ID A4II36_XENTR Unreviewed; 722 AA.
AC A4II36; F6QSE4;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 128.
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:NP_001096352.1,
GN ECO:0000313|RefSeq:XP_031759034.1,
GN ECO:0000313|Xenbase:XB-GENE-1001365};
GN Synonyms=LOC100124942 {ECO:0000313|EMBL:AAI35833.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI35833.1};
RN [1] {ECO:0000313|RefSeq:NP_001096352.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI35833.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Whole embryo {ECO:0000313|EMBL:AAI35833.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001096352.1, ECO:0000313|RefSeq:XP_031759034.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_031759034.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_031759034.1};
RG RefSeq;
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}.
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DR EMBL; BC135832; AAI35833.1; -; mRNA.
DR RefSeq; NP_001096352.1; NM_001102882.1.
DR RefSeq; XP_031759034.1; XM_031903174.1.
DR MEROPS; M12.004; -.
DR PaxDb; 8364-ENSXETP00000061320; -.
DR DNASU; 100124942; -.
DR GeneID; 100124942; -.
DR KEGG; xtr:100124942; -.
DR AGR; Xenbase:XB-GENE-1001365; -.
DR CTD; 4225; -.
DR Xenbase; XB-GENE-1001365; mep1b.
DR eggNOG; KOG3714; Eukaryota.
DR HOGENOM; CLU_021966_0_0_1; -.
DR OMA; VYCTRKR; -.
DR OrthoDB; 2876645at2759; -.
DR PhylomeDB; A4II36; -.
DR TreeFam; TF315280; -.
DR Proteomes; UP000008143; Chromosome 6.
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; 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; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS50144; MATH; 1.
PE 2: Evidence at transcript level;
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:UP000008143};
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..18
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 19..722
FT /note="Meprin A subunit"
FT /evidence="ECO:0000256|RuleBase:RU361183,
FT ECO:0000313|RefSeq:NP_001096352.1"
FT /id="PRO_5033207306"
FT TRANSMEM 674..699
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..589
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 625..665
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 597..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..623
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 722 AA; 81360 MW; C99CC065E43C0BBA CRC64;
MKPMVLPLIL LSLHNVIGVP LQDNTEIDVD GGKKLDIFDI NEGAGLDLFE GDIILADTNQ
RNSIIGDRYR WPIPVPYFLE DSLEINAKAL VLEAFERYRL KTCIDFKPWE GEPNYISVFK
DSGCYSYVGN LRQGKQQLSL GVNCDRIATI QHEFLHALGF WHEQSRADRD DYVTIVWDRI
LPGREHNFNV YDDTRSNSLN VPYDYTSVMH YSKTAFQNGS EPTIVTKIDA FSDVIGQRMD
FSDYDLEKLN RLYNCSSSIS FMDSCTFEYN NICGMIQGTG DNSDWNHVLL SAAGPSNDHT
HLGNCKDSGY YMHFSTSTGN AGDKALLESR LFYPKRGFQC LEFFYYYNGN ENDALNIWIR
EYTEASPNGT LTFITSIKGN PAEYWQLHHV SLNVKNKFRV VFEGVKGNGP SNGGFAIDDI
NFSEALCPHY IWHIRNFTHE SIKENGRIYS PPLYSKDGYA YQVQVRPNGP ADSPYDLAIY
FHLISGANDD TLQWPCSLRQ AKMELMDQNP DIRKRMSNQR SITTDPTQVA SNGDLFWDKP
AKVGTSVTFP NGTQFFRGPG YGTSAFISHD RLHSRDFLKG GDAFFLLSVE DVSHLSASQP
TPVPTTTTKP PVTDIPSPTK PGPDVPKECE GFGCKNDGVC VLENEKPVCR CKVTKDWWYV
GDKCERKVSS QDTLVIAVSS SVTIFAVMLI ITLTSVLCLK KKHKKQIAKA GKAQTTENAY
TF
//
