ID A0A087YEJ0_POEFO Unreviewed; 951 AA.
AC A0A087YEJ0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSPFOP00000016443.2};
GN Name=ADAM22 {ECO:0000313|Ensembl:ENSPFOP00000016443.2};
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:ENSPFOP00000016443.2, 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:ENSPFOP00000016443.2}
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; AYCK01006469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007556213.1; XM_007556151.2.
DR AlphaFoldDB; A0A087YEJ0; -.
DR STRING; 48698.ENSPFOP00000016443; -.
DR MEROPS; M12.978; -.
DR Ensembl; ENSPFOT00000016465.2; ENSPFOP00000016443.2; ENSPFOG00000016101.2.
DR GeneID; 103140831; -.
DR KEGG; pfor:103140831; -.
DR CTD; 53616; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000156889; -.
DR OMA; TAWGYNM; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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 Gene3D; 2.10.25.10; Laminin; 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; IPR013111; EGF_extracell.
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:SF14; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 22; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF07974; EGF_2; 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; PS00022; EGF_1; 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};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..951
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001834387"
FT TRANSMEM 739..762
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 242..441
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 447..534
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 678..715
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 872..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 506..526
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 705..714
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 951 AA; 105006 MW; 9973BF8F05E70396 CRC64;
MMLRMPWWIS LLCVCGLMHV GHQSSLDASN GDALSSLEAL RDAGRFVGKE NTVPLRLVYS
SQNHSQITHD ELSTRVKASP DSTQMEHVIQ ATFQVDAFGK TFILDVELNH DLLSSGYQER
HLSENGKIVV TKGGEHCYYQ GRVRDAPRSF AALSTCHGLH GMFFDGNHTY MIEPGGQASN
SGDLQVHLIY KSAGQEELSD FFGGDLPEPP FPSPPFPESK VVHWRKKRQA PRLSRSVEDE
TKYIELMVIN DHVMYKKHRL SVGHTNNNAK TVVNIADMIF REQLNTQIVL VAMETWSVDN
KFNIDDDPMV TLKEFMKYRK DFIKEKCDSV HLFSGNQFHS NRGAVSYTGG VCSLTKGGGV
NEYGKTNEMA ITLAQSLGQN IGIFSDKKRI LNGECKCDDR WAGCIMDDVG FYLPKKFTDC
NVEEYHNFLN SGGGACLFNK PRKLLDPPEC GNGILEAGEE CDCGSTEECA KEGENCCKNC
TLTKGSNCSN GLCCRNCQME VVGVLCRDAV NDCDIPEKCT GNSSQCPPNV HKMDGYTCEK
DQGRCFNGRC KTKDRQCKYI WGEKATAADK FCYEKLNIEG TEKGNCGKEK DTWIQCNKQD
VHCGYLLCSN ISPAPRLGDL QGGLTSFSVA QHGAPLDCSG AHVLIDGDTD LGYVEDGTAC
GTDSICLDHK CLPIEQFNFS TCPGTTDKTI CSGHGVCSNE LRCVCELGWT GDDCYSRSPF
SNLVVGPTAP VSGITSTNII IGAITGSILF LALILAVTAW CYKSYKKRRY AESEVHRRFC
RQIPPGDYVT KPGDADSFYS DMPPGVSTNS GCSSKKRSAC LSHLQICTLS FTPSFPSISQ
NFSVFGFRSN GLSHSWSERI PDAKHITDIC ENGRPRSNSW QGNLSGNRKK LKGKKFRARS
NSTETLSPAK SPTSSTGSIA SSRRYPYPMP PLPDDQRKAN RQNARLWETS I
//
