ID A0A286ZN86_PIG Unreviewed; 789 AA.
AC A0A286ZN86;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 3.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=ADAM metallopeptidase domain 18 {ECO:0000313|Ensembl:ENSSSCP00000032923.3};
GN Name=ADAM18 {ECO:0000313|Ensembl:ENSSSCP00000032923.3,
GN ECO:0000313|VGNC:VGNC:111203};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000032923.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000032923.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000032923.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000032923.3}
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; A0A286ZN86; -.
DR Ensembl; ENSSSCT00000044825.3; ENSSSCP00000032923.3; ENSSSCG00000007008.5.
DR VGNC; VGNC:111203; ADAM18.
DR GeneTree; ENSGT00940000162281; -.
DR Proteomes; UP000008227; Chromosome 17.
DR Bgee; ENSSSCG00000007008; Expressed in testis and 1 other cell type or tissue.
DR ExpressionAtlas; A0A286ZN86; baseline.
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 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; 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:SF158; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 18; 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; PS00427; DISINTEGRIN_1; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 273..433
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 442..531
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 670..704
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 389..394
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 694..703
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 789 AA; 87961 MW; 81ACACCC7C95AECF CRC64;
MAVDWKLQQP SRGTRGSMRR MSSPSESQGG AAPGRRQAQS SAPCPGQHWT PESPAREPRK
AQRSLALAVH PAPRPAMLLL LALLAAFGGL QARLDSEGIF LQVTVPQKIR SRESEDSETQ
VTYIITIDRK PYTLHLRKHP FLAQNFLVYT RNKNGSFHSE PSYFMMHCHY QGYVADFPNS
AVTLSICSGL RGFLQFENIS YGIEPLDSSA SFEHIIYQVK NDSPDIPVLA ENDSNVLQKD
EPYKIHLSSQ ETTLSELLPQ YLEMHIIVEK ALMCSQFKLT VILSSLELWP DENQISTNGD
MDDLLQRFLT WKQDSLILRP HDITFLLIYR KQPKYVGATS SGTICNKSGD ANIIMYSEAI
TLEGFSVLMA QLLGLKIGLT YDDVNKCSCA RATCIMNREA MFSSGIKMFS NCSMHAYRYF
ISTFEGRCLQ NFPKLKPFHQ NQSVCGNGIL EPHEECDCGS ERECQFKKCC DYNTCKLKGS
VKCGSGSCCT SECELSEAGT PCRKSVDQEC DFTEYCSGTS SDCVPDTHAM NGELCRLGTA
YCYNGRCQTT DNQCAEIFGK GAQGAPFACF KEVNSLPNRP GDCGFKNSQP LPCEQSDVLC
GKLACIWPNK NSYKNDVQSA VYSYTQGHEC ITTGSAMRSD GRDYAYVADG TVCGAQMYCI
NKTCKKVPLM GYNCNATTKC RGNGICNNLG NCHCLPGYRP PDCELQIGSP GGSIDDGNDH
KSAIVFIKKA YNTHQGNWLI LSFYISLPFF IIFIFMIMKR NEMRRSCNKE NAEYEGHSVM
VPESYNVDY
//
