ID A0A087X3Y4_POEFO Unreviewed; 712 AA.
AC A0A087X3Y4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 24-JAN-2024, entry version 58.
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 Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000000487.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000000487.2}
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 EMBL; AYCK01012077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007567798.1; XM_007567736.2.
DR AlphaFoldDB; A0A087X3Y4; -.
DR STRING; 48698.ENSPFOP00000000487; -.
DR MEROPS; M12.002; -.
DR Ensembl; ENSPFOT00000000488.2; ENSPFOP00000000487.2; ENSPFOG00000000495.2.
DR GeneID; 103148799; -.
DR KEGG; pfor:103148799; -.
DR CTD; 565535; -.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00950000183111; -.
DR OMA; FEMFRLR; -.
DR OrthoDB; 2876645at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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; 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; 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:UP000028760};
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..29
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 30..712
FT /note="Meprin A subunit"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5005106496"
FT TRANSMEM 682..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..263
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 270..434
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 432..589
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 634..674
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 605..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
FT /evidence="ECO:0000256|PIRSR:PIRSR001196-1,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001196-2"
FT BINDING 158
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"
FT BINDING 168
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 712 AA; 79789 MW; 6860A4E7871E376F CRC64;
MLLFNMGPEG RLKKIAVLIG VFAILKVQAA PTITDDEADA GELGDDILEI NRGLTHLFEG
DIAVNPKRNA ILDQTRRWKF PIPYILTDSL DLNAKGVILQ AFEEYRLRSC VDFKPYEGES
TYISFVKLSG CWSYVGDDGT GQNVSIGARC DTKAIVQHEL LHALGFYHEQ SRSDRDDYVK
IWWDEIEEGK GHNFNKYEDD FITDLNTPYD YESIMHYRPF SFNKNESIPT ITTTIPYFND
VIGQRLDFSE VDITRLNRMY DCAETHTLLD QCSFELINIC GMIQNEDDNT DWVQTLSSPS
DGDHTLEGRC RDSGYFMKFD TSSGAVGSTA LLESRILYPK RSEQCLQFFY KMTGAAGDNL
VIWIRSDDGT GAVNTIRKIH TITGDGDDAW KIAHVNLKMS KKFRYIFQGI RGSAGSSGAI
LIDDITLTET VCPSLVWQIR NFTGVLATTP VGTSVRSKCV YNAEGYSFGV SVYPNGRESE
YPDYIGATLH LCSGENDGVM QWPAENRQAT IVALDQDPDV TLRMSSTRSF TSDNNTRWDK
PTATSDAVWD ESCRCYRGQD YGWSTFISHN QLQRRSFLKN DDLIITADFN DLTHLIKTEV
PVERSVQGRD LPDKKEGHEV EMKQEAPKHR KPRAADPCHP NFCLNGGVCV EAGGKALCRC
ATTQTTFYSG PRCEEVKIDR GILGALIGGA AGTVVLTLAI FAVIRRSHTN PF
//
