ID   B4E334_HUMAN            Unreviewed;       452 AA.
AC   B4E334;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   22-FEB-2023, entry version 70.
DE   SubName: Full=cDNA FLJ51465, highly similar to Phosphate-regulating neutral endopeptidase {ECO:0000313|EMBL:BAG65346.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG65346.1};
RN   [1] {ECO:0000313|EMBL:BAG65346.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Uterus {ECO:0000313|EMBL:BAG65346.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; AK304551; BAG65346.1; -; mRNA.
DR   AlphaFoldDB; B4E334; -.
DR   MEROPS; M13.091; -.
DR   PeptideAtlas; B4E334; -.
DR   ProteomicsDB; 5875; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd08662; M13; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1380.10; Neutral endopeptidase , domain2; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR000718; Peptidase_M13.
DR   InterPro; IPR018497; Peptidase_M13_C.
DR   InterPro; IPR042089; Peptidase_M13_dom_2.
DR   InterPro; IPR008753; Peptidase_M13_N.
DR   PANTHER; PTHR11733:SF133; PHOSPHATE-REGULATING NEUTRAL ENDOPEPTIDASE PHEX; 1.
DR   PANTHER; PTHR11733; ZINC METALLOPROTEASE FAMILY M13 NEPRILYSIN-RELATED; 1.
DR   Pfam; PF01431; Peptidase_M13; 1.
DR   Pfam; PF05649; Peptidase_M13_N; 1.
DR   PRINTS; PR00786; NEPRILYSIN.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51885; NEPRILYSIN; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          14..182
FT                   /note="Peptidase M13 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05649"
FT   DOMAIN          241..444
FT                   /note="Peptidase M13 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01431"
SQ   SEQUENCE   452 AA;  53067 MW;  F796365000A037E5 CRC64;
     MIHLPRPPKV LGLQFDWLGY IKKVIDTRLY PHLKDISPSE NVVVRVPQYF KDLFRILGSE
     RKKTIANYLV WRMVYSRIPN LSRRFQYRWL EFSRVIQGTT TLLPQWDKCV NFIESALPYV
     VGKMFVDVYF QEDKKEMMEE LVEGVRWAFI DMLEKENEWM DAGTKRKAKE KARAVLAKVG
     YPEFIMNDTH VNEDLKAIKF SEADYFGNVL QTRKYLAQSD FFWLRKAVPK TEWFTNPTTV
     NAFYSASTNQ IRFPAGELQK PFFWGTEYPR SLSYGAIGVI VGHEFTHGFD NNGRKYDKNG
     NLDPWWSTES EEKFKEKTKC MINQYSNYYW KKAGLNVKGK RTLGENIADN GGLREAFRAY
     RKWINDRRQG LEEPLLPGIT FTNNQLFFLS YAHVRCNSYR PEAAREQVQI GAHSPPQFRV
     NGAISNFEEF QKAFNCPPNS TMNRGMDSCR LW
//