ID A0A2Y9DX52_TRIMA Unreviewed; 760 AA.
AC A0A2Y9DX52;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 18 {ECO:0000313|RefSeq:XP_004382194.1};
GN Name=LOC101342608 {ECO:0000313|RefSeq:XP_004382194.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004382194.1};
RN [1] {ECO:0000313|RefSeq:XP_004382194.1}
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_004382194.1; XM_004382137.1.
DR AlphaFoldDB; A0A2Y9DX52; -.
DR STRING; 127582.A0A2Y9DX52; -.
DR GeneID; 101342608; -.
DR KEGG; tmu:101342608; -.
DR InParanoid; A0A2Y9DX52; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0016020; C:membrane; 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:SF158; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 18; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 722..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 218..415
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 424..513
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 654..688
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 35..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 371..376
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 678..687
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 760 AA; 85798 MW; E9A8FF30CBE9B185 CRC64;
MAQLAWSLAR ITAVKALRQV KAELARDTWT HEMQTLGRRA GGRQRSRKEH TGDRKRGRFQ
VFSMYRRKSN ESSGPERKVI YIITIDGKPY TLHLKKQSFL PQNFLVYTYN ETGSLRSESS
YLKMHCHYQG YVADFPNSVV TLSICSGLRG FLQFENITYG IEPMESSARF EHMIFQVKND
IPDVPMLAEN GGNTWQKDQL YKVHMSSQNK PLLKQLPQYL EMHIIVEKTL YDYMGSETMA
VTQKIVQIIG LVNTMFTQFK LTVILSSLEL WSDKNQISTN GDTDDLLQRF LAWKRDYFVL
RPHDIAYLLI YRKHPKYVGA TFPGTICNKS YDAGIALYPD AISLEGFSVI VAQLLGLNIG
LTYDDINKCS CPRATCIMNR QAPHSSGIKI FSNCSMHDYT HLVSKFEPKC LQNLLHLQPL
YKNQPVCGNG ILEPNEECDC GSEEECQFKN CCDYNTCKLK GSVKCGSGAC CTSKCELSIA
GTPCRKSIDE ECDFAEYCNG TSSNCVPDTY IMNGYMCKLG TAYCYNGRCQ TTDNQCAEVF
GKGAKGAPLA CFQEVNSLHD RFGNCGFNNS QSLPCEQKDV LCGKLACVWP HENTYKNDIQ
STVYSYIQGH VCMSITIGSS VSSDGRDYAY VADGTVCGPQ MYCLNKTCKE ASLMGYNCNA
TTKCKGNGIC NNFGNCQCFP GYRPPDCEFQ IGSPGGSIDD GNVQKSGDHY TKKNWSTARQ
NWFILGFYIF LPFFIIFIIV VMKRNEMRKS WNREEAEYEG
//
