ID A0A340YIN3_LIPVE Unreviewed; 757 AA.
AC A0A340YIN3;
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=LOW QUALITY PROTEIN: ADAM metallopeptidase domain 30 {ECO:0000313|RefSeq:XP_007472402.1};
GN Name=ADAM30 {ECO:0000313|RefSeq:XP_007472402.1};
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_007472402.1};
RN [1] {ECO:0000313|RefSeq:XP_007472402.1}
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_007472402.1; XM_007472340.1.
DR STRING; 118797.A0A340YIN3; -.
DR GeneID; 103085246; -.
DR KEGG; lve:103085246; -.
DR CTD; 11085; -.
DR InParanoid; A0A340YIN3; -.
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 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:SF148; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 30; 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; 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 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 TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 205..395
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 401..486
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 630..663
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 458..478
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 653..662
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 757 AA; 84566 MW; 0FB723F30E197317 CRC64;
MRSVRTLLSP GRXLPLLVLP VLLVDSPGKD LIFHPKWGFD SYEITIPKKL SFRGGEQGVA
KHVSYLLQVK GKNHVLHLWP KRFLLPRNLQ VFSFTEQGRL LEDHPYIPSD CSYMGLVEGN
QDSKATLSTC MGGLRGILKV DANHYQIEPL RASTNFERVI YLLKKEEEFP NQICGLTDDE
TVKQLAEHEH RARIHDFSEA YMHQKYLELA LVFDNSRYLY LNSNLTQVIN DAILLTAIAD
SYFQDVRMRI QLLAMEVWTD RDKIALNAPV ILQVLGQFVQ YRSHDPSHRI PADWAHLYLK
RQFSDALSQH WGSVCSALPS GSTSSILDKN ILGPTTWTTH ALGHSVGMIH DYKYCQCKGR
HSCIMGTGRT GFSNCSYAEF YSHVSSGLNC LTDIPGLGYV VKRCGNKIVE ENEECDCGSR
EDCKEDQCCQ SDCKFKGANC STGLCCHNCQ FRPSGYTCXG EENECDLAEY CSGTSAFCPS
DAYKQDGTTC KYRARCVRKG CQSRTMQCQN IFGADAMGAP LQCYDAVNVI GDQYGNCGIL
GVPQYEKCPR EKALCGRLQC INVETIPDMQ DHTILISTHL HEENLMCWGI GYHLAMVPMG
LPDLGVISDG TSCGKERICF NGNCVNSSVL NFDCLPEKCN GXGVCSSSKN CHCMYGWVPP
FCEEVEYGGS IDSGPPGPLK REVPASLQVV SITLMRLIFL IISVIVVLFR KIIGSXYKSK
EKEMPPINTG VEQFKAKMIK KPKKQSGNPQ SLYYTGS
//
