ID   M3ZHR2_XIPMA            Unreviewed;       845 AA.
AC   M3ZHR2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Aminopeptidase O (putative) {ECO:0000313|Ensembl:ENSXMAP00000001754.2};
GN   Name=AOPEP {ECO:0000313|Ensembl:ENSXMAP00000001754.2};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000001754.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000001754.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000001754.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   STRING; 8083.ENSXMAP00000036709; -.
DR   Ensembl; ENSXMAT00000001758.2; ENSXMAP00000001754.2; ENSXMAG00000025369.1.
DR   Ensembl; ENSXMAT00000026414.1; ENSXMAP00000036709.1; ENSXMAG00000025369.1.
DR   eggNOG; KOG1047; Eukaryota.
DR   GeneTree; ENSGT00940000155211; -.
DR   HOGENOM; CLU_084103_0_0_1; -.
DR   OMA; FARCSQA; -.
DR   OrthoDB; 3108672at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.2010.30; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 1.25.40.320; Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR033577; AOPep.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR   InterPro; IPR015211; Peptidase_M1_C.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR46627; AMINOPEPTIDASE O; 1.
DR   PANTHER; PTHR46627:SF1; AMINOPEPTIDASE O; 1.
DR   Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   SMART; SM01263; Leuk-A4-hydro_C; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852}.
FT   DOMAIN          694..844
FT                   /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT                   C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01263"
FT   REGION          60..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   845 AA;  95176 MW;  3793F4399D38A952 CRC64;
     MEPDGELNPD TDDLPLRANT NHILVRHYVL DLTVCFDKKI ISGSIVLFLE PCSAEIAKTK
     DAIGPETGDG ARQEPNEEGT KLGSDTQSSD LFHSSNAEDF TLVLDCCDLE VSKVEEVDTN
     SVSAALGFPL TAASEDISLD SQADFIQHLF SMPSSHWKEK HRRFLLCSRS PGVQNSNSLH
     FHTDRWSLKL KKMGVTTSQG FPRIIRIYYM TRPLGGSVRW TKDQDNRECV YTAGSPINNR
     ALFPCQEPPV AMSTWQARVW APSDCVVLMS GEDEAVPAED GDTPFLSWNY YVTMPMPAST
     FTLAVGHWCQ VPTEAPSALE NEVEDEVGCS CLKTELGSEL TRSPGEVVRG APCQIGRDEA
     TSSDSAFCHS SLGHKELSLT DYSGMEDDGI SCSHGDYPCR FAERSAWSQR VVPHRVFSPA
     CLLQKAQMGI LKLLPQCLAA AHAVLGVHPF PRLDVLIVPA GFSSLGMASP HIIFLSQSVL
     CKECPGSGLN RLTLSGSRIC HEIAHSWFGL VIGARDWTEE WISEGFATFL EDIIWAQAQQ
     LSSQQTAEQF DLKALLRWRR LSDELQNSNE ELQILRPNME RTGQVSDSGS STIKHALNPD
     KTFMQVHYLK GYFLLRFLAS EVGDQHLIDF FRLFVKKYHG QLVLSQDFLR MFLITFPHME
     RKGLTLSAIY ADWLDRPGIP EWLHERSAVW SQARLVEEVK AEVVKWILSS RTHQAKGRKR
     KRTEPKVNYK ELTTEQLVML LELLLEESEL SVPSMRALHK TYNLQNQDAE VRHRWCELVV
     KHAYSQAYCD VEDFLLHDQA MGVYLYGELM VQEDPEQQAL ARRCLGLVQE EMDQSARRVV
     EEMIL
//