ID A0A1S3A3I1_ERIEU Unreviewed; 729 AA.
AC A0A1S3A3I1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 30 {ECO:0000313|RefSeq:XP_007528762.1};
GN Name=ADAM30 {ECO:0000313|RefSeq:XP_007528762.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007528762.1};
RN [1] {ECO:0000313|RefSeq:XP_007528762.1}
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_007528762.1; XM_007528700.1.
DR AlphaFoldDB; A0A1S3A3I1; -.
DR STRING; 9365.ENSEEUP00000009937; -.
DR GeneID; 103118479; -.
DR CTD; 11085; -.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; A0A1S3A3I1; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000079721; 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: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; 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:UP000079721};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..729
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010193292"
FT TRANSMEM 694..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 207..396
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 402..488
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 635..668
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 460..480
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 658..667
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 729 AA; 82275 MW; BB2479FEB0763536 CRC64;
MRPAGRTLPS QSLWLPALLL QMLLGDAQQH DVIFQPDSGF ASYEITIPKK LSYRVGEQGL
VQHLSYLLHI QGKKHVLHLR PKRLLLPRHL RVFSFTHQGE LVEDHPYIPR DCNFMGSVEG
SKESQATFST CMGGLRGVLK VDAQDFQIEP LRTSSTFEHI VYLLKEEEPF LSQNCDLVDD
EEIKKLMSPK DYMARIRSIK ASYKHPKYME LVLVFDHDRF LYSKSNITKV TNDAILISAI
LDTYYQDVFT RIHLTAVEVW TDRDKARIHH RTISRALGQF SVYRTSNLLV RIPHDWTHLF
AIKDYVKGLA GSAGGMCWLA SVSLAILKDE NILGPATWTA HEIGHGLGMD HDGLECLCKG
RRNCIMGSGR TGFSNCSYEE FLYFTNSEAA CLDNIPGQGL VIKRCGNKIV EENEQCDCGT
KEECEKDQCC QLDCKLKEGA NCSTGLCCHN CQFRPSRFVC RRPENECDLP EYCLGNSSDC
PEDTYKVDGT PCKYEARCFK KGCRSRYMQC QSIFGSGVRE APYQCYHVVN SVGDQFGNCR
MEERVDLVYK KCSRENSLCG RIQCVNVKSL PDSPDHATIM STHLKEENLM CWTIGYHLNM
RPLGIADAGV ISDGTSCGKD RVCFNRSCVP VQSVLNYDCL PKKCNNRGVC NNKKNCHCLY
GWAPPFCEEE GFGGSIDSGP AGPLEKEVSA NIQIVSIMFL RLALFIISLV ILAFWNVIDS
YIIPKPETQ
//
