ID A0A3Q3BHF5_KRYMA Unreviewed; 776 AA.
AC A0A3Q3BHF5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 11-like {ECO:0000313|Ensembl:ENSKMAP00000024224.1};
GN Name=ADAM11 {ECO:0000313|Ensembl:ENSKMAP00000024224.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000024224.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000024224.1}
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; A0A3Q3BHF5; -.
DR STRING; 37003.ENSKMAP00000024224; -.
DR Ensembl; ENSKMAT00000024530.1; ENSKMAP00000024224.1; ENSKMAG00000017965.1.
DR GeneTree; ENSGT00940000159790; -.
DR OMA; CIMEDTS; -.
DR Proteomes; UP000264800; 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; 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; 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; 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}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
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..776
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018744784"
FT DOMAIN 233..432
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 438..525
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 669..706
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 188..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 497..517
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 696..705
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 776 AA; 86093 MW; 21C3552240CC4598 CRC64;
MLAVRCLLFA AVCARCAETG SPAGPRGQLR LEEERVRPKR LVQQSHAEEE LLHNHLDTRT
RGPPAGQQQP THLAQSSFLV EAFGSSFILD LELNHNLLST DYVERHFEDG QLSETMGGEH
CYYHGRVRGL PDSWVALSTC HGLQGMFSDG NFSYGIEPVD SGEKDHLVYR MPDLDLFQLS
CPGCFTNSSE PEGKTDGHSK RDDDLKDGEE QHILRRSKRQ ARRGQRTVQT ETKYIELMVV
NDYELFVQLR RMVPQTKIFA KSVVNMADLI YKEQLKTRIS LVAMETWSTE NKIAVVDDAL
LTLRDFMKYR KESIKERCDA VHLFSGRTFM SSRSEAAYIG GICSLTRGGG INEFGSVSPM
AITLCQSLGQ NIGMLRVKKR PAAGGCRCPD QWLGCIMEDT GYYLSRRFSS CSIDEYHRFL
QQGGGSCLFN KPTKLLDPSE CGNGYVEPGE ECDCGSLVEC AQSGASCCKK CTLPHNAMCS
NGLCCRDCKY ELRGVTCRDA VNDCDIPETC TGDSSQCPHN VHKLDGYTCD TGQGRCYGGR
CKTRDGQCRA LWGYNSADRF CYEKLNSEGT DKGNCGLDPS SQEWVPCNKQ DVLCGLLLCT
NLTERPRIGE LQGKVTSLTV HHQNRYMDCR GGHAVLDDGM DLGYVEDGTP CGPNMMCLER
RCLAVTTFNL SSCPGSSSSH VCSHHGICSN EVKCICDPDY TGKDCSVFDP IPTLTPADGP
EKYRGVRLPG VPFSFRLRPA GRVDGLLVVP HTFKLGIRRL RGQECGPFCS KYILST
//
