ID A0A2I0MQ59_COLLI Unreviewed; 693 AA.
AC A0A2I0MQ59;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=ADAM metallopeptidase domain 20 {ECO:0000313|EMBL:PKK31787.1};
DE Flags: Fragment;
GN Name=ADAM20 {ECO:0000313|EMBL:PKK31787.1};
GN ORFNames=A306_00002008 {ECO:0000313|EMBL:PKK31787.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK31787.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK31787.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK31787.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK31787.1}.
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DR EMBL; AKCR02000005; PKK31787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0MQ59; -.
DR InParanoid; A0A2I0MQ59; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
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:SF239; A DISINTEGRIN AND METALLOPEPTIDASE DOMAIN 26B-RELATED; 1.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 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:UP000053872};
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 655..675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 170..353
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 372..458
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 597..630
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 306
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 322..327
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 430..450
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 620..629
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PKK31787.1"
SQ SEQUENCE 693 AA; 78520 MW; 1A9CEFC3F647238A CRC64;
VAAKWVAVPR QLSPRADTDP QAVSYWLEVE GRPRLLRLRP RRGLISHPFT LITYGKDGTR
WEEHPFVQDN CFYQGKVQGS PGSLVALSTC GRGLRGVLWV EDGTYEMEPI PDDPAFRHIL
YRMERANDSV GPTCGLTSEE MKHQEVLLPW FKAFRAEEEE TVKDWWMHVR YVKMVVVVDN
VRFVKSGRNE SEVLRQVIEI INIADSLYNQ LSVHLFLLAL EIWTEKNPII LTNDIGKALD
SFNKWRKSEL SPRMRHDSAH LFAYQRFGRR LGLAFLGSVC DNQWSSAVCS FTNRKLSSFI
VTFSHELGHI LGMRHDTEHC KCRRKKCIMH EHDVDTDAFS DCSYKDYFDL LSHGLGCIRR
PPVPGTFYNL KREYCGNKVV ENREQCDCGS PSSCRKDPCC HPNCTLTAGS VCAFGKCCKR
CQFLPAGTLC RGSTGYCDLP EYCNGTSPQC PLDMYMQDGT PCKGDAYCYQ GKCPSHSRQC
KHLFGKRAGV APLDCFKAVN TRGDRFGNCG IRDNTHFTKC SIENILCGRI QCENINKLPV
LQSHVTLLQT PVGDKKCWGF DYHPGIPIDD MGAVEEGTPC GSEKLCINRT CTSLSVLNYD
CNLTMCHNRG VCNSRKNCHC SYGWAPPYCE WEGLGGSIDS GPPPPRKLFE AAKTGFMVFS
LVLLFILGVT LATRYRQEIM GCVRKKKAWF HRR
//
