ID A0A2J6LLN8_LACSA Unreviewed; 884 AA.
AC A0A2J6LLN8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=LSAT_4X95001 {ECO:0000313|EMBL:PLY88246.1};
OS Lactuca sativa (Garden lettuce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY88246.1};
RN [1] {ECO:0000313|EMBL:PLY88246.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28401891; DOI=10.1038/ncomms14953;
RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT "Genome assembly with in vitro proximity ligation data and whole-genome
RT triplication in lettuce.";
RL Nat. Commun. 8:14953-14953(2017).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Microsome
CC membrane {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004174}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLY88246.1}.
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DR EMBL; NBSK01003172; PLY88246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6LLN8; -.
DR STRING; 4236.A0A2J6LLN8; -.
DR EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_4X95001_mrna; cds-PLY88246.1; gene-LSAT_4X95001.
DR Gramene; rna-gnl|WGS:NBSK|LSAT_4X95001_mrna; cds-PLY88246.1; gene-LSAT_4X95001.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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:SF274; 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|RuleBase:RU364040};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040}; Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 27..195
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 231..446
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 536..854
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 303
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 387
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 884 AA; 101309 MW; 126C257AA33E7C5D CRC64;
MNIMNQNEEQ KLEHLKGQSR LPKFATPHRY HLALKPNLEL CNFSGSVLVD LSILESTRFL
VLNSIDLVIT ESSFTDSNKH QVVPSEVVVD NDAEMLVLVF EAPLGVGEGV LEINFTGILN
EHMKGFYKGT YVDEGVRKNM AVTQFEPADA RRCFPCWDEP ALKASLSNMP VSKETINGDF
KTICFEETPI MSTYLVAVVI GLFDYIEETT PDGVRVRAYC PVGKSEKGKL ALSISIKALE
LYTKYFSMPY TLPKLDMVAV PDFSGGAMEN YGLITFRETE LLHDNLHSAA ANIQRLSIVV
THEVGHQWFG NLVTMEWWTH LWLNEGFATW VSYLATDVLF PEWRIWTQFL EVTAGGLRID
SLEQSHPVEV EVENANSVLE VFDAISYKKG SSLVRMLKEY LGDEIFQKSL SSYMKKYAFK
NAKTEDLWSV LTEESGFEVN KLMDIWTKQT GYPVIYVRFE NNTLEFVQTR FMSLGLQSEG
QWIVPITLSL GSYSNHKKFL LETKVGKLDL SELYHSYYTS LNQNGNKNQE VDEKLWVKVN
IGHTGFYRVK YDITLTARLR KAIQDKCLSP EDKFGILDDT YALCEAGEES ILSLLSLMDL
YRDDLDYLVL SRLISVCYNV AKILKDAIYD PWNHLNQFFI DLIISSAEKL GVEPVSGESH
LNTMLREEVF MALATFGHKE THEELKKRFQ TYMNDKNTSV FPVDIRKAAY ISIMRTSSAL
ERSDFDSLLK LYRETDAVQE KTRILSCIAS SPESDIVTEV LNLMFSNQIR EQDTIYVTAR
ISLEARETSW IWLKDNWDVI VKRWGQGMVF HHFIRDIVTP FSSNEKAEEV EEFFGSRVSP
SFSRNLKQSI EQIRIKAKWI EKVRKEESLI PKLARGLTRS PMLT
//
