ID H2U0A1_TAKRU Unreviewed; 703 AA.
AC H2U0A1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 78.
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|Ensembl:ENSTRUP00000030360.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000030360.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000030360.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000030360.3}
RP IDENTIFICATION.
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:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; H2U0A1; -.
DR MEROPS; M12.004; -.
DR Ensembl; ENSTRUT00000030477.3; ENSTRUP00000030360.3; ENSTRUG00000011996.3.
DR GeneTree; ENSGT00950000183111; -.
DR HOGENOM; CLU_021966_0_0_1; -.
DR InParanoid; H2U0A1; -.
DR OMA; QIMWDRI; -.
DR OrthoDB; 2876645at2759; -.
DR Proteomes; UP000005226; Chromosome 22.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06263; MAM; 1.
DR CDD; cd03782; MATH_Meprin_Beta; 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; 2.
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; 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:UP000005226};
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..21
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 22..703
FT /note="Meprin A subunit"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5025713289"
FT TRANSMEM 659..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..259
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 266..433
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 431..554
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 608..648
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 156
FT /evidence="ECO:0000256|PIRSR:PIRSR001196-1,
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:PIRSR001196-2"
FT BINDING 155
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 159
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 165
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 703 AA; 78865 MW; 98F6D8CC84132629 CRC64;
MAKRNPPALL LYWLLCGSAL CLPAAKFPDH DVDGGRDLDI FDINEAEGLD LVEGDIVVDE
WQTRNSIIGD EYRWPKTIPY YMEDDLEVNA KGVIMKAFEQ YRLKSCIDFK PWSGEANYIS
IFKGSGCFSS VGNRHVGKQR LSIGSNCDRI ATIEHEFLHA LGFWHEQSRA DRDDYVKIMW
DRITEDKQHN FNTYNDTTSS SLGVPYDYGS MMHYSKTAFS KEGEPTIVTN IPAFSDVIGQ
RMEFSDSDLL KLHRLYNCTG GSTFLDSCDF ERENICGMIQ GQGDKADWVR VASAPGGPHT
DYSNLGKCSG SGYFMHFDTG TANSGDTAQL ESRLLYPKRG QQCLQFYYYN TGGTNDTLKI
HVREYDSANP AGKLRFVETI NASPQKMWQL HHVSLDAKKK FRVVFEGTKE GSGPAAGGLS
LDDINISETM CPEFIWRVKN FSQVMENTPN NQSIFSPPFK SKEGYTFQMQ LYPNGTDRYP
GQLSAFAHLV AREGDAGQKW PCPWKQMTMM LMDQHPHIQK RMSNQRSVTT DPNMKAADSD
QFFWDDPRKV GTEVTDTNGS TYFRGPGAGT AVYLTHLRAK SRDFIKDGDA IFLLTMEDIS
HLTISQPIPN ACQNVECLND GVCVVDEGEA TCRCSVGGDW WYYGDRCQFS GSVSEKTTLA
LASSLSVLGA MVIITVVSVL CVKRKYRKQS NSDTNIDLGA QRL
//
