GenomeNet

Database: UniProt
Entry: A0A3P9D2D5_9CICH
LinkDB: A0A3P9D2D5_9CICH
Original site: A0A3P9D2D5_9CICH 
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
//
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