ID A0A212EJS3_DANPL Unreviewed; 2660 AA.
AC A0A212EJS3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Aminopeptidase N2 {ECO:0000313|EMBL:OWR41737.1};
GN ORFNames=KGM_209838 {ECO:0000313|EMBL:OWR41737.1};
OS Danaus plexippus plexippus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR41737.1, ECO:0000313|Proteomes:UP000007151};
RN [1] {ECO:0000313|EMBL:OWR41737.1, ECO:0000313|Proteomes:UP000007151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-2 {ECO:0000313|EMBL:OWR41737.1};
RX PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT "The monarch butterfly genome yields insights into long-distance
RT migration.";
RL Cell 147:1171-1185(2011).
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: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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:OWR41737.1}.
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DR EMBL; AGBW02014405; OWR41737.1; -; Genomic_DNA.
DR STRING; 278856.A0A212EJS3; -.
DR KEGG; dpl:KGM_209838; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; A0A212EJS3; -.
DR Proteomes; UP000007151; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 1.25.50.20; -; 3.
DR Gene3D; 2.60.40.1910; -; 3.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 3.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 3.
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:SF291; AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 3.
DR Pfam; PF01433; Peptidase_M1; 3.
DR Pfam; PF17900; Peptidase_M1_N; 3.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 3.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:OWR41737.1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000007151};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2660
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013324336"
FT DOMAIN 54..241
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 277..505
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 583..884
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT DOMAIN 949..1143
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 1178..1390
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 1492..1788
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT DOMAIN 1843..1997
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 2119..2305
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 2396..2590
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 1255
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 1254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 1258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 1277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 1341
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 2660 AA; 306793 MW; 7C7BD5690ECAEE3B CRC64;
MALLYKLVLL PAMISLVKSD FPLDFDEPIY FSNIDEEIYR LPEDLDPVNI LLEITPYFED
