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Database: UniProt
Entry: A0A2Y9P9B2_DELLE
LinkDB: A0A2Y9P9B2_DELLE
Original site: A0A2Y9P9B2_DELLE 
ID   A0A2Y9P9B2_DELLE        Unreviewed;       700 AA.
AC   A0A2Y9P9B2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Meprin A subunit {ECO:0000256|PIRNR:PIRNR001196};
DE            EC=3.4.24.- {ECO:0000256|PIRNR:PIRNR001196};
DE   AltName: Full=Endopeptidase-2 {ECO:0000256|PIRNR:PIRNR001196};
GN   Name=MEP1B {ECO:0000313|RefSeq:XP_022442620.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022442620.1};
RN   [1] {ECO:0000313|RefSeq:XP_022442620.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022442620.1};
RG   RefSeq;
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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_022442620.1; XM_022586912.2.
DR   AlphaFoldDB; A0A2Y9P9B2; -.
DR   STRING; 9749.A0A2Y9P9B2; -.
DR   InParanoid; A0A2Y9P9B2; -.
DR   OrthoDB; 2876645at2759; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd00054; EGF_CA; 1.
DR   CDD; cd06263; MAM; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000998; MAM_dom.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR008294; Meprin.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR049342; TRAF_MEP1_MATH_dom.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF814; MEPRIN A SUBUNIT BETA; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00629; MAM; 1.
DR   Pfam; PF21355; TRAF-mep_MATH; 1.
DR   PIRSF; PIRSF001196; Meprin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   PRINTS; PR00020; MAMDOMAIN.
DR   SMART; SM00137; MAM; 1.
DR   SMART; SM00061; MATH; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50060; MAM_2; 1.
DR   PROSITE; PS50144; MATH; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001196, ECO:0000256|PROSITE-
KW   ProRule:PRU01211};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR001196,
KW   ECO:0000256|PIRSR:PIRSR001196-2};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|PIRNR:PIRNR001196};
KW   Protease {ECO:0000256|PIRNR:PIRNR001196, ECO:0000256|PROSITE-
KW   ProRule:PRU01211}; Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361183};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PIRNR:PIRNR001196, ECO:0000256|PIRSR:PIRSR001196-2};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT   CHAIN           21..700
FT                   /note="Meprin A subunit"
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5015797603"
FT   TRANSMEM        653..677
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          62..256
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   DOMAIN          263..429
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          427..585
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   DOMAIN          604..644
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   ACT_SITE        153
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001196-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         52
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001196-2"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001196-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001196-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001196-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   700 AA;  79670 MW;  D450696372CAFE44 CRC64;
     MDSWYLPSFL FFAALLRVFG LPTPEIFDVD GGIDQDIFDI NEDSGLDLFE GDIRLDGVQE
     RNSIVGERYR WPHTIPYVLD DSLEMNARGV ILNAFERYRL KTCIDFKPWS GEPNYISVFK
     GSGCWSSVGN RRIGKQELSI GKGCDRIATV QHEFLHALGF WHEQSRSDRD DYVSIIWDRI
     ISGKKSNFES YDDRQTDSLN VPYDYSSVMH YSKTAFQNGS EPTIVTRIPD FMDVIGQRMD
     FSDSDILKLN QLYNCSSSLS FMESCDFELE NVCGMIQSSE DSADWQRVSQ VPEGPESDHS
     NMGRCKGSGF FMHFNRSSVN EGATAMLGSR ILYPKRGFQC LQFFLYNSGS EYDQLNIYIR
     EYSAASVNRT LTLVEEIKDI PIGSWQLYHV TLKVTNKFRV VFGGVRGAGA SRGGLSIDDI
     NLSETQCPHH VWHIRNFTQL IGSPSGSVFS PSFYSSKGYA FQIRLNLSSL PNVGMYFHLI
     SGANDDQLEW PCPWQQVTMT ILDQNPDIRQ RMSNKRSITT DPFMTTGNGN YFWDRPSKVG
     VQDFFPNGTQ FQRGRGYGYS VFMTHERLKS RDFMKGDDVY ILLTVEDISH LNTTQNEPIP
     TLGVNDLCTN FKCENDGICI LHHGKAECRC PSGEDWWYMG ERCEKRGSTR DTIVIAVSST
     VAVFAVMLVI TLVSVYCTRK KYQETSSNTT NMTLENQYAL
//
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