSATAVQ
KEVVELINYI DGMYSALNIQ IVLVGIEIWS DKNRIAVMEG SAGDVLQRFV SWREKDLLKR
SRNDASHLII GRDSFGGAVG MAFVGAICSQ VHGGSISTLN HDKVLGHATV VAHELGHNLG
MKHDDGRCPQ SFIMFSTANG SQNFSTCSAK DFENLILNGG GNCLKNPPKP NDIYTEPNCG
NEILDKNEEC DCGKPEECTN PCCEAATCTL KSGSQCADGL CCENCRFKVA GVECRPKMDF
CDLPEHCNGT YPYCPDDVYT MNGYPCNNMK EYCYYGVCQD FDSQCKSLYG KGARKAPDDC
FKIANIKGDR FGNCGMSGGR YRKCPDEHSL CGKLHCTSDS LQNLPAWTLF NNLTGVVCLT
TDFDLGSDFP DPAQVHAGTA CGEGKACINF ECVNASQLGY SCDVKQKCND RGVCNNHGNC
HCNYGWAPPF CDRSGYGGSI DSGPTHIDTS LRDGLLVFFL FVVPVLIGIV IAFIKRDAIK
RKFCRKSRRQ PRANNTQQAR QSNGPNQNAT RNDWPATSNS GMFTISHFPN PRQQIPSQFP
AVPPRPPRPP VPPRPVV
//
