ID A0A3P9PK86_POERE Unreviewed; 770 AA.
AC A0A3P9PK86;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Zinc metalloproteinase-disintegrin-like brevilysin H2a {ECO:0000313|Ensembl:ENSPREP00000022128.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000022128.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000022128.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000022128.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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_008415521.1; XM_008417299.2.
DR AlphaFoldDB; A0A3P9PK86; -.
DR Ensembl; ENSPRET00000022359.1; ENSPREP00000022128.1; ENSPREG00000014950.1.
DR GeneID; 103469550; -.
DR KEGG; pret:103469550; -.
DR CTD; 10863; -.
DR GeneTree; ENSGT00940000156716; -.
DR OMA; CKANDAM; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000014950; Expressed in caudal fin and 1 other cell type or tissue.
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:0048856; P:anatomical structure development; IEA:UniProt.
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:SF32; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 28; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Reference proteome {ECO:0000313|Proteomes:UP000242638};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..770
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017984126"
FT TRANSMEM 667..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 197..393
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 401..487
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 620..652
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 169..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..749
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 333
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 308..388
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 348..372
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 350..355
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 459..479
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 624..634
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 642..651
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 770 AA; 84239 MW; 608A3770E98F48B1 CRC64;
MTRTLLLLIV FLNVSLRSSE SHNPTFEVGT DYEVVRPVRL HAVRKRSTEY LRPETIKYAM
TVGGRDIQLQ LEKNNELLTR DYSETYYQED GTRVTTSPHD VDHCYYHGKI VNDSESSASI
STCEGLRGYF RTSEKRYLIE PLIGGDEGDH AVTTINDRNL TPAVCGVTNT SWEDGMEPPT
SQSRSRSGGL PVLLQQKYIE LVLVADNRAY AKMNKDLTKL RQRIFEIVNF VNMAYKPLKT
FIGLVGLEVW SNADLISVTN PANANLDAFK TWRNSELVKR IKHDNAHLIS GIDFEGATVG
LAYIGTLCTD HSVGVIQDHN ARAIAVGATL AHEMGHNLGM SHDDSSGCSC SGDSCIMAAA
LSYNIPRTFS SCSVANYERY LTTRNPSCMF DKPDVTSIVA PGVCGNGFLE KGEQCDCGSV
EECTNPCCNA TSCTLSAGSQ CAEGECCENC KIQPRSIECR RKQDDCDLAE YCDGKSATCP
EDVFAVNGLP CDKGLGYCYN GQCPQRAAQC KKVYGNAADE APSTCYNYNT KGNNYGYCRR
LSNTDFIPCQ KQDVLCGKLF CQGGNANPIY GQMVTISVVC KATFFTDYTK DYGQVDEGIM
CGEGKVCSQN QCMDLESAYR NTNCSAKCPG NAVCNHRSEC QCLPGWLPPN CGAKDEAFSS
LSTGANIAIS LAVILVILGL FFGVVGFMCR KKRSPTLPVS QAQRKAPAVS SSAPYVNQEY
TISQPRLLRQ EPKPKGAPPP PPPAGNRPEP PSQNYTAARQ ALRPVHPPKV
//
