ID   A0A3P8R769_ASTCA        Unreviewed;       492 AA.
AC   A0A3P8R769;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 6 {ECO:0000313|Ensembl:ENSACLP00000037793.1};
GN   Name=ADAMTS6 {ECO:0000313|Ensembl:ENSACLP00000037793.1};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000037793.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000037793.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000037793.1}
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:PRU00276}.
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DR   AlphaFoldDB; A0A3P8R769; -.
DR   STRING; 8154.ENSACLP00000037793; -.
DR   Ensembl; ENSACLT00000038678.1; ENSACLP00000037793.1; ENSACLG00000025480.1.
DR   GeneTree; ENSGT00940000156571; -.
DR   OMA; CKYGVRS; -.
DR   Proteomes; UP000265100; Chromosome 7.
DR   Bgee; ENSACLG00000025480; Expressed in ovary and 2 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR   Gene3D; 3.40.1620.60; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   PANTHER; PTHR13723:SF27; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 6; 1.
DR   PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   TRANSMEM        6..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        327..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          230..438
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         373
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         377
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         383
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   492 AA;  55706 MW;  B398DA88B17B3AB7 CRC64;
     ASYTYFHNIF LFLFHSLLFL VKEEFLSYLQ HYQLTVPVRV DENGEFLSYT VKHHRPGRRR
     RGAPRLFYRL SAYGKHFHLN LTLNPHLVSK HFTVEYWGKE GLEWRHNMVD NCHYIGFLQN
     QHSTTRVALS NCKGLHGVIT TEEEQYLIEP LKNISSTTSG EWNLEEAQQH VIYKMSAIPS
     PQEHSQEFSC GISDLIKTSA PCQLSTPLPQ NYSKLSNSTH RQKRSISTER FVETLVVADK
     MMVGYHGRKD IEHYILSVMN IVAKLYRDAS LGNVVNIIVT RLIVLTEDQP NLEINHHADK
     SLDSFCKWQK SILSHHSDGN KCFASTLCLY VCLACVFMCV CLGLASVAGM CEPERSCSIN
     EDIGLGSAFT IAHEIGHNFG MNHDGIGNSC GTKGHETAKL MAAHITANTN PFSWSACSKD
     YITSFLDSGR GTCLDNEPLK RDFLYPTVAP GQVYDADEQC RFQYGTSSRQ CKYGVRNQHL
     SDYSPPDSSS LH
//