ID A0A3Q1GX71_ANATE Unreviewed; 853 AA.
AC A0A3Q1GX71;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=ADAM metallopeptidase domain 22 {ECO:0000313|Ensembl:ENSATEP00000000467.1};
GN Name=ADAM22 {ECO:0000313|Ensembl:ENSATEP00000000467.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000000467.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000000467.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; A0A3Q1GX71; -.
DR STRING; 64144.ENSATEP00000000467; -.
DR Ensembl; ENSATET00000000480.2; ENSATEP00000000467.1; ENSATEG00000000240.2.
DR GeneTree; ENSGT00940000156889; -.
DR OMA; TAWGYNM; -.
DR Proteomes; UP000265040; Unplaced.
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; 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.
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:UP000265040};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..853
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018688340"
FT TRANSMEM 672..695
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 175..374
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 380..467
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 611..648
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 738..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 439..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 638..647
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 853 AA; 94381 MW; 4A87105A2081D254 CRC64;
MMHPRWWISL LCVYGLMHVG HQSNALSSFK ALRDAARFVG KEDTVPLRLL YSRHSHRQVA
QDELSTRVEA SSGSTQVNHV AQASFQVDAF GRQFILDVEL NQAFCFLLWI LIFGGEHCYY
QGKVRDIPHS FVALSSCHGL HGMFFDGNHT YMIEPGGQGS SNAPHVSRSV EDETKYIELM
VINDHLMYKK HRLSVGHTNN YAKSVVNMAD MIFKEQLNTR IVLVSMETWS ADNKFNIDDD
PMMTLKEFMK YRKDFIKEKC DSVHLFSGNR FHSSWGGASY IGGVCSLTKG GGVNEYGKTD
EMAITLAQSL GQNIGIFSDK KRILNGECKC DDRWSGCIMD DIGFYLPKRF SDCSVEEYHN
FLNSGGGACL FNKPMKLLDP PVCGNGFVEP GEECDCGGPA ECAREGENCC NKCTLTQGSK
CSNGLCCNNC QMEFMGVVCR DAVNDCDIPE NCTGNSSQCP PNVHKMDGYT CEKDQGRCFN
GRCKTKDRQC KYIWGEKATA ADKFCYEKLN IEGTEKGNCG KDKDTWIQCN KQDVHCGYLL
CSNISPAPRL GELQGGLTSF SVAIHSASLD CSGAHVLIDG DTDLGYVEDG TACGTDRICF
NHKCLPIQQF NFSTCPGTTD KTICSGHGVC SNELKCVCYL GWAGEDCNSM SPLSSLVVGP
TTLVSGITST NIIIGAIVGS ILFLALILAV TAWCYKSYKQ RRYVESEVHR RFCRQMPPGD
YVTKPGDADS FYSDMPPGVS TNSGCSSKKR SNGLSHSWSE RIPDAKHISD ICENGRPRSN
SWQGNLSGNR KKLKGKKFRA RSNSTETLSP AKSPTSSTGS IASSRRYPYP MPPLPDDQRK
ANRQSARLWE TSI
//
