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Database: UniProt
Entry: H2MM28_ORYLA
LinkDB: H2MM28_ORYLA
Original site: H2MM28_ORYLA 
ID   H2MM28_ORYLA            Unreviewed;       602 AA.
AC   H2MM28;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN   Name=mep1a.1 {ECO:0000313|Ensembl:ENSORLP00000019766.2};
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000019766.2, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000019766.2, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000019766.2,
RC   ECO:0000313|Proteomes:UP000001038};
RX   PubMed=17554307; DOI=10.1038/nature05846;
RA   Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA   Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA   Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA   Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA   Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA   Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT   "The medaka draft genome and insights into vertebrate genome evolution.";
RL   Nature 447:714-719(2007).
RN   [2] {ECO:0000313|Ensembl:ENSORLP00000019766.2}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000019766.2};
RG   Ensembl;
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   -!- 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:PRU01211}.
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DR   AlphaFoldDB; H2MM28; -.
DR   Ensembl; ENSORLT00000019767.2; ENSORLP00000019766.2; ENSORLG00000015782.2.
DR   eggNOG; KOG3714; Eukaryota.
DR   GeneTree; ENSGT00950000183111; -.
DR   HOGENOM; CLU_021966_0_0_1; -.
DR   OrthoDB; 2876645at2759; -.
DR   TreeFam; TF315280; -.
DR   Proteomes; UP000001038; Chromosome 24.
DR   Bgee; ENSORLG00000015782; Expressed in intestine and 7 other cell types or tissues.
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; cd06263; MAM; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000998; MAM_dom.
DR   InterPro; IPR002083; MATH/TRAF_dom.
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:SF828; METALLOENDOPEPTIDASE; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00629; MAM; 1.
DR   Pfam; PF21355; TRAF-mep_MATH; 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; PS00740; MAM_1; 1.
DR   PROSITE; PS50060; MAM_2; 1.
DR   PROSITE; PS50144; MATH; 1.
PE   4: Predicted;
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
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:UP000001038};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361183};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT   CHAIN           19..602
FT                   /note="Metalloendopeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5017098635"
FT   DOMAIN          59..253
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   DOMAIN          260..425
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          423..585
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   602 AA;  69224 MW;  33587E799A5E7BE7 CRC64;
     MGKVLILFGL VFFTTSYAIP VSLEVHEVYE NSEDVNPLLN EGSDANLIEG DILLPKERNA
     LINERYRWQF PIPYILGDDL DLNAKGCVHQ AFEVYRLKSC VDFKPYEGEK SYIKFEKQGG
     CFSSVGKQSD GQILSLGPGC DHKAVIEHEL LHALGFYHEQ SRTDRDDYVN IWLDQVKPGL
     EHNFNAYNDD FITDQNTAYD YESVMHYRPF SFNKNESIPT ITTKIPEFYY IIGQYLDFSE
     KDTLRLNRMY NCSGPLTLLD QCAFEYASIC GMIQASTDDV DWVHTKSTAD AEDHTLLGRC
     RDAGYFMYLN TRIGNPQDSA LLESRTLYPK RKIQCLQFFY KMTGNVQDKL VIWVKMDDGT
     GVVRSMRKIH TFQADSDHTW KIAHVQMEME VKFRYAFQAV RGDPSASSGG IYIDDISLTE
     TRCPSAVWTI HNFSKIMETA DNNTVLNSPR FYSPEGYAYG VRVKPLSEYS DFTGNYTGLY
     FHLASGENDL ILQWPAINRQ ATLVVMDQDP NILLRMSSAR SLTTDMSKAS DGNYRWDNPS
     KVGTYDSSCD CYRGESWGWR NFIKHFDLRR RNYLKNDDLI IFIDFEDLTS LIHTEVPVKP
     NE
//
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