ID A0A3B4EWL5_9CICH Unreviewed; 580 AA.
AC A0A3B4EWL5;
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:ENSPNYP00000001471.1};
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:ENSPNYP00000001471.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000001471.1}
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; A0A3B4EWL5; -.
DR Ensembl; ENSPNYT00000001498.1; ENSPNYP00000001471.1; 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); 2.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
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; 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; PF01421; Reprolysin; 2.
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; 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 547..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..255
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 263..353
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 490..524
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 198
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 214..219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 325..345
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 514..523
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 580 AA; 62205 MW; D08265628BDD41BD CRC64;
GEVEGYKDSM VALSTCSGLR GVIFFENKAF GLEPVPQSTT NDHLLYLLED VQTEPITCGV
VTEATSVPSH EPFEPGQSLT SLLRRKRNLP QTSYVELVLV VDNLRYTFKK NNATAVREEM
VQMANLLDGY YKQLNIRVVL VGLEIFKDSN PFSVDVTRGL CVLGMAFVGT VCSASSSGGI
NVFSNNNLAF VSTVVAHEMG HNLGMNHDSA NCACNGKSCI MSGGASGATN FSQCSEADFE
ALILRGGGLC LRNQPAASNV ISNPECGNGL LEQGEQCDCG KPQECTNKCC NAATCTFTQG
SACAHGACSL WLIIVLFLKV AGTPCRNSVN TCDLPEYCNG RNESCPNDFY LMDGLPCENN
AAYCYEGRCQ TYDYQCGHLF APAADICFQD ANIQGDRFGN CGSNSNGNYI KCTLANTMCG
KVQCTNVNVN NPPPGATVSI KIVAGKTCVN ADFNLGTDVL DPAYVNPGSP CATGKTCVNF
QCVNASALLP NLICDAKTTC NGRGVCNNLG HCHCENGWGP PYCDRSGWGG SIDSGPAQID
YSLRNGLLIF FLLVVPLLVL LILVLLYIFR RESLEPCLKR
//
