ID A0A2K6AIX5_MANLE Unreviewed; 715 AA.
AC A0A2K6AIX5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=ADAM metallopeptidase domain 18 {ECO:0000313|Ensembl:ENSMLEP00000040019.1};
GN Name=ADAM18 {ECO:0000313|Ensembl:ENSMLEP00000040019.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000040019.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000040019.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_011848847.1; XM_011993457.1.
DR AlphaFoldDB; A0A2K6AIX5; -.
DR Ensembl; ENSMLET00000063642.1; ENSMLEP00000040019.1; ENSMLEG00000044031.1.
DR GeneID; 105549080; -.
DR GeneTree; ENSGT00940000162281; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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:UP000233140};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..715
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014343775"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 177..357
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 366..455
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 596..630
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 313..318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 620..629
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 715 AA; 80733 MW; 12304ECBE118F078 CRC64;
MFFLLAFLTE LGRLQAHVGS EGIFLHVTVP RKILSNDSEV SERKMIYIIT IDGQPYTLHL
RKQSFLPQNF LVYTYNEAGS LHSESPYFMM HCHYQGYAAK FPNSFVTLSV CSGLRGFLQF
ENVSYGIEPL ESSARFEHII YQLKNNDPNV SILAENYSHI WQKDQSYKVP LNSQKKNLSK
LLPQYLEIYI IVEKALMFTQ FKLTVILSSL ELWSNENQIS TSGDADDILQ RFLAWKRDYL
ILRPHDIAYL LVYRKHPKYV GATFPGTICN ESYDAGIAMY PDAIDLEGFS VIIAQLLGLK
VGLTYDDITQ CFCLRATCIM NHEAVSARGI KIFSNCSMHD YRYSVSKFEA KCLQKLSNLQ
PLHQNQPVCG NGILESNEEC DCGNKKECQF KKCCDYNTCK LKGSVKCGSG PCCTSKCELS
IVGTPCRKSV DPECDFTEYC NGTSSDCVPD TYALNGHLCK LGTAYCYNGQ CQTTDNQCAK
IFGKGAQGAP FACFKEVNSL HERSENCGFK NSQPLPCEKK DVLCGKLACV QPHKNAYKSD
IQYTVYSYIQ DHVCVSIATG SSMRSDGTDN AYVADGTMCG PEMYCVNKTC RKVHLTGYNC
NTTTKCKGKG ICNNFGNCQC FPGHKPPDCK FQFGSPGGSI DDGNFQKSDE FYTEKGYNTH
WNNWFILSFY IVLPFFIIFT IVIFKRNEIR KLCNRENTEC KRNSSAVSES YDVEH
//