PSASKAFTFE GFVLLTVKAV RDNISTLTLH ENVRDILSVN ITDESGITLA SSFKRIREQQ
FLEISLLNGT VLQKNQTCKI GISYIGNINE TPLSRGMFRG SYRDNQGRRR WYAGTHLQPT
NSRQLFPCFD EPGFKSTFDI IVNRPINFTE TFSNMRIKSQ SRVGDRQQEI FQTTPRMSAY
LVSIHISEEF EVIADNNNYN ASYRIIARPN ARGQGKYALE VGPPLTKWLD DYFNISYYTM
ANDIKNDQIA SPDWASGATE NWGLVSYREM RLLHEEGETN AVDKMTIGTI TAHELAHKWF
GNLITCRWWD NVWINEGFAS YFENFAMDGV DPSLELAEKF ITGTVQSALS SDSSASTRAL
RHTVNTPAQV TGHFSGISYT KGAAFLLMLK HLLGEPTFKK ALNYFLIERS YEQALPSDLY
SAFHRAVNED GIIENLNITA FMNYWVEERG YPILDVNINM DNGIMILKQE RFFISSSSTP
TDQVWPLPIT FTTSRNSNFD NLSPKTVMLN KTIQLRKDPG EEWVIFNLQQ KDFYRVNYDT
HTWELIAAAL KNNRNSIHRL NRAQIVDDVF ALMRSERLPF ELGFRILDFL KEETDYYPWT
PAITGFTWLR NRLLHLPEKL KEFDEILSSF LDTIVSDLGY DVHYDESITK TLNRFYILNF
ACNIGHVGCI NNALAKFNSL RSSGVPVNPN LRRHVFCQGV LHGGYDDWKF LQQRWFDSNN
QADQFAMLRS LGCTRNNEAV KEYLEMILSD DLRAQDSSNA FTFLFMGDRQ NTKYTLDFMK
ERWEEVRKKV VLQTWFGTVL SNLAAYSNEE VLEDMEQWLT TNQAIIPSAQ TGLSAINSAR
ANMKWGTEKA DDIVRGARAM IWQTLLAVAC IALQPVHSDT RYRLNTTIVP SAYSLTITPY
FDTNDDRAFS FDGEVSITFV TTSNINKIKL HSQDLIYTSA NITLKNGNNI IELNETNPLE
FEEDYTFAHI NLASDILVGS EYTLNIVYQG PIRTDLNGFY RNYYFQNGVK KWLGATQMEP
THARKVFPCF DEPELKAVFT MSIDRPAEYQ PSLTNTEIMS VTEMNNGYIR ENFYTTPRMS
TYLVAFLVSE FEAGSSNTLG ANELGIYTRP DAKNQTEYAF DVAQRIVKAL SDYFGIDYYS
TNNHLRLDHV ALTDFRAGAM ENWGLIKYRE SLLLYVPEES TPYFKYRVAQ IVAHETTHMW
FGNLVTCHWW SNTWLNEGFA NYFQDYMTSL VEPDVAADDA LVIGSVYSAY NADDNPDSPA
ITNNNVNSPS EISGHFGTIT YQKAGSVIRM MHHLIGDDAF KYGLNSYLST NQFQSGYPEL
LYSALENGVR NFTSLSNYEG FHFTDIMSSW IRQSGHPVLY VNVDYENSSI ELSQKRFYIN
SSYSSDELYI IPITYTLESN FNFENTKPAL IMDKKTHVLQ MSEIKEKQTF PIFNIQETGL
YRVNYDINTW HLISEHLKSN RSGDIHYLNR AKIVNDLFAF LFADEVKFEL LHNLLHFLSN
ENEYAVWNAA LKGLTKLRNY YIGSDTLDLI DEFALELLDG VIYRMGYDVK STDDFKILRN
RMQILEFACK LGHQGCIDRS LQWFKDLKNN DTWIQPSLRS VAYCTGLRYG NDEDYEFLWN
RLVNTNVANE AWIIADVLGC SQREDKLKSY LVSMLLENSP IKTQDLTVPL ASVLTNYSNV
PLVMDELQSN ISLWKSVYSS LGSVLSSIAS SLHTQEDFEK FESFLSSCKE CSEDEVASAK
NSLAKARAVT AWADDHRSDI LSSLISAYTI EEECLNYTVY PVQYELTIIP HIYLDGMSYY
DCDIVITIIA NAPNVNVIEL DAKDLEIKGE TVQVLDNGSN LVNKHRPYEY DAKKGKLYIY
LRESLKQYRL HRTQYNIRMS FSKQISYNTD GIFVVRYTEN GKPQHVLVTR LSPSRAKYFF
PCFDNSQFEA IFKFKVYEMP PYPGYQYCNT SIVIAKELKR HQSKDSYTIV EYLPSPQVAL
HQVGFHHSKF GSQRTTAKNT NDTLVIWAPV STLPQYTFIL HFGVIIINLI HEYSSIKRPL
VYGPINIISV PAILNGYEIG SWNLLTNGDN RLAIINDYTS IQQIEDMMFE LSQQLSRIWL
GNPGESQITR WREEWFKEGV ATYLAYYFLT QYNHGEAAAS YRRPISTYGL LMKHRAMARD
WHHSTPPLAS FNRTLAIDIP SRYKDLVTMK TASLLWMVEN WLGSEKFHQA LVNYINSRRE
QYISLTDFMA SVDRETVECL NQFFNGSTTS KVLNSWFHQS GYPVVNVQVL RDRTPNAIQL
KQRKFSFTDQ HRFDTNYLIP ISYIVQNNQN CFNCYRPRFT LDMQSYTFRE NLNDGWILLN
RNASGYYRVN YDVYTWGLIA KTLADDHLSI NELNRAQIVN DIFALYAAGD IHENVAISVL
NYLNSEFSFV VWESVVNGFE MLKIEGAKMT KVLYGEWQVF MQKKVATVYK RLMANVDQRP
WTRRFRKLIV DFACAVKYRR CLNEMRRFYS DHKNSNMKLN PDFREICYYV TINEGNYDIG
TALNRFEQEE KTVAEHKVRE ESRFLYQVPI GQPRPLPIMM STTTTTEIST TTIENTNNEG
ITLYISNVLL LAVIIKCLFQ
//
