ID A0A2Y9KI25_ENHLU Unreviewed; 828 AA.
AC A0A2Y9KI25;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN Name=LOC111156717 {ECO:0000313|RefSeq:XP_022373497.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022373497.1};
RN [1] {ECO:0000313|RefSeq:XP_022373497.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022373497.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_022373497.1; XM_022517789.1.
DR AlphaFoldDB; A0A2Y9KI25; -.
DR Proteomes; UP000248482; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 5.
DR CDD; cd00054; EGF_CA; 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; 5.
DR InterPro; IPR015446; BMP_1/tolloid-like.
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 PANTHER; PTHR24251:SF42; BONE MORPHOGENETIC PROTEIN 1; 1.
DR PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 5.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 5.
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; 5.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01180; CUB; 5.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001199-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001199-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 1..162
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 164..276
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 277..389
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 389..430
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 433..545
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 589..701
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 702..818
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-1,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 828 AA; 93483 MW; 54117194737519CC CRC64;
MRTATSYSPT DPAARDRPPE LAPPSRCCSY VGRRGGGPQA ISIGKNCDKF GIVVHELGHV
IGFWHEHTRP DRDRHVSIVR ENIQPGQEYN FLKMELQEVE SLGETYDFDS IMHYARNTFS
RGIFLDTIVP KYEVNGVKPP IGQRTRLSKG DIAQARKLYK CPACGETLQD STGNFSSPEY
PNGYSAHMHC VWRISVTPGE KIILNFTSMD LYRSRLCWYD YVEVRDGFWR KAPLRGRFCG
GKLPEPIVST DSRLWVEFRS SSNWVGKGFF AVYEAICGGD VKKDNGHIQS PNYPDDYRPS
KVCIWRIQVS EGFHVGLTFQ SFEIERHDSC AYDYLEVRDG HSESSTLIGR YCGYEKPDDI
KSTSSRLWLK FVSDGSINKA GFAVNFFKEV DECSRPNRGG CEQRCLNTLG SYKCSCDPGY
ELAPDKRRCE AACGGFLTKL NGSITSPGWP KEYPPNKNCI WQLVAPTQYR ISLQFDFFET
EGNDVCKYDF VEVRSGLTAD SKLHGKFCGS EKPEVITSQY NNMRVEFKSD NTVSKKGFKA
HFFSDKDECS KDNGGCQQDC VNTFGSYECQ CRSGFVLHDN KHDCKEAGCD HKVTSTSGTI
TSPNWPDKYP SKKECTWAIS STPGHRVKLT FVEMDIESQP ECAYDHLEVY DGRDAKAPVL
GRFCGSKKPE PVLATGSRMF LRFYSDNSVQ RKGFQASHST ECGGQVRAEV KTKDLYSHAQ
FGDNNYPGGV DCEWVIVAEE GYGVELVFQT FEVEEETDCG YDYMELFDGY DSTAPRLGRY
CGSGPPEEVY SAGDSVLVKF HSDDTITKKG FHLRYTSTKF QDTLHSRK
//
