ID A0A3B4EUJ9_9CICH Unreviewed; 649 AA.
AC A0A3B4EUJ9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 9-like {ECO:0000313|Ensembl:ENSPNYP00000001403.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000001403.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000001403.1}
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; A0A3B4EUJ9; -.
DR STRING; 303518.ENSPNYP00000001403; -.
DR Ensembl; ENSPNYT00000001429.1; ENSPNYP00000001403.1; ENSPNYG00000000567.1.
DR GeneTree; ENSGT00940000166115; -.
DR Proteomes; UP000261460; Unplaced.
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: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 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:SF244; ZGC:174164 PROTEIN; 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; 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; PS01186; EGF_2; 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, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT TRANSMEM 616..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 138..330
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 338..424
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 559..593
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 289..294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 396..416
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 583..592
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 649 AA; 70078 MW; B3899148529C9B93 CRC64;
MLQTNIYTSF LFRDFLHPNF VQYSRDAAGN YNTSYPKEHV HCYYHGEVEG YKDSMVALST
CSGLRGVIFF ENKAFGLEPV PQSTTNDHLL YLLEDVQTEP ITCGVVTEAT SVPSHEPFEP
GQSLTSLLRR KRNLPQTSYV ELVLVVDNLR KNNATAVREE MVQMANLLDG YYKQLNIRVV
LVGLEIFKDS NPFSVDGSAG NVLGNFVQWR KTFLVPKIRH DIGQLIVGQS GAYPGGVLGM
AFVGTVCSAS SSGGINVFSN NNLAFVSTVV AHEMGHNLGM NHDSANCACN GKSCIMSGGA
SGATNFSQCS EADFEALILR GGGLCLRNQP AASNVISNPE CGNGLLEQGE QCDCGKPQEC
TNKCCNAATC TFTQGSACAH GACCENCQLK VAGTPCRNSV NTCDLPEYCN GRNESCPNDF
YLMDGLPCEN NAAYCYEGRC QTYDYQCGHL FAPDICFQDA NIQGDRFGNC GSNSNGNYIK
CTLANTMCGK VQCTNVNVNN PPPGATVSIK IVAGKTCVNA DFNLGTDVLD PAYVNPGSPC
ATGKTCVNFQ CVNASALLPN LICDAKTTCN GRGVCNNLGH CHCENGWGPP YCDRSGWGGS
IDSGPAQIDY SLRNGLLIFF LLVVPLLVLL ILVLLYIFRR ESLEPCLKR
//
