ID A0A3B4YND5_SERLL Unreviewed; 812 AA.
AC A0A3B4YND5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 11-like {ECO:0000313|Ensembl:ENSSLDP00000024309.1};
GN Name=ADAM11 {ECO:0000313|Ensembl:ENSSLDP00000024309.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000024309.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000024309.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B4YND5; -.
DR STRING; 1841481.ENSSLDP00000024309; -.
DR Ensembl; ENSSLDT00000025080.1; ENSSLDP00000024309.1; ENSSLDG00000018928.1.
DR GeneTree; ENSGT00940000159790; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000261360; 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; cd00054; EGF_CA; 1.
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; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF114; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 11; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF01562; Pep_M12B_propep; 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; SSF57196; EGF/Laminin; 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; 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}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..812
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017337205"
FT DOMAIN 246..445
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 451..538
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 682..719
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 184..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 510..530
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 709..718
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 812 AA; 90264 MW; A05B8D1376F4B57C CRC64;
MLAVRCLLFA AVCARCAVTG LREWASLEER LLPAEEVVQP KRLLQQIHSQ EELLHSRLDT
RVKNYTAGAQ PVHLAQSSFL VEAFGTSFIL DLELNHNLLS TDYVERHYGE DGKPSQSMGG
EHCYYHGRVR GLPGSWAALS TCHGLRGMFS DGNFSYGIEP VGSGEEHNDH IVYRMPDIDL
FPPPCPGCSV NSSEPEGRPD GHSERDRELT DGDGWSEEEK PVLTAGLKRS KRQVRRGQRT
VQTETKYIEL MVVNDHELFV QLRRSSTQTK NFAKAVVNMA DAIYKEQLNT RIVLVAMETW
LSENRVSVGD DALLTLRDFM KYRKESIKER CDTVHLFSGR TFMSSRSEAA YIGGICSLTR
GGGINEFGSV GPMAITLCQS LGQNIGMLRN KERTAAGDCR CPDPWLGCIM EDTGYYLPRK
FSRCSIDEYL RFLQQGGGSC LFNKPSKLLD QPECGNGYVE PGEECDCGSL VDCARSGANC
CKKCTLTHNA MCSNGLCCRD CKYELRGVTC RDTVNDCDIS ETCTGDSSQC PHNVHKLDGY
MCDAGQGRCY GGRCKTRDGQ CRTLWGYNSA DRFCYEKLNS EGTEKGNCGP DSSGQGWVQC
NKQDVLCGLL LCTNLTAKPR FGEMQGKLTS LTIHHQNRYL DCRGGHAVLD DGLDLGYVED
GTPCGPNMMC LERRCLPVTT FNLSTCPGSS SSRICSHHGT CSNEVKCICD PDYTGKDCSV
FDPIPIPTPP EGPEKYRETS EEEDLQEFES YAVLSSLPHV QSALRRQNKD VFRLRAIRPF
VFPLFLTLLK LSLPVFSPSG KSNYFLTVVQ KP
//
