ID A0A3P8T4M9_AMPPE Unreviewed; 701 AA.
AC A0A3P8T4M9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
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};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000019163.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000019163.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000019163.1}
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 -!- 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 AlphaFoldDB; A0A3P8T4M9; -.
DR STRING; 161767.ENSAPEP00000019163; -.
DR Ensembl; ENSAPET00000019683.1; ENSAPEP00000019163.1; ENSAPEG00000013681.1.
DR GeneTree; ENSGT00950000183111; -.
DR OMA; FEMFRLR; -.
DR Proteomes; UP000265080; Chromosome 11.
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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
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:SF824; MEPRIN A SUBUNIT ALPHA; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00008; EGF; 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; SM00235; ZnMc; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 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; PS00740; MAM_1; 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:UP000265080};
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}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 25..701
FT /note="Meprin A subunit"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5017855701"
FT TRANSMEM 676..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..258
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 265..429
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 427..583
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 628..668
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 154
FT /evidence="ECO:0000256|PIRSR:PIRSR001196-1,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001196-2"
FT BINDING 153
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 157
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 163
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 701 AA; 78484 MW; 4312A7BCE372AA9A CRC64;
MSSRDSLRKI TALISVLVIL KVQAAPTLSG DDADAGELRD DIPELNRGLD HLFEGDIAGH
PSRNAIIDQT RRWKFPIPYI LTDTLDLNAK GVILQALDEY RLRSCVDFKP YEGETSFISF
AKFSGCWSYV GDDRVGQNLS IGAGCDTKAV VEHELLHTLG FYHEQSRSDR DDYVKIWWDQ
IEEGKEHNFN KYEDDFITDL NTPYDYESIM HYRPLSFNKN ESIPTITTTI PYFNEVIGQR
LDFSAVDITR LNRMYDCANT LTLLNQCSFE LINICGMIQN EDDSADWVQT LSSPTDTDHT
LGGLCRDSGY FMEFDTSSGA AGSSALLESR ILYPNRDQQC LQFFYKMSGA AGDKLVIWIR
TDDGTGAVNS VRKIHTFTGD GDDAWKIAHV PLKVTEKFRY FFQGIRGSVS SSGAILIDDI
TLSEATCPAA VWQIHKFSTY LTSTPTGSKL TSQCFYNSEG YRFGLSVYPN GRDNAYKDYA
AMTFHLCSGE NDGVMQWPVE NRQVTIVAMD QDPDATLRMS STRSFTTDAN PRWNKPTATS
GTWDASCECF RTPDFGWSTF ISHQHLRRRS FLKGDDLIVT VDFNDLTHLI KTEVPVRPPA
PSEDVPEDEP IIEVEFQPEA PKHREARAVD PCYPNPCFNG GVCVASEGEA SCRCATSQAT
FYAGQRCEDL KIDRSILGAL VGGAAGFILL ALAIFTVIRR Q
//
