ID A0A182KB67_9DIPT Unreviewed; 1042 AA.
AC A0A182KB67;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 12 {ECO:0008006|Google:ProtNLM};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR008004-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR008004-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR008004-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 AlphaFoldDB; A0A182KB67; -.
DR STRING; 43041.A0A182KB67; -.
DR EnsemblMetazoa; ACHR008004-RA; ACHR008004-PA; ACHR008004.
DR VEuPathDB; VectorBase:ACHR008004; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000075881; 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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; 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:SF250; ADAM METALLOPROTEASE; 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 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; 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:ARBA00023049};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00023049};
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 725..746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..415
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 421..509
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 666..698
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 39..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..816
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..995
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 481..501
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 670..680
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 688..697
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1042 AA; 114560 MW; F05775526F9697D7 CRC64;
MTLSAAALLY RLGLSGEQFE LHDRIFPTYH CPRTKRALRS SSLDDDDDGN GDGFGRRDNT
FSQSTNAKRR PHRERLTIQY GMQDETMTLD LTLNENIIPE DYTFVYQSPE GRDIVERLDR
QAVELCHYEG TVRERPGSRV AISTCNGSID GVIYERNETY LIEYHNNTHL LYRRRFRRDV
QNSELLTDTD TRGSAASSKT AFTTGYREDA DSLFVELVLV VDRTLFLKFS SNVQRVHQHC
LSVVNVLNEL YRPLNIYILL VGVVLWNTRD NIVISTDSKQ TLSSFLAYRK EQLLRQIPND
NAHLLTAVRF PDGVIGKAEL GSMCSTAGSG GIAVVENFVV PPLAATIAHE LGHNFNIDHD
TEECGGSRCP GPGTCIMEAK LRDSADIPNR WSDCSVDDLR ESLQRGLGAC LKNKPARLLV
RAVCGNGLLE PGEQCDCGRR DQCDNGCCDA STCQLRANAT CATGSCCDLD TCQPKQAGSV
CRQARGECDL PEYCDGVGEL CPKDVFLRDT SPCRKGEAYC YRGECNTRDR QCRRLWGSTA
RSGLEVCYEA NVNGTVFGNC GFELSSEQYQ PCAVHDMHCG LLHCTHQSEK LEYGVEAYAK
RTATKFQHYG PRGTVRTTIC NAVIVDLGLD VVNPGLVPDG TKCGAGRMCF QQQCVAISRL
QEEQDIGDEC PDNCNGNGAC NSAGHCHCNP GFAPPFCDVP GEGGSIDSGP VGVPASSMHD
LLLKLLIPLL SFGGILMIVS FTLLIVQRTL VMAQLRVVLK RFRERKYGHI VVPPASPTGL
VPPPTTASKL EGQRNAANEV RRPTVPPPPP LPEPKQPQCF INVNISKDGK VTIENKLIDS
PFLHKASVVD THEAFRMRLL QERSYSVESA TSSEHPLVTA ETHKPSTPNT PEPEMEVKSF
GTVLHQLKQT DRMHTFHNRR SKSDEKPAPA RQLPKLPRQY TISDFDSIER LPDVDEEEPQ
PVSKLAKPST PKPIAIPRPL PRVAPGTPGP RLLPSTPPTG NGSRTGKAKL TAGPTGKVTA
GHGSNVAALK AKLNLAEIGA RR
//
