ID A0A287AM26_PIG Unreviewed; 648 AA.
AC A0A287AM26;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Aminopeptidase B isoform a {ECO:0000313|EMBL:HDB79107.1};
DE SubName: Full=Arginyl aminopeptidase {ECO:0000313|Ensembl:ENSSSCP00000044965.1};
GN Name=RNPEP {ECO:0000313|Ensembl:ENSSSCP00000044965.1,
GN ECO:0000313|VGNC:VGNC:95469};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000044965.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000044965.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000044965.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDB79107.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000044965.1}
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:PIRSR634015-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; DQIR01223630; HDB79107.1; -; Transcribed_RNA.
DR STRING; 9823.ENSSSCP00000044965; -.
DR Ensembl; ENSSSCT00000041095.2; ENSSSCP00000044965.1; ENSSSCG00000034151.2.
DR VGNC; VGNC:95469; RNPEP.
DR GeneTree; ENSGT00940000160431; -.
DR OMA; FEMEKPI; -.
DR OrthoDB; 443480at2759; -.
DR Proteomes; UP000008227; Chromosome 10.
DR Bgee; ENSSSCG00000034151; Expressed in blood and 42 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd09599; M1_LTA4H; 1.
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; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR InterPro; IPR034015; M1_LTA4H.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR015211; Peptidase_M1_C.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR45726:SF1; AMINOPEPTIDASE B; 1.
DR PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
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 1: Evidence at protein level;
KW Aminopeptidase {ECO:0000313|EMBL:HDB79107.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634015-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A287AM26};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634015-3}.
FT DOMAIN 498..643
FT /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT C-terminal"
FT /evidence="ECO:0000259|SMART:SM01263"
FT ACT_SITE 324
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 412
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 167..169
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT BINDING 294..299
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 598..600
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
SQ SEQUENCE 648 AA; 72140 MW; 85568D437F568A1D CRC64;
MAGSGPGAGR RVLRSAQAED VASASNFRAF ELLHLHLDLR AEFGPPGPGP GSRGLSGSAV
LELRCLEPGG AAELRLDSHP CLEVTAAVLR RGQPGPGQPE PEPEPVPVCT QPFSHYGQAL
CVRFPQPCSA GEHMQVQLTY RVGEGPGVCW LTPEQTAGKK KPFVYTQGQA VLNRAFFPCF
DTPAVKCRYS ALIEVPDGFT AVMSADTWEK RGPRKFFFQM SQPIPSYLIA LAIGDLVSAE
VGPRSRVWAE PCLIDAAKEE YDGVIEEFLA TGEKLFGPYV WGRYDVLFMP PSFPFGGMEN
PCLTFVTPCL LAGDRSLADV IIHEISHSWF GNLVTNAHWG EFWLNEGFTM FAQRRISTIL
FGAAYTCLEA ATGRALLRQH MDVTGEEHPL NKLRVKIEPG VDPDDTYNET PYEKGFCFVS
YLAHLVGDQD QFDRFLRAYV EEFKFQSILA DDFLEFFLDY FPELKRRKVD SIPGLEFDRW
LNTPGWPPFL PDLSPGDALM KPADELAELW ATEALDMRAI GAVSTSAWKT YQLVYFLDRI
LQKSPLPPGN VKKLGETYPK ISNAQNAELR LRWGQIVLKN DHQEDFWKVK EFLCSQGKQK
YTLPLYHAMM GGSEAARALA KETFAATASQ LHSNVVHYVQ QIVEPLGS
//
