ID A0A3P9D2D5_9CICH Unreviewed; 743 AA.
AC A0A3P9D2D5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 11 {ECO:0000313|Ensembl:ENSMZEP00005028362.1};
GN Name=ADAM11 {ECO:0000313|Ensembl:ENSMZEP00005028362.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005028362.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005028362.1}
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; A0A3P9D2D5; -.
DR Ensembl; ENSMZET00005029264.1; ENSMZEP00005028362.1; ENSMZEG00005021147.1.
DR GeneTree; ENSGT00940000159790; -.
DR Proteomes; UP000265160; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..743
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018178866"
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 190..215
FT /note="Disordered"
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 743 AA; 82646 MW; 931CB169C6E7D4C7 CRC64;
MLAVRCLLFA TVYARYAETA LREWGSPEGR LPPAEEVVQP KRLLQQIHTE EELLHSRLDT
RVKNHPAGEQ PIHLAQSSFL VKAFGTAFIL DLELNHNLLS TDYVERHFEE DGQLSQNMGG
EHCFYHGRIR GVPGSWAALS TCHGLQGMFS DGNFSYGIEP LGTGAENNDH VVFRMPNTDL
FPPPCPGCSM NSTEAKMQSR RQSEEDGELS DEVNWSTEEK PILTEGLRRS RRQVRRGQRT
VQTETKYIEL MVVNDYELFV QLRRSTTQTK IFSKSVVNMA DLIYKEQLNT RIVLVAMETW
SSENRVAVGD DPLLTLRDFM KYRKESIKER VDAVHLFSGR TFMSSRSEAA YIGGICSLTR
GGGINEFGSV GPMAITLSQS LGQNIGMLRN KERTAAGDCR CPDPWLGCIM EDTGYYLPRK
FSRCSIDEYL RFLQQGGGSC LFNKPTKLLD PSECGNGYVE LGEECDCGSL VECTLSGANC
CKKCTLTHNA MCSNGLCCRD CKYELRGVTC RSAVNDCDIP ETCTGDSSQC PHNVHKLDGY
TCEDGQGRCY GGRCKTRDSQ CKTLWGFNSA DRFCYEKLNS EGTERGNCGP HSSGQGWVPC
NKQDVLCGLL LCTNLTDRPR FGELQGKVTS LTIHHQSRYL DCRGGHAVLD DGLDLGYVED
GTPCGPNMMC LERRCLPVTT FNLSTCPGSS SLRICSHHGT CSNEVKCICD PDYTGKDCSV
FDPIPTPTSP DGPEKYKVLC LEM
//