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Database: UniProt
Entry: W5Q9C5_SHEEP
LinkDB: W5Q9C5_SHEEP
Original site: W5Q9C5_SHEEP 
ID   W5Q9C5_SHEEP            Unreviewed;      1026 AA.
AC   W5Q9C5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Leucyl-cystinyl aminopeptidase {ECO:0008006|Google:ProtNLM};
GN   Name=LNPEP {ECO:0000313|Ensembl:ENSOARP00000019317.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000019317.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000019317.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000019317.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000019317.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; AMGL01094771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01094772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01094773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01094774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AMGL01094775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012034381.1; XM_012178991.2.
DR   AlphaFoldDB; W5Q9C5; -.
DR   STRING; 9940.ENSOARP00000019317; -.
DR   PaxDb; 9940-ENSOARP00000019317; -.
DR   Ensembl; ENSOART00000019587.1; ENSOARP00000019317.1; ENSOARG00000017994.1.
DR   GeneID; 101102729; -.
DR   KEGG; oas:101102729; -.
DR   CTD; 4012; -.
DR   eggNOG; KOG1046; Eukaryota.
DR   HOGENOM; CLU_003705_2_2_1; -.
DR   OMA; ERFFLSM; -.
DR   OrthoDB; 3085317at2759; -.
DR   Proteomes; UP000002356; Chromosome 5.
DR   Bgee; ENSOARG00000017994; Expressed in thymus and 55 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09601; M1_APN-Q_like; 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; 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   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634016-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002356};
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        111..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;  116996 MW;  3181EC4EED515227 CRC64;
     MEPFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG SRLLVRGLGE
     HELDEDEEDY ESSAKLLGMS FMNRSSGLRN SAAGYRPSSD GTCSAHSART VGVCIFIIIV
     AVAIIMMIYL LPRCIFTKEG CHKKNQPMEP IQPIATNGKL FPWAQIRLPT AVAPVRYDLT
     LHPNLTSMTF RGSVTISLQA LQATWNIVLH STGHNISRVT FMTAVSSQEK EVDVLEYPLH
     EQIAIVAPET LLEGHNYTLK IEYSANISSS SYGFYGISYR DESNEKKYFA ATQFEPLAAR
     SAFPCFDEPA FKATFVIRIK RDEQYTALSN MPKKSSVVLE DGLVQDEFFE SVKMSTYLVA
     FIVGEMKNLS QDVNGTLVSI YAVPEKIGQV HHALETTVKL LDFYQNYFEI QYPLKKLDLV
     AIPDFEAGAM ENWGLLTFRE ETLLYDGNTS SVADRKLVTK IIAHELAHQW FGNLVTMQWW
     NDLWLNEGFA TFMEYFSLEK IFGELSSYED FLDARFKTMR KDALNSSHPI SSSSVQSSEQ
     IEEMFDSLSY FKGASLLLML KTYLSEDIFQ HAIILYLHNH SYTSTHSDDL WDSFNESTNK
     TLDVKKMMRT WTLQKGFPLV TVQRKGKQIL VQQERFSLNV KPEIQPSDAS SLWHIPLSYV
     TDGKNYSKHR SVSLLDKKSG VINLTEEVQW IKVNTNMTGY YIVHYADDNW EALIKQLKTN
     PYVLSDKDRA NLINNIFELA GLGKVSLQRA FDLIDYLRNE TYTAPISEAL FQTELIYNLL
     DKLGHMDLAS RLVNKVFKLL QSQIQQQTWT DEGTPSTREL RTVLLDFACT HSLENCSAAA
     LKLFNDWMAS NGTQSLPTDV MATVFKAGAK TEGGWSFLLS KYVSLGSEAE KNKILKALAS
     SEDVRKLYWL MKKSLDGDLI RTQKLSFIIR TVARHFPGHL LAWDFVKENW SKLVQKFHLG
     SYTIQSIVAG STHLFSTKAH LSEVQAFFEN QSEATFQLRC VQEALEVIQL NMQWVEKNLK
     TLTYWL
//
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