ID A0A3Q7TXC1_VULVU Unreviewed; 826 AA.
AC A0A3Q7TXC1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 22 isoform X6 {ECO:0000313|RefSeq:XP_025874428.1};
GN Name=ADAM22 {ECO:0000313|RefSeq:XP_025874428.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025874428.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025874428.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025874428.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025874428.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_025874428.1; XM_026018643.1.
DR AlphaFoldDB; A0A3Q7TXC1; -.
DR Proteomes; UP000286640; 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; 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; 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; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 633..656
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..334
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 340..427
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 676..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 399..419
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 826 AA; 91919 MW; 946FF94B6ED86A7E CRC64;
MLNHDLLSSE YIERHVEHGG KTVEVKGGEH CYYQGHIRGN PDSFVALSTC HGLHGMFYDG
NHTYLIEPEE NDTSQEDFHF HSVYKSRLFE FPLDDLPSEF QQVHITPPKF TLKPRPKRSK
RQLRRHPRNV EEETKYIELM IVNDHLMFKK HRLSVVHTNT YAKSVVNMAD LIYKDQLKTR
IVLVAMETWA ADNKFAISEN PLITLREFMK YRRDFIKEKS DAVHLFSGSQ FESSRSGAAY
IGGICSLLKG GGVNEFGKTD LMAVTLAQSL AHNIGIISDK RKLASGECKC EDTWSGCIMG
DTGYYLPKKF TQCNIEEYHD FLNSGGGACL FNKPSKLLDP PECGNGFIET GEECDCGTPA
ECVLEGAECC KKCTLTQESQ CSDGLCCKKC KFQPMGTVCR EAVNDCDIRE TCSGNSSQCA
PNIHKMDGYS CDGIQGICFG GRCKTRDRQC KYIWGQKVMA SDKYCYEKLN IEGTEKGNCG
KDKDTWIQCN KRDVLCGYLL CTNIGNIPRL GELDGEITST LVVQQGRTLN CSGGHVKLEE
DVDLGYVEDG TPCGPQMMCL EHRCLPVASF NFSTCLSNKE GTVCSGNGIC SNELKCVCNR
HWIGADCSTY FPHNDDAKTG ITLSGNGVAG TNIIIGIIAG TILVLALILG ITAWGYKSNG
LSHSWSERIP DTKHISDICE NGRPRSNSWQ GNLGGNRKKI RGKRFRPRSN STEREPQAPE
PGHSLAQTVP SQGISPGGSD SPQTGSLDHR YLNPWFKRDY NVAKWVEDVN KNTEGPYFRT
LSPAKSPSSS TGSIASSRKY PYPMPPLPDE EKKVNRQSAR LWETSI
//
