ID A0A340X9D4_LIPVE Unreviewed; 865 AA.
AC A0A340X9D4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 15 isoform X2 {ECO:0000313|RefSeq:XP_007458031.1};
GN Name=ADAM15 {ECO:0000313|RefSeq:XP_007458031.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007458031.1};
RN [1] {ECO:0000313|RefSeq:XP_007458031.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_007458031.1; XM_007457969.1.
DR AlphaFoldDB; A0A340X9D4; -.
DR GeneID; 103072406; -.
DR CTD; 8751; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000265300; 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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
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:SF130; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 15; 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; 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:UP000265300};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..865
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016302562"
FT TRANSMEM 700..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..415
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 422..509
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 656..688
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 20..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..827
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..865
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 481..501
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 660..670
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 678..687
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 865 AA; 92618 MW; A0BCD63A5D019AA6 CRC64;
MRLALLWALG LLGAGSPLPS RPLPDIGGTE EKQARPERAL NGSSEPQILQ DNLMLSLAEV
LQTSLPEALR IKLELDGESH ILELLQNREL VSGRPSLVWY QPDGTRVVSE GHTLENCCYH
GKVQGHADSW VSVCTCSGLR GLVILSPERS YSLELGPGDL QGPPVISRLQ DLLLPGHTCA
LSWPASVPTQ APPEHPLGQR HLLRWRRDVV TETKIVELVI VADHSEVQRY RDFQSLLNRT
LEVALLLDTF FRPLNVRVAL VGLEAWTQRD LIEISQHPGL TLDSFLRWRR TDLLPRLPHD
SAQLVTATSF SGPMVGMAIQ NSICSPEFSG GVNMDHSTSI LGVASSIAHE LGHSLGLGHD
SPGNSCPCPG PAPAKSCIME ASTDFLPGLN FSNCSRQALE KALLGGMGSC LFERLSGLPS
MASVCGNMLV EPGEQCDCGF PDDCTDPCCD YFTCQLRPGA QCASDGLCCQ NCQLRPAGWQ
CRSTRGDCDL PEFCPGDSSQ CPPDVSLGDG EPCAGGQAVC MQGRCTSYAQ QCQALWGPGA
QPAAPLCLLT ANTRGDAFGS CGRSPDGSYV SCAPRDAICG QLQCQGGRAQ PLLGSARDLH
WEMLEANGTQ LKLNCSWVHL DLGNDLAQPL MTLPGTACGP GLVCINHQCQ PVEILGTQEC
RSKCHGHGVC NSNRHCHCEE GWAPPDCTTH IRATSSLTTG LPLSLLLLLV LVLLGASYWH
RARLRQRLCQ LKGPSCQYRA AQSGPPERPG PPQRALLMPG AKASALGFPA PPSRPLPPDP
VPKRLQAELA DRPNPPTRPL PADPVVRYPK SQGPTKPPPP RKPLPTDPQG QHPSADLPGP
GAGIPPPVVP SRPAPPPPAV SSLYL
//
