ID A0A3B4ZDF0_9TELE Unreviewed; 997 AA.
AC A0A3B4ZDF0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000005561.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000005561.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
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; A0A3B4ZDF0; -.
DR STRING; 144197.ENSSPAP00000005561; -.
DR Ensembl; ENSSPAT00000005674.1; ENSSPAP00000005561.1; ENSSPAG00000004282.1.
DR GeneTree; ENSGT00940000157225; -.
DR Proteomes; UP000261400; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0048264; P:determination of ventral identity; IEA:Ensembl.
DR GO; GO:0035124; P:embryonic caudal fin morphogenesis; IEA:Ensembl.
DR GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
DR GO; GO:0001885; P:endothelial cell development; IEA:Ensembl.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 4.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 4.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR034036; ZnMP_TLD/BMP1.
DR PANTHER; PTHR24251:SF42; BONE MORPHOGENETIC PROTEIN 1; 1.
DR PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 4.
DR Pfam; PF14670; FXa_inhibition; 2.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 4.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 4.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01180; CUB; 4.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT DOMAIN 119..318
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 320..432
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 433..545
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 545..586
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 589..701
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 701..741
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 745..785
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 82..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 181..203
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 183..184
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 997 AA; 112576 MW; 9A55BDE9F1B08E94 CRC64;
MTSTRVNLFP NTVYSMKMNN YILLFPRMLK MMTDMLLIML VMIIKTFLCF LPAVFWGDIA
LDEEDLRMFQ IDRTIDLTQH THIHTHSRQG ATPGTASPKS QTGKGGKTGK VVKSRIPRAA
TSRAERIWPG GVIPYVIGGN FTGSQRAMFK QAMRHWEKQT CVTFIEKTDE ESYIVFTYRP
CGCCSYVGRR GNGPQAISIG KNCDKFGIVV HELGHVIGFW HEHTRPDRDD HVTIIRDNIQ
PGQEYNFLKM EPGEVNSLGE PYDFDSIMHY ARNTFSRGMF LDTILPSRDE NGVRPAIGQR
TRLSKGDIAQ ARKLYRCPAC GETLQESTGN FSSPGYPNGY PSYTHCVWRI SVTPGEKIVL
NFTTMDLYKS SLCWYDYIEV RDGYWRKAPL LGRFCGDKVP EVLISSDSRM WIEFRSSSNW
VGKGFAAIYE AICGGEITKD SGQIQSPNYP DDYRPSKECV WRITVSEGYN VGLSFQAFEI
ERHDSCAYDY LEVRDGPLET SPLIGRFCGY DKPEDVRSTS HTLWMKFVSD GTVNKAGFAA
NFFKEEDECA KPDNGGCEQR CVNTLGSFKC ACDPGYELAP DKKSCEAACG GLLSKLNGTI
STPGWPKEYP PNKNCVWQVV APTQYRISMQ FEAFELEGNE VCKYDYVEVR SGLSSDSKLH
GKYCGTEVPE VITSQYNNMR IEFKSDNTVS KKGFKAHFFS DKDECSKDNG GCQHECINTV
GSYVCQCRHG FVLHENKHDC KEAECEHKIH SPSGTLSSPN WPDKYPSRKE CTWDITATPG
HRVKIVSVHQ MKRATRVSLE HDWRTSLPYL ICVTSEKRKA ENPLSCDARI VQSLSHKLGN
DCKQRFAGCQ NTVIPNLSSV SRLLDYSTTR FGSKKHVCHK RTGFKLVLPK IQVQEQTVTH
TCSHSHSVLQ IILLKSTHVP MQVVSHTHTH THTNTVFTVC THMAGLDDTR THSTVVLQNV
RICLFTSPPP CSHMLGVIKI VINCHLVLII SFCRLCN
//
