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Database: UniProt
Entry: A0A087XW21_POEFO
LinkDB: A0A087XW21_POEFO
Original site: A0A087XW21_POEFO 
ID   A0A087XW21_POEFO        Unreviewed;       820 AA.
AC   A0A087XW21;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9-like {ECO:0000313|Ensembl:ENSPFOP00000009974.1};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000009974.1, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000009974.1}
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   EMBL; AYCK01007305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007558430.1; XM_007558368.2.
DR   AlphaFoldDB; A0A087XW21; -.
DR   STRING; 48698.ENSPFOP00000009974; -.
DR   Ensembl; ENSPFOT00000009989.1; ENSPFOP00000009974.1; ENSPFOG00000009790.1.
DR   GeneID; 103142341; -.
DR   KEGG; pfor:103142341; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000166115; -.
DR   OMA; NGSTAYC; -.
DR   OrthoDB; 5406290at2759; -.
DR   Proteomes; UP000028760; 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: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:SF244; ZGC:174164 PROTEIN; 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:UP000028760};
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..820
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001833608"
FT   TRANSMEM        698..720
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          210..406
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          414..500
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   DOMAIN          641..675
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          735..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..759
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        349
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         348
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         352
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         358
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   DISULFID        365..370
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   DISULFID        472..492
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT   DISULFID        665..674
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   820 AA;  89100 MW;  251B2B1AA16979F0 CRC64;
     MIIRKPIFIA FILHLCISEI ENKEDFSGFT SKLPKYSIVK PQVINNRWTR SLNRTSQTEE
     AYGDKVSYTL MINNKEHILH LEKNRGFLHP NFVQYSREAS GNYNTSYPRQ HVNCYYHGSV
     EGYEGSVVAL STCSGLRGVI LLENETFGLE PVPASTTNEH ALYLLKDSHS EPVTCGVVGE
     ATSTPNYEPF EPAQSMTSLL RRKRALPQTS YVELVLVVDN LRYNYKQQNE TAVREEMVQM
     ANLLDGYYKP LNIRVVLVGL EIFKQSNPFS VDGSAGQVLG EFVKWRKSTL LPKIRHDIGQ
     LIVGRSGSYG GGVLGMAYVG TVCSVASSGG INVYSNDNLN FVSTVVAHEM GHNLGMNHDS
     SGCTCNGKSC IMSAGAGGAV QFSKCSEQDF ESLIVRGGGV CLRNQPSASD VIGTAECGNG
     RLDKGEECDC GTKEECKNEC CDAATCKLTR GSSCAHGYCC EKCQFKVAGT QCRKSLDVCD
     LPEYCNGKSG FCPQDFYIMD GLPCKNDAAY CYEGRCQTYD YQCLQLFGSG AKKADDICFE
     YENVKGNVFG NCGITSSGGY IKCTVANAKC GKVQCTNVDL NNHPAGAQIS IEIVQGSKCI
     NADFNLGTDV LDPAYVNPGS PCDNGKTCVD FKCVNASVLD PKLGCDAQTT CSGRGVCNDQ
     GHCHCDNGWA PPNCNKAGRG GSIDSGPAMI DYSLRNGLLI FFLLIVPLLV AAILVLLYVF
     KRDSLDICLK RRKKTRSTGN RNANAPTNGN VQTDVTIQPP RQVPPERPPA PTVTSVPISG
     FRYGEVDYWS QEANEAPSRP PAPVQGPGVP RPIPVKDISS
//
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