ID F1SE43_PIG Unreviewed; 813 AA.
AC F1SE43;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 5.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=ADAM metallopeptidase domain 18 {ECO:0000313|Ensembl:ENSSSCP00000007469.5};
GN Name=ADAM18 {ECO:0000313|Ensembl:ENSSSCP00000007469.5,
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:ENSSSCP00000007469.5, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000007469.5, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000007469.5,
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:ENSSSCP00000007469.5}
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; F1SE43; -.
DR STRING; 9823.ENSSSCP00000007469; -.
DR PaxDb; 9823-ENSSSCP00000007469; -.
DR Ensembl; ENSSSCT00000007676.5; ENSSSCP00000007469.5; ENSSSCG00000007008.5.
DR VGNC; VGNC:111203; ADAM18.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000162281; -.
DR HOGENOM; CLU_012714_4_3_1; -.
DR InParanoid; F1SE43; -.
DR TreeFam; TF314733; -.
DR Proteomes; UP000008227; Chromosome 17.
DR Bgee; ENSSSCG00000007008; Expressed in testis and 1 other cell type or tissue.
DR ExpressionAtlas; F1SE43; baseline.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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 762..782
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 260..457
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 466..555
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 694..728
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 413..418
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 718..727
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 813 AA; 90754 MW; 60D9C3A12643A195 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 ALYDYMGSEM MVVMQKIFQI IGLVNTMCSQ
FKLTVILSSL ELWPDENQIS TNGDMDDLLQ RFLTWKQDSL ILRPHDITFL LIYRKQPKYV
GATSSGTICN KSGDANIIMY SEAITLEGFS VLMAQLLGLK IGLTYDDVNK CSCARATCIM
NREAMFSSGI KMFSNCSMHA YRYFISTFEG RCLQNFPKLK PFHQNQSVCG NGILEPHEEC
DCGSERECQF KKCCDYNTCK LKGSVKCGSG SCCTSECELS EAGTPCRKSV DQECDFTEYC
SGTSSDCVPD THAMNGELCR LGTAYCYNGR CQTTDNQCAE IFGKGAQGAP FACFKEVNSL
PNRPGDCGFK NSQPLPCEQS DVLCGKLACI WPNKNSYKND VQSAVYSYTQ GHECITTGSA
MRSDGRDYAY VADGTVCGAQ MYCINKTCKK VPLMGYNCNA TTKCRGNGIC NNLGNCHCLP
GYRPPDCELQ IGSPGGSIDD GNDHKSAIVF IKKAYNTHQG NWLILSFYIS LPFFIIFIFM
IMKRNEMRRS CNKENAEYEG HSVMVPESYN VDY
//
