ID   A0A9L0JGC2_EQUAS        Unreviewed;      1026 AA.
AC   A0A9L0JGC2;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   02-SEP-2026, entry version 15.
DE   RecName: Full=Leucyl-cystinyl aminopeptidase {ECO:0000256|ARBA:ARBA00071211};
DE            EC=3.4.11.3 {ECO:0000256|ARBA:ARBA00066490};
DE   AltName: Full=Oxytocinase {ECO:0000256|ARBA:ARBA00080172};
GN   Name=LNPEP {ECO:0000313|Ensembl:ENSEASP00005052244.1};
OS   Equus asinus (Donkey) (Equus africanus asinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9793 {ECO:0000313|Ensembl:ENSEASP00005052244.1, ECO:0000313|Proteomes:UP000694387};
RN   [1] {ECO:0000313|Ensembl:ENSEASP00005052244.1, ECO:0000313|Proteomes:UP000694387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=33293529;
RA   Wang, C., Li, H., Guo, Y., Huang, J., Sun, Y., Min, J., Wang, J., Fang, X.,
RA   Zhao, Z., Wang, S., Zhang, Y., Liu, Q., Jiang, Q., Wang, X., Guo, Y., Yang,
RA   C., Wang, Y., Tian, F., Zhuang, G., Fan, Y., Gao, Q., Li, Y., Ju, Z., Li,
RA   J., Li, R., Hou, M., Yang, G., Liu, G., Liu, W., Guo, J., Pan, S., Fan, G.,
RA   Zhang, W., Zhang, R., Yu, J., Zhang, X., Yin, Q., Ji, C., Jin, Y., Yue, G.,
RA   Liu, M., Xu, J., Liu, S., Jordana, J., Noce, A., Amills, M., Wu, D.D., Li,
RA   S., Zhou, X. and Zhong, J.;
RT   "Donkey genomes provide new insights into domestication and selection for
RT   coat color.";
RL   Nat. Commun. 11:6014-6014(2020).
RN   [2] {ECO:0000313|Ensembl:ENSEASP00005052244.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Cys-|-Xaa-, in which the
CC         half-cystine residue is involved in a disulfide loop, notably in
CC         oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl
CC         arylamides exceed that for the cystinyl derivative, however.;
CC         EC=3.4.11.3; Evidence={ECO:0000256|ARBA:ARBA00052614};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC   -!- SUBUNIT: Homodimer. Binds tankyrases 1 and 2.
CC       {ECO:0000256|ARBA:ARBA00062849}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   AlphaFoldDB; A0A9L0JGC2; -.
DR   Ensembl; ENSEAST00005061505.1; ENSEASP00005052244.1; ENSEASG00005018806.2.
DR   GeneTree; ENSGT00940000157902; -.
DR   Proteomes; UP000694387; Chromosome 11.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-ARBA.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:TreeGrafter.
DR   GO; GO:0042277; F:peptide binding; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:TreeGrafter.
DR   CDD; cd09601; M1_APN-Q_like; 1.
DR   FunFam; 1.10.390.10:FF:000010; Leucyl-cystinyl aminopeptidase; 1.
DR   FunFam; 1.25.50.20:FF:000003; Leucyl-cystinyl aminopeptidase; 1.
DR   FunFam; 2.60.40.1730:FF:000001; Leucyl-cystinyl aminopeptidase; 1.
DR   FunFam; 2.60.40.1910:FF:000001; Leucyl-cystinyl aminopeptidase; 1.
DR   Gene3D; 1.25.50.20; -; 1.
DR   Gene3D; 2.60.40.1910; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR034016; M1_APN-typ.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR050344; Peptidase_M1_aminopeptidases.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF42; LEUCYL-CYSTINYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634016-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694387};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
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|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   TRANSMEM        110..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          174..358
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          393..611
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          690..1009
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        465
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         464
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         468
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         487
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            550
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   1026 AA;  117373 MW;  91F37BE09994E076 CRC64;
     MEPFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG SRLLVRGLGE
     HEMDEDEEDY ESSAKLLGMS FMNRSSGLRN SAAGYRQSPD GTCSLPSARA MVVCASVIVI
     AVAVIMVIYL LPRCTFTKEG CHKKNQSMVL IQPLATNGKL FPWAQIRLPT AIMPLRYELN
     LHPNLTSMTF RGSVTISLQA LQATWNIILH STGHNISRVT FMSAVSSQEK HAEVLEYPFH
     EQIAIVAPDA LLEGHNYTLK IEYSANISSS YYGFYGISYT DESNEKKYFA ATQFEPLAAR
     SAFPCFDEPA FKATFIIRII RDEQYTALSN MPKKSSVIME DGLVQDEFSE SVKMSTYLVA
     FVVGEMKNLS QDINGTLVSI YAVPEKIGQV HHALETTVKL LEFYQNYFEI QYPLKKLDLV
     AIPDFEAGAM ENWGLLTFRE ETLLYDNTTS SVVDRKLVTK IIAHELAHQW FGNLVTMQWW
     NDLWLNEGFA TFMEYFSLEK IFEDLSSYED FLDARFKTMK KDSLNSSHPI SSLSVQSSEQ
     IEEMFDSLSY FKGASLLLML KTYLSEDVFQ HAIVLYLHNH SYAAVRSDDL WDSFNEVTNK
     TLDVKKMMKT WTLQKGFPLV TVQRKGKELL VQQERFFLNT KPEIQPSDAS YLWHIPLSCV
     TEGRNYSKYP LVLLLDKKSG VINLTEEVQW VKVNTNMNGY YIVHYADDDW EALIKQLKIN
     PYVLSDKDRA NLINNIFELA GLGKVPLQRA FDLIDYLGNE TFTAPITEAL FQTGLIHNLL
     EKLGYMDLAS RLATRVFKLL QSQIQQQTWT DEGTPSIREL RSVLLEFACT HSLENCSTIA
     MKLFDDWVAS NGTQSLPTDV MTTVFKVGAK TESGWSFLLS KYISIGSEAE KNKILEALAS
     SEDVRKLYWL MKTSLDGDII RTQKLSFVIR TVARRFPGHL LAWDFVKENW NKLVQKFHLG
     SYTMHSIVAG STHLFSTKAH LSEVQAFFES QSETTFRLRY VQEALEVIQL NIQWMEKNLK
     ALTWWL
//