ID   A0A1I7UPF9_9PELO        Unreviewed;       767 AA.
AC   A0A1I7UPF9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Disintegrin and metalloproteinase domain-containing protein 22 {ECO:0000313|WBParaSite:Csp11.Scaffold630.g18025.t1};
OS   Caenorhabditis tropicalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold630.g18025.t1};
RN   [1] {ECO:0000313|WBParaSite:Csp11.Scaffold630.g18025.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR   AlphaFoldDB; A0A1I7UPF9; -.
DR   STRING; 1561998.A0A1I7UPF9; -.
DR   WBParaSite; Csp11.Scaffold630.g18025.t1; Csp11.Scaffold630.g18025.t1; Csp11.Scaffold630.g18025.
DR   eggNOG; KOG3607; Eukaryota.
DR   Proteomes; UP000095282; Unplaced.
DR   GO; GO:0016020; C:membrane; 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   Gene3D; 2.10.25.10; Laminin; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
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; IPR034027; Reprolysin_adamalysin.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF248; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN UNC-71; 1.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF01421; Reprolysin; 1.
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; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00068}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        488..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..180
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          186..273
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   REGION          521..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          711..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..546
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..750
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        245..265
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   767 AA;  83781 MW;  364CDEE98BD0947D CRC64;
     MDAISYMLES LNVADSMLSR DLNIRLSAVY VELWSDVQRI DLWEDIERTL SGVVDYTAGH
     IYHIQKDATI LFTAGSFANQ EASNAAIRSI CTARSAVIVR SIEQFATHWN GELVAQSIGH
     LLGLEHDTTA CSCEPSPECL MRQQPGRLGA PFSWQFSKCS VARMHGIWQD GNIQCLLNKP
     FQVSELRECG NGIVDGAEEC DCGTRENCND PCCDPLTCTL RPHAQCAAHH KCCHRCELRK
     AGETCRASQS PCDVAESCDG KSGDCPPDGH LIDGTVCGTD GQCWRGNCSD SHLQCQKLWG
     RDARLADPVC FDQNTKGAEY ANCGVQADGS YHPCRLEDTK CGTLHCHSGS ITPLDQTLKA
     FTFHFSQNSQ QIQCKSIAGG IATVPDGTNC GSGRVCVASS CVEMSSVTSP TTCPTNNLAL
     LCSGHGHCTT TAKCVCFNGW AGTACDIRSN TSTYQGQMGF SDSSGSKDRK TIMIPHLNIG
     TTLETATLFA ILLGFGVFLL LCLVCLMLCY RRRSVVEIPK PSDEKMEESP DRQIKFGNMP
     SYREEKRKRK SNKRIYGALN RITEADERDS TSLRSRDSAG SQQLLDRNGQ PVMIRDPYAS
     EHHIYAESSS TSAPQRQFRG INSDGSYPLR SFGSWRSSGP ISPASSSGHL TDVSSSTTPL
     RLNKIGKLLK TMQQSDDETS PFSDHPLLGR PGFQPTYSNP EEELSAVEAD HDVGSNTESS
     RGCEDGPIDG WDPPSIVNGS SSNFQFRQSP SLFSDPFKLE MTNSMHN
//