ID A0A452SJF3_URSAM Unreviewed; 747 AA.
AC A0A452SJF3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=ADAM metallopeptidase domain 30 {ECO:0000313|Ensembl:ENSUAMP00000032704.1};
GN Name=ADAM30 {ECO:0000313|Ensembl:ENSUAMP00000032704.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000032704.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000032704.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A452SJF3; -.
DR STRING; 9643.ENSUAMP00000032704; -.
DR Ensembl; ENSUAMT00000036439.1; ENSUAMP00000032704.1; ENSUAMG00000024960.1.
DR GeneTree; ENSGT00940000162954; -.
DR OMA; ICGRLQC; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:1990913; C:sperm head plasma membrane; IEA:Ensembl.
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:UP000291022};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..747
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019467163"
FT TRANSMEM 683..705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 199..390
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 396..482
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 626..659
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 339
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 DISULFID 454..474
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 649..658
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 747 AA; 84371 MW; CF344A7BFD11DCCB CRC64;
MRSVRTLIPM LVLVALLLDA LGEDLLFHPE WGFESYEIII PKKLSFRGGQ QGAVQQVSYL
LQVKDKKYVL HLWPKRFLLP RNLKVFSFTE QEKLLEDHPY IPRDCNYIGL VEGTQDSEAT
LSTCTGSLRG ILKIDEERYQ IEPLKASSSF EHVMYLLKKE DKFQNQTCGL TNDELEKQMA
RSENMARLRD YPGSYKHQKY MELALVFDHS RFLFSDSNLT RLIQDAILLT GIMDTFFRDV
NMRLHLQGVE IWTHGDKLNV QQMTSQEILS TFLKYRTTTL SARISADWAH LYITSAFIHS
LGWAYIGGAC MEKYSGSVSS YTNLNILEAS RMSAHELGHG VGMRHDTVYC QCRGKQTCIM
GTGSSGFSNC SYIEYFNHVY SGAECLNNIP GLGYVVERCG NKIVEGDEEC DCGSREDCKK
DRCCQPDCKL TQGANCSTGL CCHNCRFRPL GYMCRKEENE CDLAEYCNGI SSFCPDDAYK
HDGTICKSNS LCFKKRCHSR YAQCQNIFGP DAREAPDQCY HAVNLMGDQY GNCGIVGVRT
YKACTRENAV CGRLQCINVK SIPELPDHTT IISTHLRAEN LLCWGLGYHK SMIPMGIPDI
GVISDGTPCG FDRLCVNRTC VHISVLNLEC LPKKCNHRGV CNNNQNCHCV YGWAPPFCEE
VGYGGSIDSG PTRRLKEEVP APVQVVSIML MRLIFLILSV IAVFFRRLIE QRSTVLEEQS
RSSKENMNSD YNVASCKVLS SSVLIMS
//
